S10AA_MOUSE
ID S10AA_MOUSE Reviewed; 97 AA.
AC P08207;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Protein S100-A10;
DE AltName: Full=Calpactin I light chain;
DE AltName: Full=Calpactin-1 light chain;
DE AltName: Full=Cellular ligand of annexin II;
DE AltName: Full=S100 calcium-binding protein A10;
DE AltName: Full=p10 protein;
DE AltName: Full=p11;
GN Name=S100a10; Synonyms=Cal1l;
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].
RX PubMed=3038891; DOI=10.1016/s0021-9258(18)61015-4;
RA Saris C.J.M., Kristensen T., D'Eustachio P., Hicks L.J., Noonan D.J.,
RA Glenney J.R. Jr., Hunter T., Tack B.F.;
RT "cDNA sequence and tissue distribution of the mRNA for bovine and murine
RT p11, the S100-related light chain of the protein-tyrosine kinase substrate
RT p36 (calpactin I).";
RL J. Biol. Chem. 262:10663-10671(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 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).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP INTERACTION WITH TASOR.
RX PubMed=31112734; DOI=10.1016/j.yexcr.2019.05.018;
RA Gresakova V., Novosadova V., Prochazkova M., Bhargava S., Jenickova I.,
RA Prochazka J., Sedlacek R.;
RT "Fam208a orchestrates interaction protein network essential for early
RT embryonic development and cell division.";
RL Exp. Cell Res. 382:111437-111437(2019).
CC -!- FUNCTION: Because S100A10 induces the dimerization of ANXA2/p36, it may
CC function as a regulator of protein phosphorylation in that the ANXA2
CC monomer is the preferred target (in vitro) of tyrosine-specific kinase.
CC -!- SUBUNIT: Heterotetramer containing 2 light chains of S100A10/p11 and 2
CC heavy chains of ANXA2/p36 (By similarity). Interacts with SCN10A (By
CC similarity). Interacts with TASOR (PubMed:31112734).
CC {ECO:0000250|UniProtKB:P05943, ECO:0000250|UniProtKB:P60903,
CC ECO:0000269|PubMed:31112734}.
CC -!- INTERACTION:
CC P08207; P07356: Anxa2; NbExp=2; IntAct=EBI-643986, EBI-738510;
CC -!- MISCELLANEOUS: Does not appear to bind calcium. Contains 2 ancestral
CC calcium site related to EF-hand domains that have lost their ability to
CC bind calcium.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; M16465; AAA37363.1; -; mRNA.
DR EMBL; BC025044; AAH25044.1; -; mRNA.
DR CCDS; CCDS38526.1; -.
DR PIR; A28489; A28489.
DR RefSeq; NP_033138.1; NM_009112.2.
DR AlphaFoldDB; P08207; -.
DR SMR; P08207; -.
DR BioGRID; 203049; 11.
DR ComplexPortal; CPX-898; Annexin A2 - S100-A10 complex.
DR ComplexPortal; CPX-899; SMARCA3 - Annexin A2 - S100-A10 complex.
DR ComplexPortal; CPX-905; AHNAK - Annexin A2 - S100-A10 complex.
DR CORUM; P08207; -.
DR IntAct; P08207; 7.
DR STRING; 10090.ENSMUSP00000036949; -.
DR iPTMnet; P08207; -.
DR PhosphoSitePlus; P08207; -.
DR EPD; P08207; -.
DR jPOST; P08207; -.
DR PaxDb; P08207; -.
DR PeptideAtlas; P08207; -.
DR PRIDE; P08207; -.
DR ProteomicsDB; 255435; -.
DR Antibodypedia; 1093; 512 antibodies from 39 providers.
DR DNASU; 20194; -.
DR Ensembl; ENSMUST00000045756; ENSMUSP00000036949; ENSMUSG00000041959.
DR Ensembl; ENSMUST00000170612; ENSMUSP00000130712; ENSMUSG00000041959.
DR GeneID; 20194; -.
DR KEGG; mmu:20194; -.
DR UCSC; uc008qfk.1; mouse.
DR CTD; 6281; -.
DR MGI; MGI:1339468; S100a10.
DR VEuPathDB; HostDB:ENSMUSG00000041959; -.
DR eggNOG; ENOG502S6TB; Eukaryota.
DR GeneTree; ENSGT00940000154197; -.
DR HOGENOM; CLU_138624_2_1_1; -.
DR InParanoid; P08207; -.
DR OMA; SEMEHAP; -.
DR OrthoDB; 1508691at2759; -.
DR PhylomeDB; P08207; -.
DR TreeFam; TF332727; -.
DR Reactome; R-MMU-75205; Dissolution of Fibrin Clot.
DR BioGRID-ORCS; 20194; 1 hit in 74 CRISPR screens.
DR ChiTaRS; S100a10; mouse.
DR PRO; PR:P08207; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P08207; protein.
DR Bgee; ENSMUSG00000041959; Expressed in conjunctival fornix and 302 other tissues.
DR ExpressionAtlas; P08207; baseline and differential.
DR Genevisible; P08207; MM.
DR GO; GO:1990665; C:AnxA2-p11 complex; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0098797; C:plasma membrane protein complex; IPI:ComplexPortal.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0001765; P:membrane raft assembly; ISO:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0051099; P:positive regulation of binding; IMP:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; IC:ComplexPortal.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:1905686; P:positive regulation of plasma membrane repair; IC:ComplexPortal.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; ISO:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0050767; P:regulation of neurogenesis; IDA:ComplexPortal.
DR GO; GO:0006900; P:vesicle budding from membrane; ISO:MGI.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028476; S100-A10.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF74; PTHR11639:SF74; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Reference proteome; Repeat.
FT CHAIN 1..97
FT /note="Protein S100-A10"
FT /id="PRO_0000144004"
FT DOMAIN 47..82
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 60..71
FT /note="Ancestral calcium site"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 28
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60903"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60903"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60903"
SQ SEQUENCE 97 AA; 11186 MW; E7F092D4DAF6B43E CRC64;
MPSQMEHAME TMMLTFHRFA GDKDHLTKED LRVLMEREFP GFLENQKDPL AVDKIMKDLD
QCRDGKVGFQ SFLSLVAGLT IACNDYFVVN MKQKGKK
