SORCN_HUMAN
ID SORCN_HUMAN Reviewed; 198 AA.
AC P30626; A8MTH6; B4DKK2; D6W5Q0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Sorcin;
DE AltName: Full=22 kDa protein;
DE AltName: Full=CP-22;
DE Short=CP22;
DE AltName: Full=V19;
GN Name=SRI;
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).
RX PubMed=7873602; DOI=10.1016/0167-4781(94)00206-i;
RA Wang S.L., Tam M.F., Ho Y.S., Pai S.H., Kao M.C.;
RT "Isolation and molecular cloning of human sorcin a calcium-binding protein
RT in vincristine-resistant HOB1 lymphoma cells.";
RL Biochim. Biophys. Acta 1260:285-293(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8561500; DOI=10.1006/abbi.1996.0027;
RA Lee W.P.;
RT "Purification, cDNA cloning, and expression of human sorcin in vincristine-
RT resistant HOB1 lymphoma cell lines.";
RL Arch. Biochem. Biophys. 325:217-226(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Sugimoto Y., Asami N., Okochi E., Ogura M., Tsuruo T.;
RT "Isolation of the cDNA clone for human CP22 overexpressed in multidrug-
RT resistant cell lines.";
RL Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Colon;
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 2).
RC TISSUE=Ascites;
RX PubMed=16341674; DOI=10.1007/s00335-005-0075-2;
RA Oh J.H., Yang J.O., Hahn Y., Kim M.R., Byun S.S., Jeon Y.J., Kim J.M.,
RA Song K.S., Noh S.M., Kim S., Yoo H.S., Kim Y.S., Kim N.S.;
RT "Transcriptome analysis of human gastric cancer.";
RL Mamm. Genome 16:942-954(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [9]
RP PROTEIN SEQUENCE OF 57-116; 128-135 AND 154-165, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 128-135 AND 154-165.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [11]
RP INTERACTION WITH GCA.
RX PubMed=12804766; DOI=10.1016/s0014-5793(03)00518-0;
RA Hansen C., Tarabykina S., la Cour J.M., Lollike K., Berchtold M.W.;
RT "The PEF family proteins sorcin and grancalcin interact in vivo and in
RT vitro.";
RL FEBS Lett. 545:151-154(2003).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=11714909; DOI=10.1110/ps.36701;
RA Xie X., Dwyer M.D., Swenson L., Parker M.H., Botfield M.C.;
RT "Crystal structure of calcium-free human sorcin: a member of the penta-EF-
RT hand protein family.";
RL Protein Sci. 10:2419-2425(2001).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT LEU-112, SUBUNIT, FUNCTION,
RP CALCIUM-BINDING, AND INTERACTION WITH RYR2 AND ANXA7.
RX PubMed=17699613; DOI=10.1096/fj.07-8988com;
RA Franceschini S., Ilari A., Verzili D., Zamparelli C., Antaramian A.,
RA Rueda A., Valdivia H.H., Chiancone E., Colotti G.;
RT "Molecular basis for the impaired function of the natural F112L sorcin
RT mutant: X-ray crystal structure, calcium affinity, and interaction with
RT annexin VII and the ryanodine receptor.";
RL FASEB J. 22:295-306(2008).
CC -!- FUNCTION: Calcium-binding protein that modulates excitation-contraction
CC coupling in the heart. Contributes to calcium homeostasis in the heart
CC sarcoplasmic reticulum. Modulates the activity of RYR2 calcium
CC channels. {ECO:0000269|PubMed:17699613}.
CC -!- SUBUNIT: Homodimer. Interacts with GCA, RYR2 and ANXA7.
CC {ECO:0000269|PubMed:12804766, ECO:0000269|PubMed:17699613}.
CC -!- INTERACTION:
CC P30626; Q13137: CALCOCO2; NbExp=5; IntAct=EBI-750459, EBI-739580;
CC P30626; Q08493-2: PDE4C; NbExp=3; IntAct=EBI-750459, EBI-12169289;
CC P30626; Q08493-3: PDE4C; NbExp=3; IntAct=EBI-750459, EBI-10225541;
CC P30626; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-750459, EBI-740924;
CC P30626; P40763: STAT3; NbExp=3; IntAct=EBI-750459, EBI-518675;
CC P30626; Q99081: TCF12; NbExp=3; IntAct=EBI-750459, EBI-722877;
CC P30626; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-750459, EBI-739895;
CC P30626-1; P20073: ANXA7; NbExp=2; IntAct=EBI-10816740, EBI-2338704;
CC P30626-1; P30626-1: SRI; NbExp=4; IntAct=EBI-10816740, EBI-10816740;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Sarcoplasmic reticulum membrane;
CC Peripheral membrane protein; Cytoplasmic side. Note=Relocates to the
CC sarcoplasmic reticulum membrane in response to elevated calcium levels.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P30626-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30626-2; Sequence=VSP_046277;
CC Name=3;
CC IsoId=P30626-3; Sequence=VSP_046277, VSP_054463;
CC -!- TISSUE SPECIFICITY: Detected in cardiac myocytes.
