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S10A1_MOUSE
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   03-AUG-2022, entry version 158.
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; 3.
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; P56565; -.
DR   PeptideAtlas; P56565; -.
DR   PRIDE; P56565; -.
DR   ProteomicsDB; 256857; -.
DR   TopDownProteomics; P56565; -.
DR   DNASU; 20193; -.
DR   GeneID; 20193; -.
DR   KEGG; mmu:20193; -.
DR   CTD; 6271; -.
DR   MGI; MGI:1338917; S100a1.
DR   eggNOG; ENOG502SSF0; Eukaryota.
DR   InParanoid; P56565; -.
DR   OrthoDB; 1495576at2759; -.
DR   PhylomeDB; P56565; -.
DR   Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
DR   BioGRID-ORCS; 20193; 2 hits in 71 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; ISO:MGI.
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:0043005; C:neuron projection; ISO:MGI.
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:0051000; P:positive regulation of nitric-oxide synthase activity; ISO:MGI.
DR   GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:MGI.
DR   GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; ISO:MGI.
DR   GO; GO:0008016; P:regulation of heart contraction; IEA:InterPro.
DR   CDD; cd05025; S-100A1; 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   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; SSF47473; 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
 
 
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