(data stored in ACNUC27125 zone)

SWISSPROT: PP2BC_MOUSE

ID   PP2BC_MOUSE             Reviewed;         513 AA.
AC   P48455; Q3V074;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   11-DEC-2019, entry version 145.
DE   RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform;
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:P48454};
DE   AltName: Full=CAM-PRP catalytic subunit;
DE   AltName: Full=Calcineurin, testis-specific catalytic subunit;
DE   AltName: Full=Calmodulin-dependent calcineurin A subunit gamma isoform;
GN   Name=Ppp3cc; Synonyms=Calnc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=1309945; DOI=10.1073/pnas.89.2.529;
RA   Muramatsu T., Giri P.R., Higuchi S., Kincaid R.L.;
RT   "Molecular cloning of a calmodulin-dependent phosphatase from murine
RT   testis: identification of a developmentally expressed nonneural
RT   isoenzyme.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:529-533(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE21630.1};
RC   TISSUE=Testis {ECO:0000312|EMBL:BAE21630.1};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:AAI41080.1};
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase
CC       which plays an essential role in the transduction of intracellular
CC       Ca(2+)-mediated signals. Dephosphorylates and activates transcription
CC       factor NFATC1. Dephosphorylates and inactivates transcription factor
CC       ELK1. Dephosphorylates DARPP32. {ECO:0000250|UniProtKB:P48454}.
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:0000250|UniProtKB:P48454};
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:0000250|UniProtKB:P48454};
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC         Evidence={ECO:0000250|UniProtKB:P16298};
CC       Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250|UniProtKB:P16298};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P16298};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P16298};
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.
CC       {ECO:0000250|UniProtKB:P16298}.
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). There are three catalytic
CC       subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC)
CC       and two regulatory subunits which are also encoded by separate genes
CC       (PPP3R1 and PPP3R2). In response to an increase in Ca(2+) intracellular
CC       levels, forms a complex composed of PPP3CC/calcineurin A, calcineurin B
CC       and calmodulin. Interacts (via calmodulin-binding domain) with
CC       calmodulin; the interaction depends on calmodulin binding to Ca(2+).
CC       {ECO:0000250|UniProtKB:P16298, ECO:0000250|UniProtKB:P48454}.
CC   -!- TISSUE SPECIFICITY: Testis.
CC   -!- DOMAIN: The autoinhibitory domain prevents access to the catalytic
CC       site. {ECO:0000250|UniProtKB:P16298}.
CC   -!- DOMAIN: The autoinhibitory segment prevents access to the substrate
CC       binding site. {ECO:0000250|UniProtKB:P16298}.
CC   -!- DOMAIN: Possible isomerization of Pro-305 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:0000250|UniProtKB:Q08209}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC       {ECO:0000305}.
DR   EMBL; M81475; AAA39968.1; -; mRNA.
DR   EMBL; AK133393; BAE21630.1; -; mRNA.
DR   EMBL; CH466535; EDL35914.1; -; Genomic_DNA.
DR   EMBL; BC141079; AAI41080.1; -; mRNA.
DR   CCDS; CCDS36968.1; -.
DR   PIR; A38193; A38193.
DR   RefSeq; NP_032941.1; NM_008915.3.
DR   BioGrid; 202346; 3.
DR   ComplexPortal; CPX-1007; Calcineurin-Calmodulin complex, gamma-R1 variant.
DR   ComplexPortal; CPX-1051; Calcineurin-Calmodulin complex, gamma-R2 variant.
DR   ComplexPortal; CPX-1113; Calcineurin-Calmodulin-AKAP5 complex, gamma-R1 variant.
DR   ComplexPortal; CPX-1119; Calcineurin-Calmodulin-AKAP5 complex, gamma-R2 variant.
DR   IntAct; P48455; 1.
DR   STRING; 10090.ENSMUSP00000077532; -.
DR   iPTMnet; P48455; -.
DR   PhosphoSitePlus; P48455; -.
DR   EPD; P48455; -.
DR   PaxDb; P48455; -.
DR   PeptideAtlas; P48455; -.
DR   PRIDE; P48455; -.
