(data stored in SCRATCH zone)

SWISSPROT: CNBL3_ARATH

ID   CNBL3_ARATH             Reviewed;         226 AA.
AC   Q8LEM7; O81447;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   11-DEC-2019, entry version 131.
DE   RecName: Full=Calcineurin B-like protein 3;
DE   AltName: Full=SOS3-like calcium-binding protein 6;
GN   Name=CBL3; Synonyms=SCABP6; OrderedLocusNames=At4g26570;
GN   ORFNames=T15N24.20;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=10200328; DOI=10.1073/pnas.96.8.4718;
RA   Kudla J., Xu Q., Harter K., Gruissem W., Luan S.;
RT   "Genes for calcineurin B-like proteins in Arabidopsis are differentially
RT   regulated by stress signals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:4718-4723(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INTERACTION WITH CIPK1; CIPK2; CIPK3 AND CIPK6.
RX   PubMed=10590166; DOI=10.1105/tpc.11.12.2393;
RA   Shi J., Kim K.-N., Ritz O., Albrecht V., Gupta R., Harter K., Luan S.,
RA   Kudla J.;
RT   "Novel protein kinases associated with calcineurin B-like calcium sensors
RT   in Arabidopsis.";
RL   Plant Cell 11:2393-2405(1999).
RN   [7]
RP   INTERACTION WITH CIPK1; CIPK2; CIPK4; CIPK6; CIPK7; CIPK11; CIPK12 AND
RP   CIPK13.
RX   PubMed=11230129; DOI=10.1093/emboj/20.5.1051;
RA   Albrecht V., Ritz O., Linder S., Harter K., Kudla J.;
RT   "The NAF domain defines a novel protein-protein interaction module
RT   conserved in Ca(2+)-regulated kinases.";
RL   EMBO J. 20:1051-1063(2001).
RN   [8]
RP   GENE FAMILY.
RX   PubMed=14730064; DOI=10.1104/pp.103.033068;
RA   Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.;
RT   "Calcium sensors and their interacting protein kinases: genomics of the
RT   Arabidopsis and rice CBL-CIPK signaling networks.";
RL   Plant Physiol. 134:43-58(2004).
RN   [9]
RP   INTERACTION WITH CIPK23.
RX   PubMed=16814720; DOI=10.1016/j.cell.2006.06.011;
RA   Xu J., Li H.-D., Chen L.-Q., Wang Y., Liu L.-L., He L., Wu W.-H.;
RT   "A protein kinase, interacting with two calcineurin B-like proteins,
RT   regulates K+ transporter AKT1 in Arabidopsis.";
RL   Cell 125:1347-1360(2006).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH CIPK6; CIPK16 AND CIPK23.
RX   PubMed=17898163; DOI=10.1073/pnas.0707912104;
RA   Lee S.-C., Lan W.-Z., Kim B.-G., Li L., Cheong Y.H., Pandey G.K., Lu G.,
RA   Buchanan B.B., Luan S.;
RT   "A protein phosphorylation/dephosphorylation network regulates a plant
RT   potassium channel.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:15959-15964(2007).
RN   [11]
RP   INTERACTION WITH MTN1, AND DOMAIN.
RX   PubMed=18945934; DOI=10.1104/pp.108.130419;
RA   Oh S.I., Park J., Yoon S., Kim Y., Park S., Ryu M., Nam M.J., Ok S.H.,
RA   Kim J.K., Shin J.S., Kim K.N.;
RT   "The Arabidopsis calcium sensor calcineurin B-like 3 inhibits the 5'-
RT   methylthioadenosine nucleosidase in a calcium-dependent manner.";
RL   Plant Physiol. 148:1883-1896(2008).
RN   [12]
RP   SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH CIPK14.
RX   PubMed=19832944; DOI=10.1111/j.1365-313x.2009.04045.x;
RA   Batistic O., Waadt R., Steinhorst L., Held K., Kudla J.;
RT   "CBL-mediated targeting of CIPKs facilitates the decoding of calcium
RT   signals emanating from distinct cellular stores.";
RL   Plant J. 61:211-222(2010).
RN   [13]
RP   INTERACTION WITH PP2CA.
RX   PubMed=21596690; DOI=10.1093/mp/ssr031;
RA   Lan W.Z., Lee S.C., Che Y.F., Jiang Y.Q., Luan S.;
RT   "Mechanistic analysis of AKT1 regulation by the CBL-CIPK-PP2CA
RT   interactions.";
RL   Mol. Plant 4:527-536(2011).
RN   [14]
RP   DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP   CALCIUM-BINDING, AND DISRUPTION PHENOTYPE.
RX   PubMed=23184060; DOI=10.1038/cr.2012.161;
RA   Tang R.J., Liu H., Yang Y., Yang L., Gao X.S., Garcia V.J., Luan S.,
RA   Zhang H.X.;
RT   "Tonoplast calcium sensors CBL2 and CBL3 control plant growth and ion
RT   homeostasis through regulating V-ATPase activity in Arabidopsis.";
RL   Cell Res. 22:1650-1665(2012).
