(data stored in SCRATCH zone)

SWISSPROT: PP2BA_HUMAN

ID   PP2BA_HUMAN             Reviewed;         521 AA.
AC   Q08209; A1A441; A8K3B7; A8W6Z7; A8W6Z8; B5BUA2; Q8TAW9;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   11-DEC-2019, entry version 211.
DE   RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform;
DE            EC=3.1.3.16 {ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:19154138, ECO:0000269|PubMed:23468591, ECO:0000305|PubMed:26248042};
DE   AltName: Full=CAM-PRP catalytic subunit;
DE   AltName: Full=Calmodulin-dependent calcineurin A subunit alpha isoform;
GN   Name=PPP3CA {ECO:0000312|HGNC:HGNC:9314}; Synonyms=CALNA, CNA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=8392375; DOI=10.1016/0167-4889(93)90117-8;
RA   Muramatsu T., Kincaid R.L.;
RT   "Molecular cloning of a full-length cDNA encoding the catalytic subunit of
RT   human calmodulin-dependent protein phosphatase (calcineurin A alpha).";
RL   Biochim. Biophys. Acta 1178:117-120(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND ALTERNATIVE SPLICING.
RX   PubMed=20590401; DOI=10.3109/10826084.2010.482449;
RA   Chiocco M.J., Zhu X., Walther D., Pletnikova O., Troncoso J.C., Uhl G.R.,
RA   Liu Q.R.;
RT   "Fine mapping of calcineurin (PPP3CA) gene reveals novel alternative
RT   splicing patterns, association of 5'UTR trinucleotide repeat with addiction
RT   vulnerability, and differential isoform expression in Alzheimer's
RT   disease.";
RL   Subst. Use Misuse 45:1809-1826(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RX   PubMed=21647268;
RA   Landreville S., Lupien C.B., Vigneault F., Gaudreault M., Mathieu M.,
RA   Rousseau A.P., Guerin S.L., Salesse C.;
RT   "Identification of differentially expressed genes in uveal melanoma using
RT   suppressive subtractive hybridization.";
RL   Mol. Vis. 17:1324-1333(2011).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=19054851; DOI=10.1038/nmeth.1273;
RA   Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA   Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA   Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA   Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA   Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA   Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA   Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA   Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA   Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA   Nomura N.;
RT   "Human protein factory for converting the transcriptome into an in vitro-
RT   expressed proteome.";
RL   Nat. Methods 5:1011-1017(2008).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   INTERACTION WITH MYOZ1 AND MYOZ2.
RX   PubMed=11114196; DOI=10.1073/pnas.260501097;
RA   Frey N., Richardson J.A., Olson E.N.;
RT   "Calsarcins, a novel family of sarcomeric calcineurin-binding proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14632-14637(2000).
RN   [11]
RP   INTERACTION WITH MYOZ3.
RX   PubMed=11842093; DOI=10.1074/jbc.m200712200;
RA   Frey N., Olson E.N.;
RT   "Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin
RT   family, interacts with multiple Z-disc proteins.";
RL   J. Biol. Chem. 277:13998-14004(2002).
RN   [12]
RP   INTERACTION WITH RCAN1.
RX   PubMed=12809556; DOI=10.1042/bj20030267;
RA   Genesca L., Aubareda A., Fuentes J.J., Estivill X., De La Luna S.,
RA   Perez-Riba M.;
RT   "Phosphorylation of calcipressin 1 increases its ability to inhibit
RT   calcineurin and decreases calcipressin half-life.";
RL   Biochem. J. 374:567-575(2003).
RN   [13]
RP   INTERACTION WITH CRTC2.
RX   PubMed=15454081; DOI=10.1016/j.cell.2004.09.015;
RA   Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G.,
RA   Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H.,
RA   Okamoto M., Montminy M.;
RT   "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive
RT   coincidence detector.";
RL   Cell 119:61-74(2004).
RN   [14]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15671020; DOI=10.1074/jbc.m411494200;
RA   Wang Y., Shibasaki F., Mizuno K.;
RT   "Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot
RT   via calcineurin.";
RL   J. Biol. Chem. 280:12683-12689(2005).
RN   [15]
RP   INTERACTION WITH SYNPO2.
RX   PubMed=17923693; DOI=10.1128/mcb.00950-07;
RA   Faul C., Dhume A., Schecter A.D., Mundel P.;
RT   "Protein kinase A, Ca2+/calmodulin-dependent kinase II, and calcineurin
RT   regulate the intracellular trafficking of myopodin between the Z-disc and
RT   the nucleus of cardiac myocytes.";
RL   Mol. Cell. Biol. 27:8215-8227(2007).
RN   [16]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH DMN1L.
RX   PubMed=18838687; DOI=10.1073/pnas.0808249105;
RA   Cereghetti G.M., Stangherlin A., Martins de Brito O., Chang C.R.,
RA   Blackstone C., Bernardi P., Scorrano L.;
RT   "Dephosphorylation by calcineurin regulates translocation of Drp1 to
RT   mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15803-15808(2008).
RN   [17]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=19154138; DOI=10.1021/bi8019355;
RA   Kilka S., Erdmann F., Migdoll A., Fischer G., Weiwad M.;
RT   "The proline-rich N-terminal sequence of calcineurin Abeta determines
RT   substrate binding.";
RL   Biochemistry 48:1900-1910(2009).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [21]
RP   INVOLVEMENT IN IECEE1, AND VARIANTS IECEE1 ARG-92; GLN-281; LYS-282;
RP   445-GLN--GLN-521 DEL AND THR-447.