DR   Ensembl; ENSMUST00000078434; ENSMUSP00000077532; ENSMUSG00000022092.
DR   GeneID; 19057; -.
DR   KEGG; mmu:19057; -.
DR   UCSC; uc007unp.2; mouse.
DR   CTD; 5533; -.
DR   MGI; MGI:107162; Ppp3cc.
DR   eggNOG; KOG0375; Eukaryota.
DR   eggNOG; COG0639; LUCA.
DR   GeneTree; ENSGT00940000154115; -.
DR   InParanoid; P48455; -.
DR   KO; K04348; -.
DR   OrthoDB; 463522at2759; -.
DR   PhylomeDB; P48455; -.
DR   TreeFam; TF105557; -.
DR   Reactome; R-MMU-111447; Activation of BAD and translocation to mitochondria.
DR   ChiTaRS; Ppp3cc; mouse.
DR   PRO; PR:P48455; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; P48455; protein.
DR   Bgee; ENSMUSG00000022092; Expressed in 243 organ(s), highest expression level in testis.
DR   ExpressionAtlas; P48455; baseline and differential.
DR   Genevisible; P48455; MM.
DR   GO; GO:0005955; C:calcineurin complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0098793; C:presynapse; ISO:MGI.
DR   GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR   GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR   GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; ISO:MGI.
DR   GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISO:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR   GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:MGI.
DR   CDD; cd07416; MPP_PP2B; 1.
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; P48455.
DR   SWISS-2DPAGE; P48455.
KW   Calmodulin-binding; Hydrolase; Iron; Metal-binding; Protein phosphatase;
KW   Reference proteome; Zinc.
FT   CHAIN           1..513
FT                   /note="Serine/threonine-protein phosphatase 2B catalytic
FT                   subunit gamma isoform"
FT                   /id="PRO_0000058829"
FT   REGION          52..343
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000305"
FT   REGION          344..366
FT                   /note="Calcineurin B binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16298"
FT   REGION          385..399
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16298"
FT   REGION          400..407
FT                   /note="Autoinhibitory segment"
FT                   /evidence="ECO:0000250|UniProtKB:P16298"
FT   REGION          458..480
FT                   /note="Autoinhibitory domain"
FT                   /evidence="ECO:0000250|UniProtKB:P16298"
FT   MOTIF           303..307
FT                   /note="SAPNY motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q08209"
FT   ACT_SITE        147
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q08209"
FT   METAL           86
FT                   /note="Iron"
FT                   /evidence="ECO:0000250|UniProtKB:P16298"
FT   METAL           88
FT                   /note="Iron; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P16298"
FT   METAL           114
FT                   /note="Iron"
FT                   /evidence="ECO:0000250|UniProtKB:P16298"
FT   METAL           114
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:P16298"
FT   METAL           146
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:P16298"
FT   METAL           195
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P16298"
FT   METAL           277
FT                   /note="Zinc; via pros nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P16298"
SQ   SEQUENCE   513 AA;  58699 MW;  521CB2B1DD9E03A0 CRC64;
     MSVRRPQFST TERVIKAVPF PPTRRLTLKE VFENGKPKMD LLKNHLVKEG RVEEEVALKI
     INDGAAILKQ EKTMIEVEAP ITVCGDVHGQ FFDLMKLFEV GGSPSNTRYL FLGDYVDRGY
     FSIECVLYLW SLKINHPKTL FLLRGNHECR HLTEYFTFKQ ECRIKYSEMV YDACMHTFDC
     LPLAALLNQQ FLCVHGGMSP EITCLEDIRK LDRFSEPPAF GPVCDLLWSD PLEDYGSEKT
     LEHYTHNTVR GCSYFFSYPA VCEFLQNNSL LSIIRAHEAQ DAGYRMYRKN QATGFPSLIT
     IFSAPNYLDV YNNKAAVLKY ENNVMNIRQF NCSPHPYWLP NFMDVFTWSL PFVGEKVTEM
     LVNILNICSD EEMNVTDEEG ATTGRKEVIK NKIRAIGKMA RVFTVLREES ENVLTLKGLT
     PTGTLPLGVL SGGKQTIETA KQEAAEEREA IRGFTIAHRI RSFEEARGLD RINERMPPRK
     EASYHHDAGR MHSHSHPPHP QASRRTDHGK KAL
//

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