CC -!- MISCELLANEOUS: This protein is encoded by an amplified gene in
CC multidrug-resistant cells.
CC -!- MISCELLANEOUS: This protein has been shown to bind calcium with high
CC affinity.
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DR EMBL; L12387; AAA92155.1; -; mRNA.
DR EMBL; M32886; AAA60588.1; -; mRNA.
DR EMBL; AK296601; BAG59214.1; -; mRNA.
DR EMBL; BM739144; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC003991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471091; EAW76909.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76910.1; -; Genomic_DNA.
DR EMBL; BC011025; AAH11025.1; -; mRNA.
DR CCDS; CCDS47638.1; -. [P30626-2]
DR CCDS; CCDS5612.1; -. [P30626-1]
DR CCDS; CCDS59063.1; -. [P30626-3]
DR PIR; S52094; S52094.
DR RefSeq; NP_001243820.1; NM_001256891.1.
DR RefSeq; NP_001243821.1; NM_001256892.1. [P30626-3]
DR RefSeq; NP_003121.1; NM_003130.3. [P30626-1]
DR RefSeq; NP_944490.1; NM_198901.1. [P30626-2]
DR PDB; 1JUO; X-ray; 2.20 A; A/B=1-198.
DR PDB; 2JC2; X-ray; 2.50 A; A/B/C/D=1-198.
DR PDB; 4U8D; X-ray; 2.30 A; A/B=1-198.
DR PDB; 4UPG; X-ray; 2.10 A; A=30-198.
DR PDB; 4USL; X-ray; 1.65 A; A=1-198, D=1-32.
DR PDB; 5MRA; X-ray; 3.74 A; A/B/C/D=32-198.
DR PDBsum; 1JUO; -.
DR PDBsum; 2JC2; -.
DR PDBsum; 4U8D; -.
DR PDBsum; 4UPG; -.
DR PDBsum; 4USL; -.
DR PDBsum; 5MRA; -.
DR AlphaFoldDB; P30626; -.
DR SMR; P30626; -.
DR BioGRID; 112595; 64.
DR CORUM; P30626; -.
DR DIP; DIP-40970N; -.
DR IntAct; P30626; 21.
DR MINT; P30626; -.
DR STRING; 9606.ENSP00000265729; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR iPTMnet; P30626; -.
DR MetOSite; P30626; -.
DR PhosphoSitePlus; P30626; -.
DR SwissPalm; P30626; -.
DR BioMuta; SRI; -.
DR DMDM; 267021; -.
DR OGP; P30626; -.
DR EPD; P30626; -.
DR jPOST; P30626; -.
DR MassIVE; P30626; -.
DR MaxQB; P30626; -.
DR PaxDb; P30626; -.
DR PeptideAtlas; P30626; -.
DR PRIDE; P30626; -.
DR ProteomicsDB; 2025; -.
DR ProteomicsDB; 4466; -.
DR ProteomicsDB; 54730; -. [P30626-1]
DR TopDownProteomics; P30626-1; -. [P30626-1]
DR Antibodypedia; 29805; 197 antibodies from 31 providers.
DR DNASU; 6717; -.
DR Ensembl; ENST00000265729.7; ENSP00000265729.3; ENSG00000075142.14. [P30626-1]
DR Ensembl; ENST00000394641.7; ENSP00000378137.3; ENSG00000075142.14. [P30626-2]
DR Ensembl; ENST00000431660.5; ENSP00000391148.1; ENSG00000075142.14. [P30626-3]
DR GeneID; 6717; -.
DR KEGG; hsa:6717; -.
DR MANE-Select; ENST00000265729.7; ENSP00000265729.3; NM_003130.4; NP_003121.1.
DR UCSC; uc003ujq.3; human. [P30626-1]
DR CTD; 6717; -.