RX   PubMed=28942967; DOI=10.1016/j.ajhg.2017.08.013;
RA   Myers C.T., Stong N., Mountier E.I., Helbig K.L., Freytag S.,
RA   Sullivan J.E., Ben Zeev B., Nissenkorn A., Tzadok M., Heimer G.,
RA   Shinde D.N., Rezazadeh A., Regan B.M., Oliver K.L., Ernst M.E., Lippa N.C.,
RA   Mulhern M.S., Ren Z., Poduri A., Andrade D.M., Bird L.M., Bahlo M.,
RA   Berkovic S.F., Lowenstein D.H., Scheffer I.E., Sadleir L.G.,
RA   Goldstein D.B., Mefford H.C., Heinzen E.L.;
RT   "De Novo Mutations in PPP3CA Cause Severe Neurodevelopmental Disease with
RT   Seizures.";
RL   Am. J. Hum. Genet. 101:516-524(2017).
RN   [22]
RP   TISSUE SPECIFICITY.
RX   PubMed=29043977; DOI=10.7554/elife.27356;
RA   Mishra A., Oules B., Pisco A.O., Ly T., Liakath-Ali K., Walko G.,
RA   Viswanathan P., Tihy M., Nijjher J., Dunn S.J., Lamond A.I., Watt F.M.;
RT   "A protein phosphatase network controls the temporal and spatial dynamics
RT   of differentiation commitment in human epidermis.";
RL   Elife 6:0-0(2017).
RN   [23]
RP   FUNCTION, AND INTERACTION WITH CRTC1 AND CRTC2.
RX   PubMed=30611118; DOI=10.1016/j.isci.2018.12.012;
RA   Sonntag T., Ostojic J., Vaughan J.M., Moresco J.J., Yoon Y.S.,
RA   Yates J.R. III, Montminy M.;
RT   "Mitogenic Signals Stimulate the CREB Coactivator CRTC3 through PP2A
RT   Recruitment.";
RL   IScience 11:134-145(2018).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PPP3R1; IRON AND
RP   ZINC, AND ACTIVE SITE.
RX   PubMed=8524402; DOI=10.1038/378641a0;
RA   Kissinger C.R., Parge H.E., Knighton D.R., Lewis C.T., Pelletier L.A.,
RA   Tempczyk A., Kalish V.J., Tucker K.D., Showalter R.E., Moomaw E.W.,
RA   Gastinel L.N., Habuka N., Chen X., Maldonado F., Barker J.E., Bacquet R.,
RA   Villafranca J.E.;
RT   "Crystal structures of human calcineurin and the human FKBP12-FK506-
RT   calcineurin complex.";
RL   Nature 378:641-644(1995).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-372 IN COMPLEX WITH PPIA;
RP   PPP3R1; IRON AND ZINC.
RX   PubMed=12218175; DOI=10.1073/pnas.192206699;
RA   Huai Q., Kim H.Y., Liu Y., Zhao Y., Mondragon A., Liu J.O., Ke H.;
RT   "Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but
RT   distinct recognition of immunophilin-drug complexes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12037-12042(2002).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 20-392 IN COMPLEX WITH PPIA AND
RP   PPP3R1.
RX   PubMed=12357034; DOI=10.1073/pnas.212504399;
RA   Jin L., Harrison S.C.;
RT   "Crystal structure of human calcineurin complexed with cyclosporin A and
RT   human cyclophilin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13522-13526(2002).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-380 IN COMPLEX WITH SUBSTRATE
RP   PEPTIDE; PPP3R1; IRON AND ZINC, AND FUNCTION.
RX   PubMed=17498738; DOI=10.1016/j.jmb.2007.04.032;
RA   Li H., Zhang L., Rao A., Harrison S.C., Hogan P.G.;
RT   "Structure of calcineurin in complex with PVIVIT peptide: portrait of a
RT   low-affinity signalling interaction.";
RL   J. Mol. Biol. 369:1296-1306(2007).
RN   [28]
RP   STRUCTURE BY NMR OF 21-347 IN COMPLEX WITH PEPTIDE SUBSTRATE, AND FUNCTION.
RX   PubMed=17502104; DOI=10.1016/j.str.2007.03.015;
RA   Takeuchi K., Roehrl M.H., Sun Z.Y., Wagner G.;
RT   "Structure of the calcineurin-NFAT complex: defining a T cell activation
RT   switch using solution NMR and crystal coordinates.";
RL   Structure 15:587-597(2007).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 389-413 IN COMPLEX WITH CALM1.
RX   PubMed=18384083; DOI=10.1002/prot.22032;
RA   Ye Q., Wang H., Zheng J., Wei Q., Jia Z.;
RT   "The complex structure of calmodulin bound to a calcineurin peptide.";
RL   Proteins 73:19-27(2008).
RN   [30]
RP   STRUCTURE BY NMR OF 391-414 IN COMPLEX WITH CALM1.
RA   Chyan C., Huang J., Irene D., Lin T.;
RT   "Structure of Calmodulin complexed with the Calmodulin Binding Domain of
RT   Calcineurin.";
RL   Submitted (JAN-2008) to the PDB data bank.
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 395-411 IN COMPLEX WITH CALM1.
RX   PubMed=19404396; DOI=10.1371/journal.pone.0005402;
RA   Majava V., Kursula P.;
RT   "Domain swapping and different oligomeric States for the complex between
RT   calmodulin and the calmodulin-binding domain of calcineurin a.";
RL   PLoS ONE 4:E5402-E5402(2009).
RN   [32]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 14-370 IN COMPLEX WITH PPP3R1;
RP   AKAP5 PEPTIDE; IRON AND ZINC, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=22343722; DOI=10.1038/nsmb.2238;
RA   Li H., Pink M.D., Murphy J.G., Stein A., Dell'Acqua M.L., Hogan P.G.;
RT   "Balanced interactions of calcineurin with AKAP79 regulate Ca2+-
RT   calcineurin-NFAT signaling.";
RL   Nat. Struct. Mol. Biol. 19:337-345(2012).
