S10A4_HUMAN
ID S10A4_HUMAN Reviewed; 101 AA.
AC P26447; A8K7R8; D3DV46; Q6ICP8;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Protein S100-A4;
DE AltName: Full=Calvasculin;
DE AltName: Full=Metastasin;
DE AltName: Full=Placental calcium-binding protein;
DE AltName: Full=Protein Mts1;
DE AltName: Full=S100 calcium-binding protein A4;
GN Name=S100A4; Synonyms=CAPL, MTS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=1384693; DOI=10.1021/bi00157a012;
RA Engelkamp D., Schaefer B.W., Erne P., Heizmann C.W.;
RT "S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of
RT three calcium-binding proteins from human heart.";
RL Biochemistry 31:10258-10264(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8341667; DOI=10.1073/pnas.90.14.6547;
RA Engelkamp D., Schaefer B.W., Mattei M.-G., Erne P., Heizmann C.W.;
RT "Six S100 genes are clustered on human chromosome 1q21: identification of
RT two genes coding for the two previously unreported calcium-binding proteins
RT S100D and S100E.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6547-6551(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Spleen;
RX PubMed=1329089; DOI=10.1073/pnas.89.19.9146;
RA Tulchinsky E.M., Ford H.L., Kramerov D., Reshetnyak E., Grigorian M.,
RA Zain S., Lukanidin E.;
RT "Transcriptional analysis of the mts1 gene with specific reference to 5'
RT flanking sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9146-9150(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and Prostate;
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 [9]
RP PROTEIN SEQUENCE OF 8-18 AND 36-57.
RC TISSUE=Platelet;
RX PubMed=1482346; DOI=10.1016/0006-291x(92)90216-8;
RA Tomida Y., Terasawa M., Kobayashi R., Hidaka H.;
RT "Calcyclin and calvasculin exist in human platelets.";
RL Biochem. Biophys. Res. Commun. 189:1310-1316(1992).
RN [10]
RP INTERACTION WITH PPFIBP1.
RX PubMed=11836260; DOI=10.1074/jbc.m110976200;
RA Kriajevska M., Fischer-Larsen M., Moertz E., Vorm O., Tulchinsky E.,
RA Grigorian M., Ambartsumian N., Lukanidin E.;
RT "Liprin beta 1, a member of the family of LAR transmembrane tyrosine
RT phosphatase-interacting proteins, is a new target for the metastasis-
RT associated protein S100A4 (Mts1).";
RL J. Biol. Chem. 277:5229-5235(2002).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [12]
RP FUNCTION, AND INTERACTION WITH MYH9.
RX PubMed=16707441; DOI=10.1158/0008-5472.can-05-3087;
RA Li Z.H., Bresnick A.R.;
RT "The S100A4 metastasis factor regulates cellular motility via a direct
RT interaction with myosin-IIA.";
RL Cancer Res. 66:5173-5180(2006).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7 AND LYS-35, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP INTERACTION WITH FCGR3A.
RX PubMed=23024279; DOI=10.4049/jimmunol.1200704;
RA Li X., Baskin J.G., Mangan E.K., Su K., Gibson A.W., Ji C., Edberg J.C.,
RA Kimberly R.P.;
RT "The unique cytoplasmic domain of human FcgammaRIIIA regulates receptor-
RT mediated function.";
RL J. Immunol. 189:4284-4294(2012).
RN [16]
RP FUNCTION, INTERACTION WITH TP53, AND SUBCELLULAR LOCATION.
RX PubMed=23752197; DOI=10.1038/onc.2013.213;
RA Orre L.M., Panizza E., Kaminskyy V.O., Vernet E., Graeslund T.,
RA Zhivotovsky B., Lehtioe J.;
RT "S100A4 interacts with p53 in the nucleus and promotes p53 degradation.";
RL Oncogene 32:5531-5540(2013).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PGLYRP1.
RX PubMed=26654597; DOI=10.1080/15384101.2015.1104440;
RA Dukhanina E.A., Lukyanova T.I., Romanova E.A., Guerriero V., Gnuchev N.V.,
RA Georgiev G.P., Yashin D.V., Sashchenko L.P.;
RT "A new role for PGRP-S (Tag7) in immune defense: lymphocyte migration is
RT induced by a chemoattractant complex of Tag7 with Mts1.";
RL Cell Cycle 14:3635-3643(2015).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP FUNCTION, INTERACTION WITH PGLYRP1 AND CCR5, AND SUBCELLULAR LOCATION.
