ID S10A1_MOUSE Reviewed; 94 AA.
AC P56565; O88949;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 08-NOV-2023, entry version 163.
DE RecName: Full=Protein S100-A1;
DE AltName: Full=S-100 protein alpha chain;
DE AltName: Full=S-100 protein subunit alpha;
DE AltName: Full=S100 calcium-binding protein A1;
GN Name=S100a1;
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].
RA Marra M., Hillier L., Allen M., Bowles M., Dietrich N., Dubuque T.,
RA Geisel S., Kucaba T., Lacy M., Le M., Martin J., Morris M.,
RA Schellenberg K., Steptoe M., Tan F., Underwood K., Moore B., Theising B.,
RA Wylie T., Lennon G., Soares B., Wilson R., Waterston R.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9920416; DOI=10.1016/s0167-4889(98)00137-2;
RA Ridinger K., Ilg E.C., Niggli F.K., Heizmann C.W., Schaefer B.W.;
RT "Clustered organization of S100 genes in human and mouse.";
RL Biochim. Biophys. Acta 1448:254-263(1998).
RN [3]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=3276520; DOI=10.1111/j.1432-1033.1988.tb13805.x;
RA Haimoto H., Kato K.;
RT "S100a0 (alpha alpha) protein in cardiac muscle. Isolation from human
RT cardiac muscle and ultrastructural localization.";
RL Eur. J. Biochem. 171:409-415(1988).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11909974; DOI=10.1128/mcb.22.8.2821-2829.2002;
RA Du X.J., Cole T.J., Tenis N., Gao X.M., Koentgen F., Kemp B.E.,
RA Heierhorst J.;
RT "Impaired cardiac contractility response to hemodynamic stress in S100A1-
RT deficient mice.";
RL Mol. Cell. Biol. 22:2821-2829(2002).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16952982; DOI=10.1161/circulationaha.106.622415;
RA Most P., Seifert H., Gao E., Funakoshi H., Voelkers M., Heierhorst J.,
RA Remppis A., Pleger S.T., DeGeorge B.R. Jr., Eckhart A.D., Feldman A.M.,
RA Koch W.J.;
RT "Cardiac S100A1 protein levels determine contractile performance and
RT propensity toward heart failure after myocardial infarction.";
RL Circulation 114:1258-1268(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATP5F1A AND ATP5F1B.
RX PubMed=17438143; DOI=10.1128/mcb.02045-06;
RA Boerries M., Most P., Gledhill J.R., Walker J.E., Katus H.A., Koch W.J.,
RA Aebi U., Schoenenberger C.A.;
RT "Ca2+ -dependent interaction of S100A1 with F1-ATPase leads to an increased
RT ATP content in cardiomyocytes.";
RL Mol. Cell. Biol. 27:4365-4373(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Small calcium binding protein that plays important roles in
CC several biological processes such as Ca(2+) homeostasis, chondrocyte
CC biology and cardiomyocyte regulation (PubMed:11909974,
CC PubMed:16952982). In response to an increase in intracellular Ca(2+)
CC levels, binds calcium which triggers conformational changes. These
CC changes allow interactions with specific target proteins and modulate
CC their activity. Regulates a network in cardiomyocytes controlling
CC sarcoplasmic reticulum Ca(2+) cycling and mitochondrial function
CC through interaction with the ryanodine receptors RYR1 and RYR2,
CC sarcoplasmic reticulum Ca(2+)-ATPase/ATP2A2 and mitochondrial F1-ATPase
CC (PubMed:17438143). Facilitates diastolic Ca(2+) dissociation and
CC myofilament mechanics in order to improve relaxation during diastole
CC (By similarity). {ECO:0000250|UniProtKB:P23297,
CC ECO:0000269|PubMed:11909974, ECO:0000269|PubMed:16952982,
CC ECO:0000269|PubMed:17438143}.
CC -!- SUBUNIT: Dimer of either two alpha chains, or two beta chains, or one
CC alpha and one beta chain. Also forms heterodimers with S100P (By
CC similarity). Interacts with AGER (By similarity). Interacts with CAPZA1
CC (By similarity). Interacts with FKBP4. Interacts with RYR1 and RYR2.
CC Interacts with CACYBP in a calcium-dependent manner. Interacts with
CC PPP5C (via TPR repeats); the interaction is calcium-dependent and
CC modulates PPP5C activity. Interacts with ATP2A2 and PLN in a Ca(2+)-
CC dependent manner (By similarity). Interacts with mitochondrial F1-
CC ATPase subunits ATP5F1A and ATP5F1B; these interactions increase F1-
CC ATPase activity (PubMed:17438143). {ECO:0000250|UniProtKB:P23297,
CC ECO:0000250|UniProtKB:P35467, ECO:0000269|PubMed:17438143}.