RN   [33]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-370 IN COMPLEX WITH PPP3R1 AND
RP   AFRICAN SWINE FEVER VIRUS MAL-047/A238L, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=23468591; DOI=10.1371/journal.pbio.1001492;
RA   Grigoriu S., Bond R., Cossio P., Chen J.A., Ly N., Hummer G., Page R.,
RA   Cyert M.S., Peti W.;
RT   "The molecular mechanism of substrate engagement and immunosuppressant
RT   inhibition of calcineurin.";
RL   PLoS Biol. 11:E1001492-E1001492(2013).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 391-414 IN COMPLEX WITH CALM1.
RX   PubMed=25144868; DOI=10.1021/bi5004734;
RA   Dunlap T.B., Guo H.F., Cook E.C., Holbrook E., Rumi-Masante J.,
RA   Lester T.E., Colbert C.L., Vander Kooi C.W., Creamer T.P.;
RT   "Stoichiometry of the calcineurin regulatory domain-calmodulin complex.";
RL   Biochemistry 53:5779-5790(2014).
RN   [35]
RP   X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 2-346 IN COMPLEX WITH IRON AND
RP   ZINC, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH
RP   RCAN3 AND NFATC2, MOTIF, AND MUTAGENESIS OF TYR-288; TYR-341 AND
RP   328-VAL--ARG-332.
RX   PubMed=26248042; DOI=10.1371/journal.pone.0134569;
RA   Guasch A., Aranguren-Ibanez A., Perez-Luque R., Aparicio D.,
RA   Martinez-Hoyer S., Mulero M.C., Serrano-Candelas E., Perez-Riba M.,
RA   Fita I.;
RT   "Calcineurin Undergoes a Conformational Switch Evoked via Peptidyl-Prolyl
RT   Isomerization.";
RL   PLoS ONE 10:E0134569-E0134569(2015).
RN   [36]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-370 IN COMPLEX WITH PPP3R1;
RP   PEPTIDE SUBSTRATE; IRON AND ZINC, AND FUNCTION.
RX   PubMed=27974827; DOI=10.1038/srep38920;
RA   Sheftic S.R., Page R., Peti W.;
RT   "Investigating the human Calcineurin Interaction Network using the piLxVP
RT   SLiM.";
RL   Sci. Rep. 6:38920-38920(2016).
RN   [37]
RP   VARIANTS ACCIID LEU-470 AND THR-473, INVOLVEMENT IN ACCIID, AND VARIANTS
RP   IECEE1 ARG-92; ILE-150 AND GLU-234.
RX   PubMed=29432562; DOI=10.1093/hmg/ddy052;
RA   Mizuguchi T., Nakashima M., Kato M., Okamoto N., Kurahashi H.,
RA   Ekhilevitch N., Shiina M., Nishimura G., Shibata T., Matsuo M., Ikeda T.,
RA   Ogata K., Tsuchida N., Mitsuhashi S., Miyatake S., Takata A., Miyake N.,
RA   Hata K., Kaname T., Matsubara Y., Saitsu H., Matsumoto N.;
RT   "Loss-of-function and gain-of-function mutations in PPP3CA cause two
RT   distinct disorders.";
RL   Hum. Mol. Genet. 27:1421-1433(2018).
CC   -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase
CC       which plays an essential role in the transduction of intracellular
CC       Ca(2+)-mediated signals (PubMed:15671020, PubMed:18838687,
CC       PubMed:19154138, PubMed:23468591). Many of the substrates contain a
CC       PxIxIT motif and/or a LxVP motif (PubMed:17498738, PubMed:17502104,
CC       PubMed:23468591, PubMed:27974827, PubMed:22343722). In response to
CC       increased Ca(2+) levels, dephosphorylates and activates phosphatase
CC       SSH1 which results in cofilin dephosphorylation (PubMed:15671020). In
CC       response to increased Ca(2+) levels following mitochondrial
CC       depolarization, dephosphorylates DNM1L inducing DNM1L translocation to
CC       the mitochondrion (PubMed:18838687). Dephosphorylates heat shock
CC       protein HSPB1 (By similarity). Dephosphorylates and activates
CC       transcription factor NFATC1 (PubMed:19154138). In response to increased
CC       Ca(2+) levels, regulates NFAT-mediated transcription probably by
CC       dephosphorylating NFAT and promoting its nuclear translocation
CC       (PubMed:26248042). Dephosphorylates and inactivates transcription
CC       factor ELK1 (PubMed:19154138). Dephosphorylates DARPP32
CC       (PubMed:19154138). May dephosphorylate CRTC2 at 'Ser-171' resulting in
CC       CRTC2 dissociation from 14-3-3 proteins (PubMed:30611118).