RX PubMed=30713770;
RA Sharapova T.N., Romanova E.A., Sashchenko L.P., Yashin D.V.;
RT "Tag7-Mts1 Complex Induces Lymphocytes Migration via CCR5 and CXCR3
RT Receptors.";
RL Acta Naturae 10:115-120(2018).
RN [21]
RP STRUCTURE BY NMR.
RX PubMed=12379109; DOI=10.1021/bi020365r;
RA Vallely K.M., Rustandi R.R., Ellis K.C., Varlamova O., Bresnick A.R.,
RA Weber D.J.;
RT "Solution structure of human Mts1 (S100A4) as determined by NMR
RT spectroscopy.";
RL Biochemistry 41:12670-12680(2002).
RN [22] {ECO:0007744|PDB:5LPU}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND INTERACTION WITH ANNEXIN
RP 2/ANXA2.
RX PubMed=28669632; DOI=10.1016/j.str.2017.06.001;
RA Ecsedi P., Kiss B., Gogl G., Radnai L., Buday L., Koprivanacz K.,
RA Liliom K., Leveles I., Vertessy B., Jeszenoi N., Hetenyi C., Schlosser G.,
RA Katona G., Nyitray L.;
RT "Regulation of the Equilibrium between Closed and Open Conformations of
RT Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding.";
RL Structure 25:1195-1207.e5(2017).
RN [23] {ECO:0007744|PDB:6T58}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-93, AND INTERACTION WITH TP53.
RX PubMed=32442400; DOI=10.1016/j.str.2020.05.001;
RA Ecsedi P., Gogl G., Hof H., Kiss B., Harmat V., Nyitray L.;
RT "Structure Determination of the Transactivation Domain of p53 in Complex
RT with S100A4Using Annexin A2 as a Crystallization Chaperone.";
RL Structure 28:943-953.e4(2020).
CC -!- FUNCTION: Calcium-binding protein that plays a role in various cellular
CC processes including motility, angiogenesis, cell differentiation,
CC apoptosis, and autophagy (PubMed:16707441, PubMed:23752197,
CC PubMed:30713770). Increases cell motility and invasiveness by
CC interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9
CC (PubMed:16707441). Mechanistically, promotes filament depolymerization
CC and increases the amount of soluble myosin-IIA, resulting in the
CC formation of stable protrusions facilitating chemotaxis (By
CC similarity). Modulates also the pro-apoptotic function of TP53 by
CC binding to its C-terminal transactivation domain within the nucleus and
CC reducing its protein levels (PubMed:23752197). Within the extracellular
CC space, stimulates cytokine production including granulocyte colony-
CC stimulating factor and CCL24 from T-lymphocytes (By similarity). In
CC addition, stimulates T-lymphocyte chemotaxis by acting as a
CC chemoattractant complex with PGLYRP1 that promotes lymphocyte migration
CC via CCR5 and CXCR3 receptors (PubMed:30713770, PubMed:26654597).
CC {ECO:0000250|UniProtKB:P07091, ECO:0000269|PubMed:16707441,
CC ECO:0000269|PubMed:23752197, ECO:0000269|PubMed:26654597,
CC ECO:0000269|PubMed:30713770}.
CC -!- SUBUNIT: Homodimer. Interacts with PPFIBP1 in a calcium-dependent mode
CC (PubMed:11836260). Interacts with PGLYRP1; this complex acts as a
CC chemoattractant that promotes lymphocyte movement (PubMed:30713770,
CC PubMed:26654597). Interacts with MYH9; this interaction increases cell
CC motility (PubMed:16707441). Interacts with Annexin 2/ANXA2
CC (PubMed:28669632). Interacts with TP53; this interaction promotes TP53
CC degradation (PubMed:23752197, PubMed:32442400). Interacts with CCR5
CC (PubMed:30713770). Interacts with FCGR3A; this interaction inhibits
CC PKC-dependent phosphorylation of FCGR3A. {ECO:0000269|PubMed:11836260,
CC ECO:0000269|PubMed:16707441, ECO:0000269|PubMed:23024279,
CC ECO:0000269|PubMed:23752197, ECO:0000269|PubMed:26654597,
CC ECO:0000269|PubMed:28669632, ECO:0000269|PubMed:30713770,
CC ECO:0000269|PubMed:32442400}.
