Full text data of S100A4
S100A4
(CAPL, MTS1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Protein S100-A4 (Calvasculin; Metastasin; Placental calcium-binding protein; Protein Mts1; S100 calcium-binding protein A4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein S100-A4 (Calvasculin; Metastasin; Placental calcium-binding protein; Protein Mts1; S100 calcium-binding protein A4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00032313
IPI00032313 S100 calcium-binding protein A4 ubiquitous, Homodimer. Interacts with PPFIBP1 in a calcium-dependent mode soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00032313 S100 calcium-binding protein A4 ubiquitous, Homodimer. Interacts with PPFIBP1 in a calcium-dependent mode soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P26447
ID S10A4_HUMAN Reviewed; 101 AA.
AC P26447; A8K7R8; D3DV46; Q6ICP8;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1992, sequence version 1.
DT 22-JAN-2014, entry version 141.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT of 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
RT of two genes coding for the two previously unreported calcium-binding
RT proteins 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
RT 5' 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-7 AND LYS-35, MASS
RP SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [12]
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.,
RA Buerckstuemmer T., 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 [13]
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).
CC -!- SUBUNIT: Homodimer. Interacts with PPFIBP1 in a calcium-dependent
CC mode.
CC -!- INTERACTION:
CC P15514:AREGB; NbExp=4; IntAct=EBI-717058, EBI-953674;
CC P35070:BTC; NbExp=2; IntAct=EBI-717058, EBI-6590057;
CC Q00987:MDM2; NbExp=3; IntAct=EBI-717058, EBI-389668;
CC P04637:TP53; NbExp=3; IntAct=EBI-717058, EBI-366083;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- SIMILARITY: Belongs to the S-100 family.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and 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; CAI14754.1; -; 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 PIR; A48219; A48219.
DR RefSeq; NP_002952.1; NM_002961.2.
DR RefSeq; NP_062427.1; NM_019554.2.
DR RefSeq; XP_005245484.1; XM_005245427.1.
DR RefSeq; XP_005245485.1; XM_005245428.1.
DR UniGene; Hs.654444; -.
DR PDB; 1M31; NMR; -; A/B=1-101.
DR PDB; 2LNK; 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; 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 PDBsum; 1M31; -.
DR PDBsum; 2LNK; -.
DR PDBsum; 2Q91; -.
DR PDBsum; 3C1V; -.
DR PDBsum; 3CGA; -.
DR PDBsum; 3KO0; -.
DR PDBsum; 3M0W; -.
DR PDBsum; 3ZWH; -.
DR PDBsum; 4ETO; -.
DR PDBsum; 4HSZ; -.
DR ProteinModelPortal; P26447; -.
DR SMR; P26447; 2-98.
DR DIP; DIP-44938N; -.
DR IntAct; P26447; 11.
DR MINT; MINT-1372269; -.
DR STRING; 9606.ENSP00000346294; -.
DR ChEMBL; CHEMBL2362976; -.
DR PhosphoSite; P26447; -.
DR DMDM; 115601; -.
DR DOSAC-COBS-2DPAGE; P26447; -.
DR SWISS-2DPAGE; P26447; -.
DR PaxDb; P26447; -.
DR PeptideAtlas; P26447; -.
DR PRIDE; P26447; -.
DR DNASU; 6275; -.
DR Ensembl; ENST00000354332; ENSP00000346294; ENSG00000196154.
DR Ensembl; ENST00000368714; ENSP00000357703; ENSG00000196154.
DR Ensembl; ENST00000368715; ENSP00000357704; ENSG00000196154.
DR Ensembl; ENST00000368716; ENSP00000357705; ENSG00000196154.
DR GeneID; 6275; -.
DR KEGG; hsa:6275; -.
DR UCSC; uc001fby.3; human.
DR CTD; 6275; -.
DR GeneCards; GC01M153517; -.
DR HGNC; HGNC:10494; S100A4.
DR HPA; CAB002618; -.
DR HPA; CAB027387; -.
DR HPA; CAB058698; -.
DR HPA; HPA007973; -.
DR MIM; 114210; gene.
DR neXtProt; NX_P26447; -.
DR PharmGKB; PA34906; -.
DR eggNOG; NOG40931; -.