CC       {ECO:0000250|UniProtKB:P48452, ECO:0000269|PubMed:15671020,
CC       ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:17502104,
CC       ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:19154138,
CC       ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591,
CC       ECO:0000269|PubMed:26248042, ECO:0000269|PubMed:27974827,
CC       ECO:0000269|PubMed:30611118}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:18838687,
CC         ECO:0000269|PubMed:19154138, ECO:0000269|PubMed:23468591,
CC         ECO:0000305|PubMed:26248042};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:18838687,
CC         ECO:0000269|PubMed:19154138, ECO:0000269|PubMed:23468591,
CC         ECO:0000305|PubMed:26248042};
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC         Evidence={ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:17498738,
CC         ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:26248042,
CC         ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402};
CC       Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000269|PubMed:12218175,
CC       ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
CC       ECO:0000269|PubMed:26248042, ECO:0000269|PubMed:27974827,
CC       ECO:0000269|PubMed:8524402};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:17498738,
CC         ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:26248042,
CC         ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12218175,
CC       ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
CC       ECO:0000269|PubMed:26248042, ECO:0000269|PubMed:27974827,
CC       ECO:0000269|PubMed:8524402};
CC   -!- ACTIVITY REGULATION: Activated by Ca(2+)-bound calmodulin following an
CC       increase in intracellular Ca(2+). At low Ca(2+) concentrations, the
CC       catalytic subunit (also known as calcineurin A) is inactive and is
CC       bound to the regulatory subunit (also known as calcineurin B) in which
CC       only two high-affinity binding sites are occupied by Ca(2+). In
CC       response to elevated calcium levels, the occupancy of the low-affinity
CC       sites on calcineurin B by Ca(2+) causes a conformational change of the
CC       C-terminal regulatory domain of calcineurin A, resulting in the
CC       exposure of the calmodulin-binding domain and in the partial activation
CC       of calcineurin A. The subsequent binding of Ca(2+)-bound calmodulin
CC       leads to the displacement of the autoinhibitory domain from the active
CC       site and possibly of the autoinhibitory segment from the substrate
CC       binding site which fully activates calcineurin A. Inhibited by
CC       immunosuppressant drug FK506 (tacrolimus) in complex with FKBP12 and
CC       also by immunosuppressant drug cyclosporin A (CsA) in complex with
CC       PPIA/cyclophilin A; the inhibition is Ca(2+)-dependent
CC       (PubMed:26248042). {ECO:0000250|UniProtKB:P16298,
CC       ECO:0000269|PubMed:26248042}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.04 uM for NFATC1 {ECO:0000269|PubMed:19154138};
CC         KM=2.22 uM for DARPP32 {ECO:0000269|PubMed:19154138};
CC   -!- SUBUNIT: Forms a complex composed of a calmodulin-dependent catalytic
CC       subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding
CC       subunit (also known as calcineurin B) (PubMed:8524402, PubMed:12218175,
CC       PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591,
CC       PubMed:27974827). There are three catalytic subunits, each encoded by a
CC       separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits
CC       which are also encoded by separate genes (PPP3R1 and PPP3R2). In
CC       response to an increase in Ca(2+) intracellular levels, forms a complex
CC       composed of PPP3CA/calcineurin A, calcineurin B and calmodulin (By
CC       similarity). Interacts (via calcineurin B binding domain) with
CC       regulatory subunit PPP3R1/calcineurin B (PubMed:8524402,
CC       PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722,
CC       PubMed:23468591, PubMed:27974827). Interacts (via calmodulin-binding
CC       domain) with CALM1/calmodulin; the interaction depends on calmodulin
CC       binding to Ca(2+) (PubMed:18384083, Ref.30, PubMed:19404396,
CC       PubMed:25144868). Forms a complex composed of MYOZ2 and ACTN1 (By
CC       similarity). Within the complex interacts with MYOZ2 (PubMed:11114196).
CC       Interacts with MYOZ1 (PubMed:11114196). Interacts with MYOZ3
CC       (PubMed:11842093). Interacts with CIB1; the interaction increases upon
CC       cardiomyocyte hypertrophy (By similarity). Interacts with CHP1 and CHP2
CC       (By similarity). Interacts with CRTC1 (PubMed:30611118). Interacts with
CC       CRTC2 (PubMed:15454081, PubMed:30611118). Interacts with DNM1L; the
CC       interaction dephosphorylates DNM1L and promotes its translocation to
CC       mitochondria (PubMed:18838687). Interacts with CMYA5; this interaction
CC       represses calcineurin activity in muscle (By similarity). Interacts
CC       (constitutively active form) with SYNPO2 (PubMed:17923693). Interacts
CC       with scaffold protein AKAP5 (via IAIIIT motif); the interaction
CC       recruits PPP3CA to the plasma membrane following L-type Ca(2+)-channel
CC       activation (PubMed:22343722). Interacts with NFATC2 (PubMed:26248042).
CC       Interacts with RCAN3 (PubMed:26248042). Interacts with PPIA
CC       (PubMed:12218175, PubMed:12357034). Interacts with RCAN1
CC       (PubMed:12809556). {ECO:0000250|UniProtKB:P48452,
CC       ECO:0000250|UniProtKB:P63328, ECO:0000250|UniProtKB:P63329,
CC       ECO:0000269|PubMed:11114196, ECO:0000269|PubMed:11842093,
CC       ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
CC       ECO:0000269|PubMed:12809556, ECO:0000269|PubMed:15454081,
CC       ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:17923693,
CC       ECO:0000269|PubMed:18384083, ECO:0000269|PubMed:18838687,
CC       ECO:0000269|PubMed:19404396, ECO:0000269|PubMed:22343722,
CC       ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:25144868,
CC       ECO:0000269|PubMed:26248042, ECO:0000269|PubMed:27974827,
CC       ECO:0000269|PubMed:30611118, ECO:0000269|PubMed:8524402,
CC       ECO:0000269|Ref.30}.
CC   -!- INTERACTION:
CC       O36972:A238L (xeno); NbExp=2; IntAct=EBI-15637215, EBI-16039701;
CC       P24588:AKAP5; NbExp=6; IntAct=EBI-15637215, EBI-703640;
CC       R4GN89:C16orf74; NbExp=3; IntAct=EBI-352922, EBI-10225238;
CC       Q8VHW5:Cacng8 (xeno); NbExp=2; IntAct=EBI-352922, EBI-9086576;
CC       P62993:GRB2; NbExp=3; IntAct=EBI-352922, EBI-401755;
CC       O95644:NFATC1; NbExp=4; IntAct=EBI-15637215, EBI-6907210;
CC       Q13469:NFATC2; NbExp=2; IntAct=EBI-15637215, EBI-716258;
CC       P63098:PPP3R1; NbExp=8; IntAct=EBI-11959013, EBI-915984;
CC       P54578:USP14; NbExp=3; IntAct=EBI-352922, EBI-1048016;
CC       P46939:UTRN; NbExp=3; IntAct=EBI-15637215, EBI-295856;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19154138,
CC       ECO:0000269|PubMed:22343722}. Cell membrane
CC       {ECO:0000269|PubMed:22343722}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:22343722}. Cell membrane, sarcolemma
CC       {ECO:0000250|UniProtKB:P63329}. Cytoplasm, myofibril, sarcomere, Z line
CC       {ECO:0000250|UniProtKB:P63329}. Cell projection, dendritic spine
CC       {ECO:0000269|PubMed:22343722}. Note=Colocalizes with ACTN1 and MYOZ2 at
CC       the Z line in heart and skeletal muscle (By similarity). Recruited to
CC       the cell membrane by scaffold protein AKAP5 following L-type Ca(2+)-
CC       channel activation (PubMed:22343722). {ECO:0000250|UniProtKB:P63329,
CC       ECO:0000269|PubMed:22343722}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q08209-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q08209-2; Sequence=VSP_018562;
CC       Name=3;
CC         IsoId=Q08209-3; Sequence=VSP_043378, VSP_018562;
CC       Name=4;
CC         IsoId=Q08209-4; Sequence=VSP_047755;
CC       Name=5;
CC         IsoId=Q08209-5; Sequence=VSP_054467;
CC   -!- TISSUE SPECIFICITY: Expressed in keratinocytes (at protein level).