CC -!- INTERACTION:
CC P56565; P07091: S100a4; NbExp=6; IntAct=EBI-1544186, EBI-1544173;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23297}.
CC Sarcoplasmic reticulum {ECO:0000269|PubMed:3276520}. Mitochondrion
CC {ECO:0000269|PubMed:17438143}.
CC -!- TISSUE SPECIFICITY: Expressed in the cardiac and the skeletal muscles.
CC {ECO:0000269|PubMed:3276520}.
CC -!- PTM: Glutathionylated; glutathionylation increases affinity to calcium
CC about 10-fold. {ECO:0000250|UniProtKB:P23297}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice show unaltered baseline cardiac
CC function and heart rate, but display deficiencies in their contractile
CC function in response to beta-adrenergic stimulation and enhanced
CC transsarcolemmal Ca(2+) influx (PubMed:11909974). It also significantly
CC accelerates the development of contractile dysfunction after myocardial
CC infarction, with a rapid onset of cardiac remodeling and a transition
CC to heart failure combined with excessive mortality (PubMed:16952982).
CC {ECO:0000269|PubMed:11909974, ECO:0000269|PubMed:16952982}.
CC -!- MISCELLANEOUS: Able to bind zinc in vitro; the binding sites are
CC different from the calcium binding sites. The physiological relevance
CC of zinc binding is unclear. Physiological concentrations of potassium
CC antagonize the binding of both divalent cations, especially affecting
CC the high-affinity calcium-binding sites.
CC {ECO:0000250|UniProtKB:P02639}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; AA000715; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AA207749; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AA500563; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AA432539; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF087687; AAC64108.1; -; mRNA.
DR CCDS; CCDS38503.1; -.
DR RefSeq; NP_035439.1; NM_011309.3.
DR AlphaFoldDB; P56565; -.
DR SMR; P56565; -.
DR BioGRID; 203048; 4.
DR IntAct; P56565; 1.
DR STRING; 10090.ENSMUSP00000058237; -.
DR iPTMnet; P56565; -.
DR PhosphoSitePlus; P56565; -.
DR EPD; P56565; -.
DR jPOST; P56565; -.
DR MaxQB; P56565; -.
DR PaxDb; 10090-ENSMUSP00000058237; -.
DR PeptideAtlas; P56565; -.
DR ProteomicsDB; 256857; -.
DR TopDownProteomics; P56565; -.
DR DNASU; 20193; -.
DR GeneID; 20193; -.
DR KEGG; mmu:20193; -.
DR AGR; MGI:1338917; -.
DR CTD; 6271; -.
DR MGI; MGI:1338917; S100a1.
DR eggNOG; ENOG502SSF0; Eukaryota.
DR InParanoid; P56565; -.
DR OrthoDB; 4234580at2759; -.
DR PhylomeDB; P56565; -.
DR Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
DR BioGRID-ORCS; 20193; 4 hits in 76 CRISPR screens.
DR ChiTaRS; S100a1; mouse.
DR PRO; PR:P56565; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P56565; Protein.
DR GO; GO:0031672; C:A band; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0031674; C:I band; ISO:MGI.
DR GO; GO:0031430; C:M band; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044548; F:S100 protein binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:MGI.
DR GO; GO:0008016; P:regulation of heart contraction; IEA:InterPro.
DR CDD; cd05025; S-100A1; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028486; S100-A1.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF134; PROTEIN S100-A1-RELATED; 1.
DR PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM00054; EFh; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Metal-binding; Mitochondrion; Reference proteome;
KW Repeat; S-nitrosylation; Sarcoplasmic reticulum.
FT CHAIN 1..94
FT /note="Protein S100-A1"
FT /id="PRO_0000143962"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 50..85
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P35467"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P35467"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 86
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P23297"
FT CONFLICT 22
FT /note="Q -> E (in Ref. 1; AA207749)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="Q -> H (in Ref. 1; AA432539)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="Q -> K (in Ref. 2; AAC64108)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="Q -> M (in Ref. 1; AA500563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 94 AA; 10505 MW; 6060736751C4ED15 CRC64;
MGSELESAME TLINVFHAHS GQEGDKYKLS KKELKDLLQT ELSGFLDVQK DADAVDKVMK
ELDENGDGEV DFKEYVVLVA ALTVACNNFF WETS
//