CC -!- INTERACTION:
CC P26447; P15514: AREG; NbExp=5; IntAct=EBI-717058, EBI-953674;
CC P26447; P35070: BTC; NbExp=2; IntAct=EBI-717058, EBI-6590057;
CC P26447; Q9HB71: CACYBP; NbExp=2; IntAct=EBI-717058, EBI-1047302;
CC P26447; P00533: EGFR; NbExp=6; IntAct=EBI-717058, EBI-297353;
CC P26447; P21860: ERBB3; NbExp=4; IntAct=EBI-717058, EBI-720706;
CC P26447; Q15303: ERBB4; NbExp=4; IntAct=EBI-717058, EBI-80371;
CC P26447; P15311: EZR; NbExp=3; IntAct=EBI-717058, EBI-1056902;
CC P26447; Q00987: MDM2; NbExp=3; IntAct=EBI-717058, EBI-389668;
CC P26447; P35579: MYH9; NbExp=18; IntAct=EBI-717058, EBI-350338;
CC P26447; P23297: S100A1; NbExp=4; IntAct=EBI-717058, EBI-743686;
CC P26447; P26447: S100A4; NbExp=6; IntAct=EBI-717058, EBI-717058;
CC P26447; P04271: S100B; NbExp=8; IntAct=EBI-717058, EBI-458391;
CC P26447; P04637: TP53; NbExp=9; IntAct=EBI-717058, EBI-366083;
CC P26447; Q8TD43: TRPM4; NbExp=2; IntAct=EBI-717058, EBI-11723041;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26654597,
CC ECO:0000269|PubMed:30713770}. Nucleus {ECO:0000269|PubMed:23752197}.
CC Cytoplasm {ECO:0000250|UniProtKB:P07091}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/S100A4ID42192ch1q21.html";
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DR EMBL; M80563; AAA51920.1; -; mRNA.
DR EMBL; Z18950; CAA79474.1; -; Genomic_DNA.
DR EMBL; Z33457; CAA83880.1; -; Genomic_DNA.
DR EMBL; CR450345; CAG29341.1; -; mRNA.
DR EMBL; AK292083; BAF84772.1; -; mRNA.
DR EMBL; BX470102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53310.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53311.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53312.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53313.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53314.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53315.1; -; Genomic_DNA.
DR EMBL; BC000838; AAH00838.1; -; mRNA.
DR EMBL; BC016300; AAH16300.1; -; mRNA.
DR CCDS; CCDS1042.1; -.
DR PIR; A48219; A48219.
DR RefSeq; NP_002952.1; NM_002961.2.
DR RefSeq; NP_062427.1; NM_019554.2.
DR PDB; 1M31; NMR; -; A/B=1-101.
DR PDB; 2LNK; NMR; -; A/B=1-101.
DR PDB; 2MRD; NMR; -; A/B=1-101.
DR PDB; 2Q91; X-ray; 1.63 A; A/B=1-101.
DR PDB; 3C1V; X-ray; 1.50 A; A/B/C/D=1-101.
DR PDB; 3CGA; X-ray; 2.03 A; A/B=1-101.
DR PDB; 3KO0; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-101.
DR PDB; 3M0W; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J=2-101.
DR PDB; 3ZWH; X-ray; 1.94 A; A/B=1-101.
DR PDB; 4CFQ; X-ray; 1.37 A; A/B/C/D=1-88.
DR PDB; 4CFR; X-ray; 1.40 A; A/B=1-101.
DR PDB; 4ETO; X-ray; 1.54 A; A/B=1-93.
DR PDB; 4HSZ; X-ray; 2.25 A; A/B/C/D=1-93.
DR PDB; 5LPU; X-ray; 2.10 A; C/D=1-101.
DR PDB; 6T58; X-ray; 3.10 A; A/B=1-93.
DR PDBsum; 1M31; -.
DR PDBsum; 2LNK; -.
DR PDBsum; 2MRD; -.
DR PDBsum; 2Q91; -.
DR PDBsum; 3C1V; -.
DR PDBsum; 3CGA; -.
DR PDBsum; 3KO0; -.
DR PDBsum; 3M0W; -.
DR PDBsum; 3ZWH; -.
DR PDBsum; 4CFQ; -.
DR PDBsum; 4CFR; -.