CC       {ECO:0000269|PubMed:29043977}.
CC   -!- DOMAIN: The autoinhibitory domain prevents access to the catalytic
CC       site. {ECO:0000250|UniProtKB:P63328}.
CC   -!- DOMAIN: The autoinhibitory segment prevents access to the substrate
CC       binding site. {ECO:0000250|UniProtKB:P63328}.
CC   -!- DOMAIN: Possible isomerization of Pro-309 within the SAPNY motif
CC       triggers a conformation switch which affects the organization and thus
CC       accessibility of the active site and the substrate binding region
CC       (PxIxIF motif). The trans- to cis-transition may favor calcineurin A
CC       activation and substrate binding. The reverse cis- to trans-transition
CC       may be enhanced by peptidyl-prolyl isomerases such as PPIA.
CC       {ECO:0000269|PubMed:26248042}.
CC   -!- DISEASE: Epileptic encephalopathy, infantile or early childhood, 1
CC       (IECEE1) [MIM:617711]: A form of epileptic encephalopathy, a
CC       heterogeneous group of severe childhood onset epilepsies characterized
CC       by refractory seizures, neurodevelopmental impairment, and poor
CC       prognosis. Development is normal prior to seizure onset, after which
CC       cognitive and motor delays become apparent. IECEE1 is an autosomal
CC       dominant condition with onset of seizures between the first weeks and
CC       first years of life. {ECO:0000269|PubMed:28942967,
CC       ECO:0000269|PubMed:29432562}. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Arthrogryposis, cleft palate, craniosynostosis, and impaired
CC       intellectual development (ACCIID) [MIM:618265]: An autosomal dominant
CC       disease characterized by moderate to severe intellectual disability,
CC       craniosynostosis, cleft palate, micrognathia, arthrogryposis, and short
CC       stature. Some patients may present bone abnormalities and generalized
CC       seizures. {ECO:0000269|PubMed:29432562}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: Although African swine fever virus infects pigs and not
CC       humans, human PPP3CA has been used for the crystallization. PPP3CA
CC       interacts with African swine fever virus Mal-047/A238L (via PKIIIT and
CC       FLCVK motifs); the interaction does not block catalytic activity per se
CC       but inhibits PPP3CA function by blocking the access to the two
CC       substrate recognition sites. {ECO:0000269|PubMed:23468591}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Calcineurin entry;
CC       URL="https://en.wikipedia.org/wiki/Calcineurin";
DR   EMBL; L14778; AAA02631.1; -; mRNA.
DR   EMBL; EU192652; ABW74484.1; -; mRNA.
DR   EMBL; EU192653; ABW74485.1; -; mRNA.
DR   EMBL; AY904364; AAY17314.1; -; mRNA.
DR   EMBL; AK290532; BAF83221.1; -; mRNA.
DR   EMBL; AL353950; CAB89253.1; -; mRNA.
DR   EMBL; AB451338; BAG70152.1; -; mRNA.
DR   EMBL; AB451487; BAG70301.1; -; mRNA.
DR   EMBL; AC092671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471057; EAX06125.1; -; Genomic_DNA.
DR   EMBL; CH471057; EAX06124.1; -; Genomic_DNA.
DR   EMBL; BC025714; AAH25714.1; -; mRNA.
DR   CCDS; CCDS34037.1; -. [Q08209-1]
DR   CCDS; CCDS47113.1; -. [Q08209-3]
DR   CCDS; CCDS47114.1; -. [Q08209-2]
DR   PIR; S35067; S35067.
DR   RefSeq; NP_000935.1; NM_000944.4. [Q08209-1]
DR   RefSeq; NP_001124163.1; NM_001130691.1. [Q08209-2]
DR   RefSeq; NP_001124164.1; NM_001130692.1. [Q08209-3]
DR   PDB; 1AUI; X-ray; 2.10 A; A=1-521.
DR   PDB; 1M63; X-ray; 2.80 A; A/E=1-372.
DR   PDB; 1MF8; X-ray; 3.10 A; A=20-392.
DR   PDB; 2JOG; NMR; -; A=21-347.
DR   PDB; 2JZI; NMR; -; B=391-414.
DR   PDB; 2P6B; X-ray; 2.30 A; A/C=1-380.
DR   PDB; 2R28; X-ray; 1.86 A; C/D=389-413.
DR   PDB; 2W73; X-ray; 1.45 A; K/L/M/O=395-411.
DR   PDB; 3LL8; X-ray; 2.00 A; A/C=14-370.
DR   PDB; 4F0Z; X-ray; 1.70 A; A=1-370.
DR   PDB; 4Q5U; X-ray; 1.95 A; C=391-414.
DR   PDB; 5C1V; X-ray; 3.35 A; A/B=2-346.
DR   PDB; 5SVE; X-ray; 2.60 A; A=1-370.
DR   PDB; 6NUC; X-ray; 1.90 A; A=1-370.
DR   PDB; 6NUF; X-ray; 1.90 A; A=1-370.