DR HOGENOM; HOG000246968; -.
DR HOVERGEN; HBG001479; -.
DR InParanoid; P26447; -.
DR OMA; NEFFEGC; -.
DR OrthoDB; EOG7R833W; -.
DR PhylomeDB; P26447; -.
DR ChiTaRS; S100A4; human.
DR EvolutionaryTrace; P26447; -.
DR GeneWiki; S100A4; -.
DR GenomeRNAi; 6275; -.
DR NextBio; 24355; -.
DR PRO; PR:P26447; -.
DR Bgee; P26447; -.
DR CleanEx; HS_S100A4; -.
DR Genevestigator; P26447; -.
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:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; TAS:HGNC.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IDA:UniProtKB.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028496; S100-A2/S100-A4.
DR InterPro; IPR001751; S100/CaBP-9k_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF15; PTHR11639:SF15; 1.
DR Pfam; PF01023; S_100; 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; Complete proteome;
KW Direct protein sequencing; Metal-binding; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 101 Protein S100-A4.
FT /FTId=PRO_0000143977.
FT DOMAIN 12 47 EF-hand 1.
FT DOMAIN 50 85 EF-hand 2.
FT CA_BIND 20 33 1; low affinity (Potential).
FT CA_BIND 63 74 2; high affinity (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 7 7 N6-acetyllysine.
FT MOD_RES 35 35 N6-acetyllysine.
FT HELIX 4 20
FT STRAND 22 25
FT HELIX 31 41
FT HELIX 43 46
FT HELIX 52 62
FT STRAND 64 66
FT STRAND 67 71
FT HELIX 72 88
FT TURN 89 91
SQ SEQUENCE 101 AA; 11729 MW; 286D2B7B07EDB562 CRC64;
MACPLEKALD VMVSTFHKYS GKEGDKFKLN KSELKELLTR ELPSFLGKRT DEAAFQKLMS
NLDSNRDNEV DFQEYCVFLS CIAMMCNEFF EGFPDKQPRK K
//
ID S10A4_HUMAN Reviewed; 101 AA.
AC P26447; A8K7R8; D3DV46; Q6ICP8;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1992, sequence version 1.
DT 22-JAN-2014, entry version 141.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT of 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
RT of two genes coding for the two previously unreported calcium-binding
RT proteins 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
RT 5' 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-7 AND LYS-35, MASS
RP SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [12]
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.,
RA Buerckstuemmer T., 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 [13]
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).
CC -!- SUBUNIT: Homodimer. Interacts with PPFIBP1 in a calcium-dependent
CC mode.
CC -!- INTERACTION:
CC P15514:AREGB; NbExp=4; IntAct=EBI-717058, EBI-953674;
CC P35070:BTC; NbExp=2; IntAct=EBI-717058, EBI-6590057;
CC Q00987:MDM2; NbExp=3; IntAct=EBI-717058, EBI-389668;
CC P04637:TP53; NbExp=3; IntAct=EBI-717058, EBI-366083;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- SIMILARITY: Belongs to the S-100 family.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/S100A4ID42192ch1q21.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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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; CAI14754.1; -; 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 PIR; A48219; A48219.
DR RefSeq; NP_002952.1; NM_002961.2.
DR RefSeq; NP_062427.1; NM_019554.2.
DR RefSeq; XP_005245484.1; XM_005245427.1.
DR RefSeq; XP_005245485.1; XM_005245428.1.
DR UniGene; Hs.654444; -.
DR PDB; 1M31; NMR; -; A/B=1-101.
DR PDB; 2LNK; 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; 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 PDBsum; 1M31; -.
DR PDBsum; 2LNK; -.
DR PDBsum; 2Q91; -.
DR PDBsum; 3C1V; -.
DR PDBsum; 3CGA; -.
DR PDBsum; 3KO0; -.
DR PDBsum; 3M0W; -.
DR PDBsum; 3ZWH; -.
DR PDBsum; 4ETO; -.
DR PDBsum; 4HSZ; -.
DR ProteinModelPortal; P26447; -.
DR SMR; P26447; 2-98.
DR DIP; DIP-44938N; -.
DR IntAct; P26447; 11.
DR MINT; MINT-1372269; -.