DR PDBsum; 4ETO; -.
DR PDBsum; 4HSZ; -.
DR PDBsum; 5LPU; -.
DR PDBsum; 6T58; -.
DR AlphaFoldDB; P26447; -.
DR BMRB; P26447; -.
DR SASBDB; P26447; -.
DR SMR; P26447; -.
DR BioGRID; 112183; 149.
DR DIP; DIP-44938N; -.
DR IntAct; P26447; 61.
DR MINT; P26447; -.
DR STRING; 9606.ENSP00000357705; -.
DR ChEMBL; CHEMBL2362976; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB00831; Trifluoperazine.
DR iPTMnet; P26447; -.
DR MetOSite; P26447; -.
DR PhosphoSitePlus; P26447; -.
DR BioMuta; S100A4; -.
DR DMDM; 115601; -.
DR DOSAC-COBS-2DPAGE; P26447; -.
DR SWISS-2DPAGE; P26447; -.
DR EPD; P26447; -.
DR jPOST; P26447; -.
DR MassIVE; P26447; -.
DR MaxQB; P26447; -.
DR PaxDb; P26447; -.
DR PeptideAtlas; P26447; -.
DR PRIDE; P26447; -.
DR ProteomicsDB; 54351; -.
DR TopDownProteomics; P26447; -.
DR Antibodypedia; 1551; 892 antibodies from 45 providers.
DR CPTC; P26447; 3 antibodies.
DR DNASU; 6275; -.
DR Ensembl; ENST00000354332.8; ENSP00000346294.4; ENSG00000196154.12.
DR Ensembl; ENST00000368714.1; ENSP00000357703.1; ENSG00000196154.12.
DR Ensembl; ENST00000368715.5; ENSP00000357704.1; ENSG00000196154.12.
DR Ensembl; ENST00000368716.9; ENSP00000357705.4; ENSG00000196154.12.
DR GeneID; 6275; -.
DR KEGG; hsa:6275; -.
DR MANE-Select; ENST00000368716.9; ENSP00000357705.4; NM_002961.3; NP_002952.1.
DR UCSC; uc001fby.4; human.
DR CTD; 6275; -.
DR DisGeNET; 6275; -.
DR GeneCards; S100A4; -.
DR HGNC; HGNC:10494; S100A4.
DR HPA; ENSG00000196154; Tissue enhanced (bone).
DR MIM; 114210; gene.
DR neXtProt; NX_P26447; -.
DR OpenTargets; ENSG00000196154; -.
DR PharmGKB; PA34906; -.
DR VEuPathDB; HostDB:ENSG00000196154; -.
DR eggNOG; ENOG502S4AU; Eukaryota.
DR GeneTree; ENSGT00940000161276; -.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; P26447; -.
DR OMA; QDLPDKM; -.
DR OrthoDB; 1560865at2759; -.
DR PhylomeDB; P26447; -.
DR TreeFam; TF332727; -.
DR PathwayCommons; P26447; -.
DR SignaLink; P26447; -.
DR SIGNOR; P26447; -.
DR BioGRID-ORCS; 6275; 12 hits in 1083 CRISPR screens.
DR ChiTaRS; S100A4; human.
DR EvolutionaryTrace; P26447; -.
DR GeneWiki; S100A4; -.
DR GenomeRNAi; 6275; -.
DR Pharos; P26447; Tchem.
DR PRO; PR:P26447; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P26447; protein.
DR Bgee; ENSG00000196154; Expressed in synovial joint and 197 other tissues.
DR Genevisible; P26447; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; 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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0050786; F:RAGE receptor binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; TAS:HGNC-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
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 3D-structure; Acetylation; Calcium; Cytoplasm; Direct protein sequencing;
KW Metal-binding; Nucleus; 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_0000143977"
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 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:4CFQ"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:4CFQ"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:2MRD"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:4CFQ"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:4CFQ"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6T58"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:4CFQ"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1M31"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:4CFQ"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:4CFQ"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:3C1V"
SQ SEQUENCE 101 AA; 11729 MW; 286D2B7B07EDB562 CRC64;
MACPLEKALD VMVSTFHKYS GKEGDKFKLN KSELKELLTR ELPSFLGKRT DEAAFQKLMS
NLDSNRDNEV DFQEYCVFLS CIAMMCNEFF EGFPDKQPRK K