DR   PDB; 6NUU; X-ray; 2.30 A; A=1-370.
DR   PDBsum; 1AUI; -.
DR   PDBsum; 1M63; -.
DR   PDBsum; 1MF8; -.
DR   PDBsum; 2JOG; -.
DR   PDBsum; 2JZI; -.
DR   PDBsum; 2P6B; -.
DR   PDBsum; 2R28; -.
DR   PDBsum; 2W73; -.
DR   PDBsum; 3LL8; -.
DR   PDBsum; 4F0Z; -.
DR   PDBsum; 4Q5U; -.
DR   PDBsum; 5C1V; -.
DR   PDBsum; 5SVE; -.
DR   PDBsum; 6NUC; -.
DR   PDBsum; 6NUF; -.
DR   PDBsum; 6NUU; -.
DR   SMR; Q08209; -.
DR   BioGrid; 111522; 75.
DR   ComplexPortal; CPX-1003; Calcineurin-Calmodulin complex, alpha-R1 variant.
DR   ComplexPortal; CPX-1048; Calcineurin-Calmodulin complex, alpha-R2 variant.
DR   ComplexPortal; CPX-1114; Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant.
DR   ComplexPortal; CPX-674; Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant.
DR   CORUM; Q08209; -.
DR   DIP; DIP-6095N; -.
DR   ELM; Q08209; -.
DR   IntAct; Q08209; 50.
DR   MINT; Q08209; -.
DR   STRING; 9606.ENSP00000378323; -.
DR   BindingDB; Q08209; -.
DR   ChEMBL; CHEMBL4445; -.
DR   DrugBank; DB08231; Myristic acid.
DR   DrugCentral; Q08209; -.
DR   DEPOD; Q08209; -.
DR   iPTMnet; Q08209; -.
DR   PhosphoSitePlus; Q08209; -.
DR   SwissPalm; Q08209; -.
DR   BioMuta; PPP3CA; -.
DR   DMDM; 1352673; -.
DR   EPD; Q08209; -.
DR   jPOST; Q08209; -.
DR   MassIVE; Q08209; -.
DR   MaxQB; Q08209; -.
DR   PaxDb; Q08209; -.
DR   PeptideAtlas; Q08209; -.
DR   PRIDE; Q08209; -.
DR   ProteomicsDB; 2488; -.
DR   ProteomicsDB; 58579; -. [Q08209-1]
DR   ProteomicsDB; 58580; -. [Q08209-2]
DR   ProteomicsDB; 58581; -. [Q08209-3]
DR   ProteomicsDB; 88; -.
DR   DNASU; 5530; -.
DR   Ensembl; ENST00000323055; ENSP00000320580; ENSG00000138814. [Q08209-3]
DR   Ensembl; ENST00000394853; ENSP00000378322; ENSG00000138814. [Q08209-2]
DR   Ensembl; ENST00000394854; ENSP00000378323; ENSG00000138814. [Q08209-1]
DR   Ensembl; ENST00000512215; ENSP00000422781; ENSG00000138814. [Q08209-4]
DR   GeneID; 5530; -.
DR   KEGG; hsa:5530; -.
DR   UCSC; uc003hvu.3; human. [Q08209-1]
DR   CTD; 5530; -.
DR   DisGeNET; 5530; -.
DR   EuPathDB; HostDB:ENSG00000138814.16; -.
DR   GeneCards; PPP3CA; -.
DR   HGNC; HGNC:9314; PPP3CA.
DR   HPA; CAB018581; -.
DR   HPA; HPA012778; -.
DR   MalaCards; PPP3CA; -.
DR   MIM; 114105; gene.
DR   MIM; 617711; phenotype.
DR   MIM; 618265; phenotype.
DR   neXtProt; NX_Q08209; -.
DR   OpenTargets; ENSG00000138814; -.
DR   Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR   Orphanet; 442835; Undetermined early-onset epileptic encephalopathy.
DR   PharmGKB; PA33678; -.
DR   eggNOG; KOG0375; Eukaryota.
DR   eggNOG; COG0639; LUCA.
DR   GeneTree; ENSGT00940000156306; -.
DR   HOGENOM; HOG000172699; -.
DR   InParanoid; Q08209; -.
DR   KO; K04348; -.
DR   OMA; LWSLKIW; -.
DR   OrthoDB; 463522at2759; -.
DR   PhylomeDB; Q08209; -.
DR   TreeFam; TF105557; -.
DR   Reactome; R-HSA-180024; DARPP-32 events.
DR   Reactome; R-HSA-2025928; Calcineurin activates NFAT.
DR   Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-HSA-4086398; Ca2+ pathway.
DR   Reactome; R-HSA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR   SIGNOR; Q08209; -.
DR   ChiTaRS; PPP3CA; human.
DR   EvolutionaryTrace; Q08209; -.
DR   GeneWiki; PPP3CA; -.
DR   GenomeRNAi; 5530; -.
DR   Pharos; Q08209; Tchem.
DR   PRO; PR:Q08209; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q08209; protein.
DR   Bgee; ENSG00000138814; Expressed in 244 organ(s), highest expression level in caudate nucleus.
DR   ExpressionAtlas; Q08209; baseline and differential.
DR   Genevisible; Q08209; HS.
DR   GO; GO:0005955; C:calcineurin complex; IDA:UniProtKB.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; IC:ARUK-UCL.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0036057; C:slit diaphragm; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR   GO; GO:0051117; F:ATPase binding; IPI:ARUK-UCL.
DR   GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR   GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0016018; F:cyclosporin A binding; IDA:UniProtKB.
DR   GO; GO:0008144; F:drug binding; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IDA:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; IPI:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:UniProtKB.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR   GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IDA:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR   GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
DR   GO; GO:0035690; P:cellular response to drug; IDA:UniProtKB.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:0016311; P:dephosphorylation; TAS:UniProtKB.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0033555; P:multicellular organismal response to stress; IEA:Ensembl.
