S10A4_CANLF
ID S10A4_CANLF Reviewed; 101 AA.
AC Q9TV56;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein S100-A4;
DE AltName: Full=Metastasin;
DE AltName: Full=S100 calcium-binding protein A4;
GN Name=S100A4; Synonyms=MTS1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=11206838; DOI=10.1023/a:1026523418456;
RA Miyamori H., Hasegawa K., Kim K.R., Sato H.;
RT "Expression of metastasis-associated mts1 gene is co-induced with membrane
RT type-1 matrix metalloproteinase (MT1-MMP) during oncogenic transformation
RT and tubular formation of Madin Darby canine kidney (MDCK) epithelial
RT cells.";
RL Clin. Exp. Metastasis 18:51-56(2000).
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; AB031064; BAA83419.1; -; mRNA.
DR RefSeq; NP_001003161.1; NM_001003161.1.
DR RefSeq; XP_005622283.1; XM_005622226.2.
DR AlphaFoldDB; Q9TV56; -.
DR SMR; Q9TV56; -.
DR STRING; 9612.ENSCAFP00000025862; -.
DR PaxDb; Q9TV56; -.
DR PRIDE; Q9TV56; -.
DR GeneID; 403787; -.
DR KEGG; cfa:403787; -.
DR CTD; 6275; -.
DR eggNOG; ENOG502S4AU; Eukaryota.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; Q9TV56; -.
DR OMA; QDLPDKM; -.
DR OrthoDB; 1560865at2759; -.
DR TreeFam; TF332727; -.
DR Proteomes; UP000002254; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
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; 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 3: Inferred from homology;
KW Acetylation; Calcium; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Secreted.
FT CHAIN 1..101
FT /note="Protein S100-A4"
FT /id="PRO_0000143976"
FT DOMAIN 12..47
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 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; 11847 MW; 5535387DB7577DF0 CRC64;
MTFPLEKALD VMVSTFHKYS GKEGDKFKLN RSELKELLMR ELPSFLGKRT DEAAFQKLMS
NLDSNRDNEV DFQEYCVFLS CVAMMCNEFF EGFPDKQPRK K