DR STRING; 9606.ENSP00000346294; -.
DR ChEMBL; CHEMBL2362976; -.
DR PhosphoSite; P26447; -.
DR DMDM; 115601; -.
DR DOSAC-COBS-2DPAGE; P26447; -.
DR SWISS-2DPAGE; P26447; -.
DR PaxDb; P26447; -.
DR PeptideAtlas; P26447; -.
DR PRIDE; P26447; -.
DR DNASU; 6275; -.
DR Ensembl; ENST00000354332; ENSP00000346294; ENSG00000196154.
DR Ensembl; ENST00000368714; ENSP00000357703; ENSG00000196154.
DR Ensembl; ENST00000368715; ENSP00000357704; ENSG00000196154.
DR Ensembl; ENST00000368716; ENSP00000357705; ENSG00000196154.
DR GeneID; 6275; -.
DR KEGG; hsa:6275; -.
DR UCSC; uc001fby.3; human.
DR CTD; 6275; -.
DR GeneCards; GC01M153517; -.
DR HGNC; HGNC:10494; S100A4.
DR HPA; CAB002618; -.
DR HPA; CAB027387; -.
DR HPA; CAB058698; -.
DR HPA; HPA007973; -.
DR MIM; 114210; gene.
DR neXtProt; NX_P26447; -.
DR PharmGKB; PA34906; -.
DR eggNOG; NOG40931; -.
DR HOGENOM; HOG000246968; -.
DR HOVERGEN; HBG001479; -.
DR InParanoid; P26447; -.
DR OMA; NEFFEGC; -.
DR OrthoDB; EOG7R833W; -.
DR PhylomeDB; P26447; -.
DR ChiTaRS; S100A4; human.
DR EvolutionaryTrace; P26447; -.
DR GeneWiki; S100A4; -.
DR GenomeRNAi; 6275; -.
DR NextBio; 24355; -.
DR PRO; PR:P26447; -.
DR Bgee; P26447; -.
DR CleanEx; HS_S100A4; -.
DR Genevestigator; P26447; -.
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:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; TAS:HGNC.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IDA:UniProtKB.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028496; S100-A2/S100-A4.
DR InterPro; IPR001751; S100/CaBP-9k_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF15; PTHR11639:SF15; 1.
DR Pfam; PF01023; S_100; 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; Complete proteome;
KW Direct protein sequencing; Metal-binding; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 101 Protein S100-A4.
FT /FTId=PRO_0000143977.
FT DOMAIN 12 47 EF-hand 1.
FT DOMAIN 50 85 EF-hand 2.
FT CA_BIND 20 33 1; low affinity (Potential).
FT CA_BIND 63 74 2; high affinity (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 7 7 N6-acetyllysine.
FT MOD_RES 35 35 N6-acetyllysine.
FT HELIX 4 20
FT STRAND 22 25
FT HELIX 31 41
FT HELIX 43 46
FT HELIX 52 62
FT STRAND 64 66
FT STRAND 67 71
FT HELIX 72 88
FT TURN 89 91
SQ SEQUENCE 101 AA; 11729 MW; 286D2B7B07EDB562 CRC64;
MACPLEKALD VMVSTFHKYS GKEGDKFKLN KSELKELLTR ELPSFLGKRT DEAAFQKLMS
NLDSNRDNEV DFQEYCVFLS CIAMMCNEFF EGFPDKQPRK K
//
MIM
114210
*RECORD*
*FIELD* NO
114210
*FIELD* TI
*114210 S100 CALCIUM-BINDING PROTEIN A4; S100A4
;;CALCIUM PLACENTAL PROTEIN; CAPL;;
read moreFIBROBLAST-SPECIFIC PROTEIN 1; FSP1
*FIELD* TX
DESCRIPTION
S100 proteins, such as S100A4, are small, acidic calcium-binding
proteins that transduce Ca(2+)-signals via interaction with
intracellular target proteins (Mandinova et al., 1998).
CLONING
Engelkamp et al. (1992) cloned S100A4, which they called CAPL, from a
human heart cDNA library. The deduced 101-amino acid protein has the
domain structure of an S100 protein, with N- and C-terminal hydrophobic
regions and 2 central calcium loops. Northern blot analysis detected
ubiquitous expression of a 650-bp transcript, with highest expression in
thymus, lung, and heart.