DR   GO; GO:0035562; P:negative regulation of chromatin binding; IEA:Ensembl.
DR   GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IEA:Ensembl.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
DR   GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; IEA:Ensembl.
DR   GO; GO:0070262; P:peptidyl-serine dephosphorylation; IMP:UniProtKB.
DR   GO; GO:1903244; P:positive regulation of cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IMP:ARUK-UCL.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:ARUK-UCL.
DR   GO; GO:1905205; P:positive regulation of connective tissue replacement; IEA:Ensembl.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR   GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR   GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR   GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR   GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR   GO; GO:0043403; P:skeletal muscle tissue regeneration; TAS:BHF-UCL.
DR   GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
DR   GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
DR   GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
DR   CDD; cd07416; MPP_PP2B; 1.
DR   DisProt; DP00092; -.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041751; MPP_PP2B.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q08209.
DR   SWISS-2DPAGE; Q08209.
KW   3D-structure; Acetylation; Alternative splicing; Calmodulin-binding;
KW   Cell junction; Cell membrane; Cell projection; Craniosynostosis; Cytoplasm;
KW   Disease mutation; Dwarfism; Epilepsy; Hydrolase; Iron; Membrane;
KW   Mental retardation; Metal-binding; Nitration; Phosphoprotein;
KW   Protein phosphatase; Reference proteome; Synapse; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:22814378"
FT   CHAIN           2..521
FT                   /note="Serine/threonine-protein phosphatase 2B catalytic
FT                   subunit alpha isoform"
FT                   /id="PRO_0000058822"
FT   REGION          56..340
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000305"
FT   REGION          327..336
FT                   /note="Interaction with PxIxIF motif in substrate"
FT                   /evidence="ECO:0000269|PubMed:17498738,
FT                   ECO:0000269|PubMed:17502104, ECO:0000269|PubMed:22343722,
FT                   ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26248042"
FT   REGION          341..369
FT                   /note="Calcineurin B binding"
FT                   /evidence="ECO:0000269|PubMed:12218175,
FT                   ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738,
FT                   ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:27974827,
FT                   ECO:0000269|PubMed:8524402"
FT   REGION          392..406
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000269|PubMed:18384083,
FT                   ECO:0000269|PubMed:19404396, ECO:0000269|PubMed:25144868,
FT                   ECO:0000269|Ref.30"
FT   REGION          407..414
FT                   /note="Autoinhibitory segment"
FT                   /evidence="ECO:0000250|UniProtKB:P16298"
FT   REGION          465..487
FT                   /note="Autoinhibitory domain"
FT                   /evidence="ECO:0000269|PubMed:8524402"
FT   MOTIF           307..311
FT                   /note="SAPNY motif"
FT                   /evidence="ECO:0000305|PubMed:26248042"
FT   ACT_SITE        151
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:8524402"
FT   METAL           90
FT                   /note="Iron"
FT                   /evidence="ECO:0000244|PDB:1AUI, ECO:0000244|PDB:1M63,
FT                   ECO:0000244|PDB:2P6B, ECO:0000244|PDB:3LL8,
FT                   ECO:0000244|PDB:5C1V, ECO:0000244|PDB:5SVE,
FT                   ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:17498738,
FT                   ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:26248042,
FT                   ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402"
FT   METAL           92
FT                   /note="Iron; via tele nitrogen"
FT                   /evidence="ECO:0000244|PDB:1AUI, ECO:0000244|PDB:1M63,
FT                   ECO:0000244|PDB:2P6B, ECO:0000244|PDB:3LL8,
FT                   ECO:0000244|PDB:5C1V, ECO:0000244|PDB:5SVE,
FT                   ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:17498738,
FT                   ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:26248042,
FT                   ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402"
FT   METAL           118
FT                   /note="Iron"
FT                   /evidence="ECO:0000244|PDB:1AUI, ECO:0000244|PDB:1M63,
FT                   ECO:0000244|PDB:2P6B, ECO:0000244|PDB:3LL8,
FT                   ECO:0000244|PDB:5C1V, ECO:0000244|PDB:5SVE,
FT                   ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:17498738,
FT                   ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:26248042,
FT                   ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402"
FT   METAL           118
FT                   /note="Zinc"
FT                   /evidence="ECO:0000244|PDB:1AUI, ECO:0000244|PDB:1M63,
FT                   ECO:0000244|PDB:2P6B, ECO:0000244|PDB:3LL8,
FT                   ECO:0000244|PDB:5C1V, ECO:0000244|PDB:5SVE,
FT                   ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:17498738,
FT                   ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:26248042,
FT                   ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402"
FT   METAL           150
FT                   /note="Zinc"
FT                   /evidence="ECO:0000244|PDB:1AUI, ECO:0000244|PDB:1M63,
FT                   ECO:0000244|PDB:2P6B, ECO:0000244|PDB:3LL8,
FT                   ECO:0000244|PDB:5C1V, ECO:0000244|PDB:5SVE,
FT                   ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:17498738,
FT                   ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:26248042,
FT                   ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402"
FT   METAL           199
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000244|PDB:1AUI, ECO:0000244|PDB:1M63,
FT                   ECO:0000244|PDB:2P6B, ECO:0000244|PDB:3LL8,
FT                   ECO:0000244|PDB:5C1V, ECO:0000244|PDB:5SVE,
FT                   ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:17498738,
FT                   ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:26248042,
FT                   ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402"
FT   METAL           281
FT                   /note="Zinc; via pros nitrogen"
FT                   /evidence="ECO:0000244|PDB:1AUI, ECO:0000244|PDB:1M63,
FT                   ECO:0000244|PDB:2P6B, ECO:0000244|PDB:3LL8,
FT                   ECO:0000244|PDB:5C1V, ECO:0000244|PDB:5SVE,
FT                   ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:17498738,
FT                   ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:26248042,
FT                   ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402"
FT   SITE            352
FT                   /note="Interaction with PxVP motif in substrate"
FT                   /evidence="ECO:0000269|PubMed:23468591,
FT                   ECO:0000269|PubMed:27974827"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000244|PubMed:22814378"
FT   MOD_RES         224
FT                   /note="Nitrated tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P63328"
FT   MOD_RES         469
