SORCN_MOUSE
ID SORCN_MOUSE Reviewed; 198 AA.
AC Q6P069; Q3UKC5; Q9CR38; Q9D7V8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Sorcin;
GN Name=Sri;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Amnion, Heart, Medulla oblongata, Placenta, Small intestine, and
RC Stomach;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RYR2, AND TISSUE
RP SPECIFICITY.
RX PubMed=12824171; DOI=10.1074/jbc.m305931200;
RA Farrell E.F., Antaramian A., Rueda A., Gomez A.M., Valdivia H.H.;
RT "Sorcin inhibits calcium release and modulates excitation-contraction
RT coupling in the heart.";
RL J. Biol. Chem. 278:34660-34666(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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-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:12824171}.
CC -!- SUBUNIT: Homodimer. Interacts with GCA, RYR2 and ANXA7 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12824171}.
CC Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:12824171};
CC Peripheral membrane protein {ECO:0000269|PubMed:12824171}; Cytoplasmic
CC side {ECO:0000269|PubMed:12824171}. Note=Relocates to the sarcoplasmic
CC reticulum membrane in response to elevated calcium levels.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P069-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P069-2; Sequence=VSP_013448;
CC -!- TISSUE SPECIFICITY: Detected in cardiac myocytes.
CC {ECO:0000269|PubMed:12824171}.
CC -!- MISCELLANEOUS: This protein has been shown to bind calcium with high
CC affinity. {ECO:0000250}.
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DR EMBL; AK008404; BAB25652.1; -; mRNA.
DR EMBL; AK008783; BAB25891.1; -; mRNA.
DR EMBL; AK008970; BAB25997.1; -; mRNA.
DR EMBL; AK134747; BAE22266.1; -; mRNA.
DR EMBL; AK146071; BAE26876.1; -; mRNA.
DR EMBL; AK146911; BAE27523.1; -; mRNA.
DR EMBL; AK168572; BAE40442.1; -; mRNA.
DR EMBL; AK168792; BAE40625.1; -; mRNA.
DR EMBL; AK168900; BAE40716.1; -; mRNA.
DR EMBL; BC065790; AAH65790.1; -; mRNA.
DR CCDS; CCDS19079.1; -. [Q6P069-2]
DR CCDS; CCDS39009.1; -. [Q6P069-1]
DR RefSeq; NP_001074443.1; NM_001080974.2. [Q6P069-1]
DR RefSeq; NP_079894.2; NM_025618.3. [Q6P069-2]
DR AlphaFoldDB; Q6P069; -.
DR SMR; Q6P069; -.
DR BioGRID; 224853; 4.
DR STRING; 10090.ENSMUSP00000118221; -.
DR iPTMnet; Q6P069; -.
DR PhosphoSitePlus; Q6P069; -.
DR REPRODUCTION-2DPAGE; IPI00556765; -.
DR EPD; Q6P069; -.
DR jPOST; Q6P069; -.
DR MaxQB; Q6P069; -.
DR PaxDb; Q6P069; -.
DR PeptideAtlas; Q6P069; -.
DR PRIDE; Q6P069; -.
DR ProteomicsDB; 261608; -. [Q6P069-1]
DR ProteomicsDB; 261609; -. [Q6P069-2]
DR Antibodypedia; 29805; 197 antibodies from 31 providers.
DR DNASU; 109552; -.
DR Ensembl; ENSMUST00000088786; ENSMUSP00000086165; ENSMUSG00000003161. [Q6P069-2]
DR Ensembl; ENSMUST00000148633; ENSMUSP00000118221; ENSMUSG00000003161. [Q6P069-1]
DR GeneID; 109552; -.
DR KEGG; mmu:109552; -.
DR UCSC; uc008wjh.2; mouse. [Q6P069-2]
DR UCSC; uc008wji.2; mouse. [Q6P069-1]
DR CTD; 6717; -.
DR MGI; MGI:98419; Sri.
DR VEuPathDB; HostDB:ENSMUSG00000003161; -.
DR eggNOG; KOG0037; Eukaryota.
DR GeneTree; ENSGT00940000153979; -.
DR HOGENOM; CLU_051357_4_1_1; -.
DR InParanoid; Q6P069; -.
DR OMA; RDTGQQG; -.
DR OrthoDB; 1330600at2759; -.
DR PhylomeDB; Q6P069; -.
DR TreeFam; TF314682; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR Reactome; R-MMU-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-MMU-425561; Sodium/Calcium exchangers.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 109552; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Sri; mouse.
DR PRO; PR:Q6P069; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6P069; protein.
DR Bgee; ENSMUSG00000003161; Expressed in granulocyte and 260 other tissues.
DR Genevisible; Q6P069; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0042584; C:chromaffin granule membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0044326; C:dendritic spine neck; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0031982; C:vesicle; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0006816; P:calcium ion transport; IPI:MGI.
DR GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IMP:BHF-UCL.
DR GO; GO:0055118; P:negative regulation of cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0010459; P:negative regulation of heart rate; ISO:MGI.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISO:MGI.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IMP:BHF-UCL.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:BHF-UCL.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IMP:BHF-UCL.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; ISO:MGI.
DR GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; ISO:MGI.
DR GO; GO:1901841; P:regulation of high voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:1901077; P:regulation of relaxation of muscle; ISO:MGI.
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 Alternative splicing; Calcium; Cytoplasm; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Sarcoplasmic reticulum.
FT CHAIN 1..198
FT /note="Sorcin"
FT /id="PRO_0000073726"
FT DOMAIN 45..64
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 70..98
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 151..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 MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05044"
FT VAR_SEQ 1..17
FT /note="MAYPGHPGAGGGYYPGG -> MQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013448"
FT CONFLICT 25
FT /note="P -> A (in Ref. 1; BAB25891)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 21627 MW; 254588544495E1BF CRC64;
MAYPGHPGAG GGYYPGGYGG APGGPAFPGQ TQDPLYGYFA AVAGQDGQID ADELQRCLTQ
SGIAGGYKPF NLETCRLMVS MLDRDMSGTM GFNEFKELWA VLNGWRQHFI SFDSDRSGTV
DPQELQKALT TMGFRLSPQT VNSVAKRYST SGKITFDDYI ACCVKLRALT DSFRRRDSGQ
QGVVNFSYDD FIQCVMTV