RN   [15]
RP   SUBCELLULAR LOCATION, AND PALMITOYLATION.
RX   PubMed=23482856; DOI=10.1105/tpc.112.108829;
RA   Zhou L.Z., Li S., Feng Q.N., Zhang Y.L., Zhao X., Zeng Y.L., Wang H.,
RA   Jiang L., Zhang Y.;
RT   "Protein S-acyl transferase10 is critical for development and salt
RT   tolerance in Arabidopsis.";
RL   Plant Cell 25:1093-1107(2013).
RN   [16]
RP   FUNCTION, INTERACTION WITH CIPK9, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=23109687; DOI=10.1104/pp.112.206896;
RA   Liu L.L., Ren H.M., Chen L.Q., Wang Y., Wu W.H.;
RT   "A protein kinase, calcineurin B-like protein-interacting protein Kinase9,
RT   interacts with calcium sensor calcineurin B-like Protein3 and regulates
RT   potassium homeostasis under low-potassium stress in Arabidopsis.";
RL   Plant Physiol. 161:266-277(2013).
RN   [17]
RP   INTERACTION WITH CIPK14.
RX   PubMed=25058458; DOI=10.1016/j.bbrc.2014.07.064;
RA   Yan J., Niu F., Liu W.Z., Zhang H., Wang B., Lan W., Che Y., Yang B.,
RA   Luan S., Jiang Y.Q.;
RT   "Arabidopsis CIPK14 positively regulates glucose response.";
RL   Biochem. Biophys. Res. Commun. 450:1679-1683(2014).
CC   -!- FUNCTION: Acts as a calcium sensor. CBL proteins interact with CIPK
CC       serine-threonine protein kinases. Binds calcium ions. Binding of a CBL
CC       protein to the regulatory NAF domain of a CIPK protein lead to the
CC       activation of the kinase in a calcium-dependent manner. Mediates the
CC       activation of AKT1 by CIPK proteins (CIPK6, CIPK16, and CIPK23) in
CC       response to low potassium conditions and in the context of stomatal
CC       movement. Negatively regulates the enzyme activity of MTN1 in the
CC       presence of calcium. {ECO:0000269|PubMed:17898163,
CC       ECO:0000269|PubMed:23109687}.
CC   -!- SUBUNIT: Homodimer (By similarity). Part of a K(+)-channel calcium-
CC       sensing kinase/phosphatase complex composed by a calcium sensor CBL
CC       (CBL1, CBL2, CBL3 or CBL9), a kinase CIPK (CIPK6, CIPK16 or CIPK23), a
CC       phosphatase PP2C (AIP1) and a K(+)-channel (AKT1). Interacts with
CC       PP2CA, CIPK1, CIPK2, CIPK3, CIPK4, CIPK6, CIPK7, CIPK11, CIPK12,
CC       CIPK13, CIPK14, CIPK16, CIPK23, and MTN1. {ECO:0000250,
CC       ECO:0000269|PubMed:10590166, ECO:0000269|PubMed:11230129,
CC       ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:17898163,
CC       ECO:0000269|PubMed:18945934, ECO:0000269|PubMed:19832944,
CC       ECO:0000269|PubMed:21596690, ECO:0000269|PubMed:23109687,
CC       ECO:0000269|PubMed:25058458}.
CC   -!- INTERACTION:
CC       Q8RWC9:CIPK1; NbExp=4; IntAct=EBI-637358, EBI-1748677;
CC       O65554:CIPK6; NbExp=4; IntAct=EBI-637358, EBI-537615;
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:19832944,
CC       ECO:0000269|PubMed:23109687, ECO:0000269|PubMed:23184060,
CC       ECO:0000269|PubMed:23482856}; Lipid-anchor
CC       {ECO:0000269|PubMed:19832944, ECO:0000269|PubMed:23109687,
CC       ECO:0000269|PubMed:23184060, ECO:0000269|PubMed:23482856}.
CC       Note=Tonoplast localization abolished by 2-bromopalmitate (2-BP)
CC       treatment.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8LEM7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8LEM7-2; Sequence=VSP_012328;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Stronger expression in roots. Expressed
CC       in root tip and root hair zone, leaf veins, vascular bundles and
CC       vasculature of sepals. {ECO:0000269|PubMed:10200328,
CC       ECO:0000269|PubMed:23109687, ECO:0000269|PubMed:23184060}.
CC   -!- DEVELOPMENTAL STAGE: Expressed early during germination and increases
CC       to a peak level when seedlings are established.
CC       {ECO:0000269|PubMed:23184060}.
CC   -!- DOMAIN: The N-terminal 22 amino acids are sufficient for vacuolar
CC       membrane targeting. The internal domain (109-199) is sufficient for the
CC       interaction with MTN1. {ECO:0000269|PubMed:18945934,
CC       ECO:0000269|PubMed:19832944}.