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P63329"
FT   MOD_RES         492
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   VAR_SEQ         20..86
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:21647268"
FT                   /id="VSP_054467"
FT   VAR_SEQ         87..318
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:20590401"
FT                   /id="VSP_047755"
FT   VAR_SEQ         318..359
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:20590401"
FT                   /id="VSP_043378"
FT   VAR_SEQ         448..457
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:20590401"
FT                   /id="VSP_018562"
FT   VARIANT         92
FT                   /note="H -> R (in IECEE1; dbSNP:rs1553925558)"
FT                   /evidence="ECO:0000269|PubMed:28942967,
FT                   ECO:0000269|PubMed:29432562"
FT                   /id="VAR_080348"
FT   VARIANT         150
FT                   /note="N -> I (in IECEE1)"
FT                   /evidence="ECO:0000269|PubMed:29432562"
FT                   /id="VAR_081900"
FT   VARIANT         234
FT                   /note="D -> E (in IECEE1)"
FT                   /evidence="ECO:0000269|PubMed:29432562"
FT                   /id="VAR_081901"
FT   VARIANT         281
FT                   /note="H -> Q (in IECEE1)"
FT                   /evidence="ECO:0000269|PubMed:28942967"
FT                   /id="VAR_080349"
FT   VARIANT         282
FT                   /note="E -> K (in IECEE1; dbSNP:rs1553923787)"
FT                   /evidence="ECO:0000269|PubMed:28942967"
FT                   /id="VAR_080350"
FT   VARIANT         445..521
FT                   /note="Missing (in IECEE1)"
FT                   /evidence="ECO:0000269|PubMed:28942967"
FT                   /id="VAR_080351"
FT   VARIANT         447
FT                   /note="A -> T (in IECEE1; unknown pathological
FT                   significance; dbSNP:rs1553920374)"
FT                   /evidence="ECO:0000269|PubMed:28942967"
FT                   /id="VAR_080352"
FT   VARIANT         470
FT                   /note="F -> L (in ACCIID)"
FT                   /evidence="ECO:0000269|PubMed:29432562"
FT                   /id="VAR_081902"
FT   VARIANT         473
FT                   /note="A -> T (in ACCIID)"
FT                   /evidence="ECO:0000269|PubMed:29432562"
FT                   /id="VAR_081903"
FT   MUTAGEN         288
FT                   /note="Y->F: Partial loss of Ca(2+)-mediated transcription
FT                   factor NFAT activation; when associated with F-341."
FT                   /evidence="ECO:0000269|PubMed:26248042"
FT   MUTAGEN         288
FT                   /note="Y->N,A: Loss of Ca(2+)-mediated transcription factor
FT                   NFAT activation; when associated with F-341."
FT                   /evidence="ECO:0000269|PubMed:26248042"
FT   MUTAGEN         328..332
FT                   /note="Missing: Loss of Ca(2+)-mediated transcription
FT                   factor NFAT activation; when associated with F-341."
FT                   /evidence="ECO:0000269|PubMed:26248042"
FT   MUTAGEN         341
FT                   /note="Y->F: Resistant to cyclosporin A-mediated
FT                   inhibition. Loss of Ca(2+)-mediated transcription factor
FT                   NFAT activation; when associated with N-288, A-228 or 328-
FT                   V--R-332 DEL. Partial loss in Ca(2+)-mediated transcription
FT                   factor NFAT activation; when associated with F-288."
FT                   /evidence="ECO:0000269|PubMed:26248042"
FT   STRAND          13..15
FT                   /evidence="ECO:0000244|PDB:6NUC"
FT   HELIX           31..34
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   HELIX           43..51
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   HELIX           58..73
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          77..81
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          83..88
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   HELIX           95..105
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   TURN            108..110
FT                   /evidence="ECO:0000244|PDB:6NUC"
FT   STRAND          113..115
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          120..123
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   HELIX           126..139
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   TURN            141..143
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          144..146
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   HELIX           154..159
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   HELIX           162..169
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   HELIX           172..183
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          188..191
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   TURN            192..194
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          195..200
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          206..208
FT                   /evidence="ECO:0000244|PDB:2JOG"
FT   HELIX           210..213
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          218..220
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          223..225
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   HELIX           226..232
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   TURN            237..240
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          247..250
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   TURN            252..254
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          255..260
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   HELIX           262..271
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          276..279
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          287..290
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   TURN            295..297
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          298..306
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   HELIX           311..313
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          319..325
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   STRAND          328..334
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   HELIX           344..346
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   HELIX           349..369
FT                   /evidence="ECO:0000244|PDB:4F0Z"
FT   HELIX           396..409
FT                   /evidence="ECO:0000244|PDB:2W73"
FT   HELIX           470..477
FT                   /evidence="ECO:0000244|PDB:1AUI"
FT   HELIX           478..481
FT                   /evidence="ECO:0000244|PDB:1AUI"
SQ   SEQUENCE   521 AA;  58688 MW;  16480D62DDBF1F40 CRC64;
     MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL MKEGRLEESV
     ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK LFEVGGSPAN TRYLFLGDYV
     DRGYFSIECV LYLWALKILY PKTLFLLRGN HECRHLTEYF TFKQECKIKY SERVYDACMD
     AFDCLPLAAL MNQQFLCVHG GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG
     NEKTQEHFTH NTVRGCSYFY SYPAVCEFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP
     SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK
     VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI RAIGKMARVF SVLREESESV
     LTLKGLTPTG MLPSGVLSGG KQTLQSATVE AIEADEAIKG FSPQHKITSF EEAKGLDRIN
     ERMPPRRDAM PSDANLNSIN KALTSETNGT DSNGSNSSNI Q
//

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