DR DisGeNET; 6717; -.
DR GeneCards; SRI; -.
DR HGNC; HGNC:11292; SRI.
DR HPA; ENSG00000075142; Tissue enhanced (intestine).
DR MIM; 182520; gene.
DR neXtProt; NX_P30626; -.
DR OpenTargets; ENSG00000075142; -.
DR PharmGKB; PA36117; -.
DR VEuPathDB; HostDB:ENSG00000075142; -.
DR eggNOG; KOG0037; Eukaryota.
DR GeneTree; ENSGT00940000153979; -.
DR InParanoid; P30626; -.
DR OMA; RDTGQQG; -.
DR PhylomeDB; P30626; -.
DR TreeFam; TF314682; -.
DR PathwayCommons; P30626; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR Reactome; R-HSA-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-HSA-425561; Sodium/Calcium exchangers.
DR Reactome; R-HSA-5578775; Ion homeostasis.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR SignaLink; P30626; -.
DR SIGNOR; P30626; -.
DR BioGRID-ORCS; 6717; 16 hits in 1073 CRISPR screens.
DR ChiTaRS; SRI; human.
DR EvolutionaryTrace; P30626; -.
DR GeneWiki; SRI_(gene); -.
DR GenomeRNAi; 6717; -.
DR Pharos; P30626; Tbio.
DR PRO; PR:P30626; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P30626; protein.
DR Bgee; ENSG00000075142; Expressed in mucosa of transverse colon and 206 other tissues.
DR ExpressionAtlas; P30626; baseline and differential.
DR Genevisible; P30626; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016529; C:sarcoplasmic reticulum; TAS:BHF-UCL.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030315; C:T-tubule; TAS:BHF-UCL.
DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR GO; GO:0005246; F:calcium channel regulator activity; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0044325; F:transmembrane transporter binding; TAS:BHF-UCL.
DR GO; GO:0001508; P:action potential; TAS:ProtInc.
DR GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; TAS:ProtInc.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; TAS:ProtInc.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0055118; P:negative regulation of cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:0010459; P:negative regulation of heart rate; IMP:BHF-UCL.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IEA:Ensembl.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:BHF-UCL.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP:BHF-UCL.
DR GO; GO:0010649; P:regulation of cell communication by electrical coupling; TAS:BHF-UCL.
DR GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IMP:BHF-UCL.
DR GO; GO:0008016; P:regulation of heart contraction; TAS:ProtInc.
DR GO; GO:1901841; P:regulation of high voltage-gated calcium channel activity; IMP:BHF-UCL.
DR GO; GO:1901077; P:regulation of relaxation of muscle; IMP:BHF-UCL.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; TAS:BHF-UCL.
DR GO; GO:0006942; P:regulation of striated muscle contraction; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13405; EF-hand_6; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Reference proteome;
KW Repeat; Sarcoplasmic reticulum.
FT CHAIN 1..198
FT /note="Sorcin"
FT /id="PRO_0000073725"
FT DOMAIN 29..64
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 70..103
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 100..135
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 134..169
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 1..17
FT /note="MAYPGHPGAGGGYYPGG -> MQ (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16341674"
FT /id="VSP_046277"
FT VAR_SEQ 191..198
FT /note="FIQCVMSV -> VSLRN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054463"
FT MUTAGEN 112
FT /note="F->L: Reduces affinity for calcium 5-fold."
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:4USL"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:4USL"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4USL"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:4USL"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:4USL"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4USL"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:4USL"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4USL"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4USL"
FT HELIX 92..112
FT /evidence="ECO:0007829|PDB:4USL"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4USL"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:4USL"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:4USL"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:4USL"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4UPG"
FT HELIX 156..176
FT /evidence="ECO:0007829|PDB:4USL"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2JC2"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1JUO"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:4USL"
SQ SEQUENCE 198 AA; 21676 MW; A4829C7650A5E3FA CRC64;
MAYPGHPGAG GGYYPGGYGG APGGPAFPGQ TQDPLYGYFA AVAGQDGQID ADELQRCLTQ
SGIAGGYKPF NLETCRLMVS MLDRDMSGTM GFNEFKELWA VLNGWRQHFI SFDTDRSGTV
DPQELQKALT TMGFRLSPQA VNSIAKRYST NGKITFDDYI ACCVKLRALT DSFRRRDTAQ
QGVVNFPYDD FIQCVMSV