CC   -!- PTM: S-acylated by PAT10.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC       conditions; due to partial redundancy with CLB2. Tolerant to low-K(+)
CC       stress. Clb2 and cbl3 double mutants show stunted growth, reduced
CC       fertility and necrotic lesions at leaf tips. They also have a reduced
CC       vacuolar H(+)-ATPase activity, are hypersensitive to excessive metal
CC       ions and are more tolerant to low-K(+) conditions.
CC       {ECO:0000269|PubMed:23109687, ECO:0000269|PubMed:23184060}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC       site. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC       {ECO:0000305}.
DR   EMBL; AF076253; AAC26010.1; -; mRNA.
DR   EMBL; AL078465; CAB43853.1; -; Genomic_DNA.
DR   EMBL; AL161565; CAB79512.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85220.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85221.1; -; Genomic_DNA.
DR   EMBL; AY072441; AAL62433.1; -; mRNA.
DR   EMBL; AY128880; AAM91280.1; -; mRNA.
DR   EMBL; AY085344; AAM62575.1; -; mRNA.
DR   PIR; T08923; T08923.
DR   RefSeq; NP_001320073.1; NM_001341813.1. [Q8LEM7-2]
DR   RefSeq; NP_194387.1; NM_118791.4. [Q8LEM7-1]
DR   SMR; Q8LEM7; -.
DR   BioGrid; 14051; 20.
DR   DIP; DIP-33307N; -.
DR   IntAct; Q8LEM7; 16.
DR   STRING; 3702.AT4G26570.2; -.
DR   iPTMnet; Q8LEM7; -.
DR   SwissPalm; Q8LEM7; -.
DR   PaxDb; Q8LEM7; -.
DR   PRIDE; Q8LEM7; -.
DR   EnsemblPlants; AT4G26570.1; AT4G26570.1; AT4G26570. [Q8LEM7-1]
DR   EnsemblPlants; AT4G26570.2; AT4G26570.2; AT4G26570. [Q8LEM7-2]
DR   GeneID; 828764; -.
DR   Gramene; AT4G26570.1; AT4G26570.1; AT4G26570. [Q8LEM7-1]
DR   Gramene; AT4G26570.2; AT4G26570.2; AT4G26570. [Q8LEM7-2]
DR   KEGG; ath:AT4G26570; -.
DR   Araport; AT4G26570; -.
DR   TAIR; locus:2133867; AT4G26570.
DR   eggNOG; KOG0034; Eukaryota.
DR   eggNOG; COG5126; LUCA.
DR   HOGENOM; HOG000233019; -.
DR   InParanoid; Q8LEM7; -.
DR   KO; K06268; -.
DR   OMA; ECPDGVV; -.
DR   OrthoDB; 1271942at2759; -.
DR   PhylomeDB; Q8LEM7; -.
DR   PRO; PR:Q8LEM7; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8LEM7; baseline and differential.
DR   Genevisible; Q8LEM7; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR   GO; GO:0005773; C:vacuole; IDA:TAIR.
DR   GO; GO:0005509; F:calcium ion binding; ISS:TAIR.
DR   GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR   GO; GO:0005513; P:detection of calcium ion; ISS:TAIR.
DR   GO; GO:0055075; P:potassium ion homeostasis; IMP:TAIR.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   1: Evidence at protein level;
DR   PRODOM; Q8LEM7.
DR   SWISS-2DPAGE; Q8LEM7.
KW   Alternative splicing; Calcium; Lipoprotein; Membrane; Metal-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Vacuole.
FT   CHAIN           1..226
FT                   /note="Calcineurin B-like protein 3"
FT                   /id="PRO_0000073504"
FT   DOMAIN          36..81
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          82..117
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          119..154
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          163..198
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CA_BIND         58..71
FT                   /note="1; atypical"
FT   CA_BIND         95..106
FT                   /note="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CA_BIND         132..143
FT                   /note="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CA_BIND         176..187
FT                   /note="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   SITE            155
FT                   /note="Involved in dimerization"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LAS7"
FT   VAR_SEQ         89
FT                   /note="R -> RYQSQ (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_012328"
SQ   SEQUENCE   226 AA;  26032 MW;  F78222E98F64983E CRC64;
     MSQCIDGFKH VCSSFFRCFD IDIYKQSGGL GDPELLARET VFSVSEIEAL YELFKKISSA
     VIDDGLINKE EFQLALFKTN KKESLFADRV FDLFDTKHNG ILGFEEFARA LSVFHPNAPI
     EDKIDFSFQL YDLKQQGFIE RQEVKQMVVA TLAESGMNLS DEIIESIIDK TFEEADTKHD
     GRIDKEEWRT LVLRHPSLLK NMTLQYLKDI TTTFPSFVFH SQVEDT
//

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