Ambartsumian et al. (1995) described 2 alternative splice variants of
S100A4 that differ in their 5-prime untranslated regions.
Using immunofluorescence analysis and confocal laser scanning
microscopy, Mandinova et al. (1998) showed that S100A1 (176940), S100A2
(176993), S100A4, and S100A6 (114110) localized to distinct
intracellular compartments in cultured human vascular and intestinal
smooth muscle cells. S100A1 and S100A4 were associated predominantly
with the sarcoplasmic reticulum and with actin stress fibers.
GENE FUNCTION
Mandinova et al. (1998) showed that elevated cytosolic Ca(2+) led to
relocalization of S100A1, S100A4, and S100A6 from sarcoplasmic reticulum
to vesicle-like structures around the nucleus in human vascular smooth
muscle cells. The localization of stress fiber-associated S100A1 and
S100A4 remained unchanged.
Fernandez-Fernandez et al. (2005) found that S100B (176990) and S100A4
bound the C-terminal tetramerization domain of p53 (191170) when the
domain was exposed in lower oligomerization states, disrupting p53
tetramerization. S100B bound to the negative regulatory and nuclear
localization domains of p53, resulting in very tight binding. Because
trafficking of p53 depends on its oligomerization state,
Fernandez-Fernandez et al. (2005) proposed that S100B and S100A4 may
regulate subcellular localization of p53 but with different effects on
p53 function in cell cycle control due to their differences in binding
p53.
GENE STRUCTURE
Ambartsumian et al. (1995) showed that the S100A4 gene consists of 4
exons.
MAPPING
Jackson-Grusby et al. (1987) isolated a probe for the mouse placental
protein for which the human equivalent was symbolized CAPL by van
Heyningen et al. (1989). By Southern blot analysis of DNAs from somatic
cell hybrids, van Heyningen et al. (1989) and Dorin et al. (1990) showed
that the CAPL gene in man cosegregates with CAGA (123885), CAGB
(123886), and calcyclin (114110). In the hands of van Heyningen et al.
(1989), Southern blot analysis of DNA from BxD recombinant inbred strain
mice showed a TaqI polymorphism for CAPL probe 18A2 to distinguish the
parental strains. CAPL cosegregated in the BxD mice with a fifth member
of this gene family, the p11 protein (mouse symbol Cal11) which had been
mapped to chromosome 3 by Saris et al. (1987). In the mouse Capl is
within 8 kb of Cacy; thus, by homology, the CAPL gene in man is probably
in region 1q21-q25 where the CACY gene has been mapped.
Schafer et al. (1995) isolated a YAC clone from the 1q21 region on which
9 different genes coding for S100 calcium-binding proteins could be
localized. The clustered organization of S100 genes allowed introduction
of a new logical nomenclature based on their physical arrangement on the
chromosome, with S100A1 (176940) being closest to the telomere and
S100A9 being closest to the centromere. In this revised nomenclature,
CAPL became S100A4.
*FIELD* RF
1. Ambartsumian, N.; Tarabykina, S.; Grigorian, M.; Tulchinsky, E.;
Hulgaard, E.; Georgiev, G.; Lukanidin, E.: Characterization of two
splice variants of metastasis-associated human mts1 gene. Gene 159:
125-130, 1995.
2. Dorin, J. R.; Emslie, E.; van Heyningen, V.: Related calcium-binding
proteins map to the same subregion of chromosome 1q and to an extended
region of synteny on mouse chromosome 3. Genomics 8: 420-426, 1990.
3. Engelkamp, D.; Schafer, B. W.; Erne, P.; Heizmann, C. W.: S100-alpha,
CAPL, and CACY: molecular cloning and expression analysis of three
calcium-binding proteins from human heart. Biochemistry 31: 10258-10264,
1992.
4. Fernandez-Fernandez, M. R.; Veprintsev, D. B.; Fersht, A. R.:
Proteins of the S100 family regulate the oligomerization of p53 tumor
suppressor. Proc. Nat. Acad. Sci. 102: 4735-4740, 2005.
