S10A4_BOVIN
ID S10A4_BOVIN Reviewed; 101 AA.
AC P35466; Q3ZBN9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein S100-A4;
DE AltName: Full=Metastasin;
DE AltName: Full=Placental calcium-binding protein homolog;
DE AltName: Full=S100 calcium-binding protein A4;
GN Name=S100A4; Synonyms=CAPL;
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=9759666; DOI=10.1177/00220345980770090501;
RA Duarte W.R., Kasugai S., Iimura T., Oida S., Takenaga K., Ohya K.,
RA Ishikawa I.;
RT "cDNA cloning of S100 calcium-binding proteins from bovine periodontal
RT ligament and their expression in oral tissues.";
RL J. Dent. Res. 77:1694-1699(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-101, AND ACETYLATION AT ALA-2.
RC TISSUE=Retina;
RX PubMed=8119967; DOI=10.1016/s0021-9258(17)37592-0;
RA Polans A.S., Palczewski K., Asson-Batres M.A., Ohguro H., Witowska D.,
RA Haley T.L., Baizer L., Crabb J.W.;
RT "Purification and primary structure of Capl, an S-100-related calcium-
RT binding protein isolated from bovine retina.";
RL J. Biol. Chem. 269:6233-6240(1994).
CC -!- FUNCTION: Calcium-binding protein that plays a role in various cellular
CC processes including motility, angiogenesis, cell differentiation,
CC apoptosis, and autophagy. Increases cell motility and invasiveness by
CC interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9 (By
CC similarity). Mechanistically, promotes filament depolymerization and
CC increases the amount of soluble myosin-IIA, resulting in the formation
CC of stable protrusions facilitating chemotaxis (By similarity).
CC Modulates also the pro-apoptotic function of TP53 by binding to its C-
CC terminal transactivation domain within the nucleus and reducing its
CC protein levels (By similarity). Within the extracellular space,
CC stimulates cytokine production including granulocyte colony-stimulating
CC factor and CCL24 from T-lymphocytes (By similarity). In addition,
CC stimulates T-lymphocyte chemotaxis by acting as a chemoattractant
CC complex with PGLYRP1 that promotes lymphocyte migration via CCR5 and
CC CXCR3 receptors (By similarity). {ECO:0000250|UniProtKB:P07091,
CC ECO:0000250|UniProtKB:P26447}.
CC -!- SUBUNIT: Homodimer. Interacts with PPFIBP1 in a calcium-dependent mode.
CC Interacts with PGLYRP1; this complex acts as a chemoattractant that
CC promotes lymphocyte movement. Interacts with MYH9; this interaction
CC increases cell motility. Interacts with Annexin 2/ANXA2. Interacts with
CC TP53; this interaction promotes TP53 degradation. Interacts with CCR5
CC and CXCR3. Interacts with FCGR3A; this interaction inhibits PKC-
CC dependent phosphorylation of FCGR3A. {ECO:0000250|UniProtKB:P26447}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P26447}. Nucleus
CC {ECO:0000250|UniProtKB:P26447}. Cytoplasm
CC {ECO:0000250|UniProtKB:P07091}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; D89056; BAA13754.1; -; mRNA.
DR EMBL; BC103192; AAI03193.1; -; mRNA.
DR PIR; A53217; A53217.
DR RefSeq; NP_777020.1; NM_174595.2.
DR AlphaFoldDB; P35466; -.
DR SMR; P35466; -.
DR STRING; 9913.ENSBTAP00000025561; -.
DR iPTMnet; P35466; -.
DR PaxDb; P35466; -.
DR PeptideAtlas; P35466; -.
DR PRIDE; P35466; -.
DR Ensembl; ENSBTAT00000025561; ENSBTAP00000025561; ENSBTAG00000019203.
DR GeneID; 282343; -.
DR KEGG; bta:282343; -.
DR CTD; 6275; -.
DR VEuPathDB; HostDB:ENSBTAG00000019203; -.
DR VGNC; VGNC:34244; S100A4.
DR eggNOG; ENOG502S4AU; Eukaryota.
DR GeneTree; ENSGT00940000161276; -.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; P35466; -.
DR OMA; QDLPDKM; -.
DR OrthoDB; 1560865at2759; -.
DR TreeFam; TF332727; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000019203; Expressed in aorta and 101 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISS:AgBase.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0050786; F:RAGE receptor binding; IBA:GO_Central.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR CDD; cd00213; S-100; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR034325; S-100_dom.
DR InterPro; IPR028496; S100-A4.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF51; PTHR11639:SF51; 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 Acetylation; Calcium; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8119967"
FT CHAIN 2..101
FT /note="Protein S100-A4"
FT /id="PRO_0000143975"
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:0000305"
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:0000305"
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 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:8119967"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26447"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26447"
SQ SEQUENCE 101 AA; 11807 MW; D30F3FDC012C7F3D CRC64;
MAYPLEKALD VMVSTFHKYS GKEGDKFKLN KSELKELLTR ELPSFLGKRT DETAFQKLMS
NLDCNKDNEV DFQEYCVFLS CIAMMCNEFF EGFPDKQPRK K
