S10A4_RAT
ID S10A4_RAT Reviewed; 101 AA.
AC P05942;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein S100-A4;
DE AltName: Full=Metastasin;
DE AltName: Full=Nerve growth factor-induced protein 42A;
DE AltName: Full=P9K;
DE AltName: Full=Placental calcium-binding protein;
DE AltName: Full=S100 calcium-binding protein A4;
GN Name=S100a4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3422491; DOI=10.1073/pnas.85.4.1277;
RA Masiakowski P., Shooter E.M.;
RT "Nerve growth factor induces the genes for two proteins related to a family
RT of calcium-binding proteins in PC12 cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1277-1281(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3430604; DOI=10.1016/0022-2836(87)90453-0;
RA Barraclough R., Savin J., Dube S.K., Rudland P.S.;
RT "Molecular cloning and sequence of the gene for p9Ka. A cultured
RT myoepithelial cell protein with strong homology to S-100, a calcium-binding
RT protein.";
RL J. Mol. Biol. 198:13-20(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 3-101.
RX PubMed=1741158;
RA de Vouge M.W., Mukherjee B.B.;
RT "Transformation of normal rat kidney cells by v-K-ras enhances expression
RT of transin 2 and an S-100-related calcium-binding protein.";
RL Oncogene 7:109-119(1992).
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 -!- INDUCTION: By nerve growth factor.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; X06916; CAA30014.1; -; Genomic_DNA.
DR EMBL; J03628; AAA42098.1; -; mRNA.
DR EMBL; X64022; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X64023; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S01759; S01759.
DR RefSeq; NP_036750.1; NM_012618.2.
DR RefSeq; XP_006232654.1; XM_006232592.3.
DR AlphaFoldDB; P05942; -.
DR SMR; P05942; -.
DR STRING; 10116.ENSRNOP00000015958; -.
DR iPTMnet; P05942; -.
DR PhosphoSitePlus; P05942; -.
DR jPOST; P05942; -.
DR PaxDb; P05942; -.
DR PRIDE; P05942; -.
DR DNASU; 24615; -.
DR Ensembl; ENSRNOT00000015958; ENSRNOP00000015958; ENSRNOG00000011821.
DR GeneID; 24615; -.
DR KEGG; rno:24615; -.
DR UCSC; RGD:3245; rat.
DR CTD; 6275; -.
DR RGD; 3245; S100a4.
DR eggNOG; ENOG502S4AU; Eukaryota.
DR GeneTree; ENSGT00940000161276; -.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; P05942; -.
DR OMA; QDLPDKM; -.
DR OrthoDB; 1560865at2759; -.
DR PhylomeDB; P05942; -.
DR TreeFam; TF332727; -.
DR PRO; PR:P05942; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011821; Expressed in lung and 20 other tissues.
DR Genevisible; P05942; RN.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; TAS:RGD.
DR GO; GO:0050786; F:RAGE receptor binding; ISO:RGD.
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; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Calcium; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P35466"
FT CHAIN 2..101
FT /note="Protein S100-A4"
FT /id="PRO_0000143979"
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 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P35466"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26447"
SQ SEQUENCE 101 AA; 11776 MW; EA0619CEE4F487C1 CRC64;
MARPLEEALD VIVSTFHKYS GNEGDKFKLN KTELKELLTR ELPSFLGRRT DEAAFQKLMN
NLDSNRDNEV DFQEYCVFLS CIAMMCNEFF EGCPDKEPRK K