5. Jackson-Grusby, L. L.; Swiergiel, J.; Linzer, D. I.: A growth-related
mRNA in cultured mouse cells encodes a placental calcium binding protein. Nucleic
Acids Res. 15: 6677-6690, 1987.
6. Mandinova, A.; Atar, D.; Schafer, B. W.; Spiess, M.; Aebi, U.;
Heizmann, C. W.: Distinct subcellular localization of calcium binding
S100 proteins in human smooth muscle cells and their relocation in
response to rises in intracellular calcium. J. Cell Sci. 111: 2043-2054,
1998.
7. Saris, C. J.; Kristensen, T.; D'Eustachio, P.; Hicks, L. J.; Noonan,
D. J.; Hunter, T.; Tack, B. F.: cDNA sequence and tissue distribution
of the mRNA for bovine and murine p11, the S100-related light chain
of the protein-tyrosine kinase substrate p36 (calpactin I). J. Biol.
Chem. 262: 10663-10671, 1987.
8. Schafer, B. W.; Wicki, R.; Engelkamp, D.; Mattei, M.-G.; Heizmann,
C. W.: Isolation of a YAC clone covering a cluster of nine S100 genes
on human chromosome 1q21: rationale for a new nomenclature of the
S100 calcium-binding protein family. Genomics 25: 638-643, 1995.
9. van Heyningen, V.; Emslie, E.; Dorin, J. R.: Related calcium binding
proteins map to the same sub-region of chromosome 1q and to an extended
region of synteny on mouse chromosome 3. (Abstract) Cytogenet. Cell
Genet. 51: 1095, 1989.
*FIELD* CN
Patricia A. Hartz - updated: 7/17/2009
Patricia A. Hartz - updated: 10/17/2006
Alan F. Scott - updated: 12/7/1995
*FIELD* CD
Victor A. McKusick: 6/2/1989
*FIELD* ED
mgross: 08/19/2009
terry: 7/17/2009
mgross: 6/17/2008
wwang: 10/19/2006
terry: 10/17/2006
mark: 4/22/1996
mark: 6/15/1995
carol: 1/23/1995
supermim: 3/16/1992
carol: 12/4/1990
carol: 12/3/1990
carol: 11/28/1990
*RECORD*
*FIELD* NO
114210
*FIELD* TI
*114210 S100 CALCIUM-BINDING PROTEIN A4; S100A4
;;CALCIUM PLACENTAL PROTEIN; CAPL;;
read moreFIBROBLAST-SPECIFIC PROTEIN 1; FSP1
*FIELD* TX
DESCRIPTION
S100 proteins, such as S100A4, are small, acidic calcium-binding
proteins that transduce Ca(2+)-signals via interaction with
intracellular target proteins (Mandinova et al., 1998).
CLONING
Engelkamp et al. (1992) cloned S100A4, which they called CAPL, from a
human heart cDNA library. The deduced 101-amino acid protein has the
domain structure of an S100 protein, with N- and C-terminal hydrophobic
regions and 2 central calcium loops. Northern blot analysis detected
ubiquitous expression of a 650-bp transcript, with highest expression in
thymus, lung, and heart.
Ambartsumian et al. (1995) described 2 alternative splice variants of
S100A4 that differ in their 5-prime untranslated regions.
Using immunofluorescence analysis and confocal laser scanning
microscopy, Mandinova et al. (1998) showed that S100A1 (176940), S100A2
(176993), S100A4, and S100A6 (114110) localized to distinct
intracellular compartments in cultured human vascular and intestinal
smooth muscle cells. S100A1 and S100A4 were associated predominantly
with the sarcoplasmic reticulum and with actin stress fibers.
GENE FUNCTION
Mandinova et al. (1998) showed that elevated cytosolic Ca(2+) led to
relocalization of S100A1, S100A4, and S100A6 from sarcoplasmic reticulum
to vesicle-like structures around the nucleus in human vascular smooth
muscle cells. The localization of stress fiber-associated S100A1 and
S100A4 remained unchanged.
