S10AA_BOVIN
ID S10AA_BOVIN Reviewed; 97 AA.
AC P60902; P08206; Q56JZ4;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
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, CLP11;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
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 TISSUE=Lymphoid epithelium;
RA Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT "Analysis of sequences obtained from constructed full-length bovine cDNA
RT libraries.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 2-57.
RX PubMed=2415974; DOI=10.1073/pnas.82.23.7884;
RA Glenney J.R. Jr., Tack B.F.;
RT "Amino-terminal sequence of p36 and associated p10: identification of the
RT site of tyrosine phosphorylation and homology with S-100.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7884-7888(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-21.
RC TISSUE=Aorta;
RX PubMed=2970844; DOI=10.1042/bj2510777;
RA Martin F., Derancourt J., Capony J.-P., Watrin A., Cavadore J.-C.;
RT "A 36 kDa monomeric protein and its complex with a 10 kDa protein both
RT isolated from bovine aorta are calpactin-like proteins that differ in their
RT Ca2+-dependent calmodulin-binding and actin-severing properties.";
RL Biochem. J. 251:777-785(1988).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P05943, ECO:0000250|UniProtKB:P08207,
CC ECO:0000250|UniProtKB:P60903}.
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; M16464; AAA30423.1; -; mRNA.
DR EMBL; AY911333; AAW82101.1; -; mRNA.
DR EMBL; BC102207; AAI02208.1; -; mRNA.
DR PIR; B28489; B28489.
DR RefSeq; NP_777075.1; NM_174650.1.
DR AlphaFoldDB; P60902; -.
DR SMR; P60902; -.
DR STRING; 9913.ENSBTAP00000020150; -.
DR PaxDb; P60902; -.
DR PeptideAtlas; P60902; -.
DR PRIDE; P60902; -.
DR Ensembl; ENSBTAT00000020150; ENSBTAP00000020150; ENSBTAG00000015147.
DR GeneID; 282466; -.
DR KEGG; bta:282466; -.
DR CTD; 6281; -.
DR VEuPathDB; HostDB:ENSBTAG00000015147; -.
DR VGNC; VGNC:34237; S100A10.
DR eggNOG; ENOG502S6TB; Eukaryota.
DR GeneTree; ENSGT00940000154197; -.
DR HOGENOM; CLU_138624_2_1_1; -.
DR InParanoid; P60902; -.
DR OMA; SEMEHAP; -.
DR OrthoDB; 1508691at2759; -.
DR TreeFam; TF332727; -.
DR Reactome; R-BTA-75205; Dissolution of Fibrin Clot.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000015147; Expressed in subcutaneous adipose tissue and 104 other tissues.
DR GO; GO:1990665; C:AnxA2-p11 complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0098797; C:plasma membrane protein complex; IEA:Ensembl.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0001765; P:membrane raft assembly; IEA:Ensembl.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0051099; P:positive regulation of binding; IEA:Ensembl.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0050767; P:regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:0006900; P:vesicle budding from membrane; IEA:Ensembl.
DR CDD; cd05024; S-100A10; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
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; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Isopeptide bond;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2415974"
FT CHAIN 2..97
FT /note="Protein S100-A10"
FT /id="PRO_0000144001"
FT REGION 60..71
FT /note="Ancestral calcium site"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60903"
FT MOD_RES 28
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60903"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
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"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P60903"
FT CONFLICT 4..6
FT /note="QME -> EMQ (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="E -> Q (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 97 AA; 11203 MW; 3E8E03A6E7DD7A8D CRC64;
MPSQMEHAME TMMFTFHKFA GDKGYLTKED LRVLMEKEFP GFLENQKDPL AVDKIMKDLD
QCRDGKVGFQ SFFSLIAGLT IACNDYFVVH MKQKGKK