Fernandez-Fernandez et al. (2005) found that S100B (176990) and S100A4
bound the C-terminal tetramerization domain of p53 (191170) when the
domain was exposed in lower oligomerization states, disrupting p53
tetramerization. S100B bound to the negative regulatory and nuclear
localization domains of p53, resulting in very tight binding. Because
trafficking of p53 depends on its oligomerization state,
Fernandez-Fernandez et al. (2005) proposed that S100B and S100A4 may
regulate subcellular localization of p53 but with different effects on
p53 function in cell cycle control due to their differences in binding
p53.
GENE STRUCTURE
Ambartsumian et al. (1995) showed that the S100A4 gene consists of 4
exons.
MAPPING
Jackson-Grusby et al. (1987) isolated a probe for the mouse placental
protein for which the human equivalent was symbolized CAPL by van
Heyningen et al. (1989). By Southern blot analysis of DNAs from somatic
cell hybrids, van Heyningen et al. (1989) and Dorin et al. (1990) showed
that the CAPL gene in man cosegregates with CAGA (123885), CAGB
(123886), and calcyclin (114110). In the hands of van Heyningen et al.
(1989), Southern blot analysis of DNA from BxD recombinant inbred strain
mice showed a TaqI polymorphism for CAPL probe 18A2 to distinguish the
parental strains. CAPL cosegregated in the BxD mice with a fifth member
of this gene family, the p11 protein (mouse symbol Cal11) which had been
mapped to chromosome 3 by Saris et al. (1987). In the mouse Capl is
within 8 kb of Cacy; thus, by homology, the CAPL gene in man is probably
in region 1q21-q25 where the CACY gene has been mapped.
Schafer et al. (1995) isolated a YAC clone from the 1q21 region on which
9 different genes coding for S100 calcium-binding proteins could be
localized. The clustered organization of S100 genes allowed introduction
of a new logical nomenclature based on their physical arrangement on the
chromosome, with S100A1 (176940) being closest to the telomere and
S100A9 being closest to the centromere. In this revised nomenclature,
CAPL became S100A4.
*FIELD* RF
1. Ambartsumian, N.; Tarabykina, S.; Grigorian, M.; Tulchinsky, E.;
Hulgaard, E.; Georgiev, G.; Lukanidin, E.: Characterization of two
splice variants of metastasis-associated human mts1 gene. Gene 159:
125-130, 1995.
2. Dorin, J. R.; Emslie, E.; van Heyningen, V.: Related calcium-binding
proteins map to the same subregion of chromosome 1q and to an extended
region of synteny on mouse chromosome 3. Genomics 8: 420-426, 1990.
3. Engelkamp, D.; Schafer, B. W.; Erne, P.; Heizmann, C. W.: S100-alpha,
CAPL, and CACY: molecular cloning and expression analysis of three
calcium-binding proteins from human heart. Biochemistry 31: 10258-10264,
1992.
4. Fernandez-Fernandez, M. R.; Veprintsev, D. B.; Fersht, A. R.:
Proteins of the S100 family regulate the oligomerization of p53 tumor
suppressor. Proc. Nat. Acad. Sci. 102: 4735-4740, 2005.
5. Jackson-Grusby, L. L.; Swiergiel, J.; Linzer, D. I.: A growth-related
mRNA in cultured mouse cells encodes a placental calcium binding protein. Nucleic
Acids Res. 15: 6677-6690, 1987.
6. Mandinova, A.; Atar, D.; Schafer, B. W.; Spiess, M.; Aebi, U.;
Heizmann, C. W.: Distinct subcellular localization of calcium binding
S100 proteins in human smooth muscle cells and their relocation in
response to rises in intracellular calcium. J. Cell Sci. 111: 2043-2054,
1998.
7. Saris, C. J.; Kristensen, T.; D'Eustachio, P.; Hicks, L. J.; Noonan,
D. J.; Hunter, T.; Tack, B. F.: cDNA sequence and tissue distribution
of the mRNA for bovine and murine p11, the S100-related light chain
of the protein-tyrosine kinase substrate p36 (calpactin I). J. Biol.
Chem. 262: 10663-10671, 1987.
8. Schafer, B. W.; Wicki, R.; Engelkamp, D.; Mattei, M.-G.; Heizmann,
C. W.: Isolation of a YAC clone covering a cluster of nine S100 genes
on human chromosome 1q21: rationale for a new nomenclature of the
S100 calcium-binding protein family. Genomics 25: 638-643, 1995.
9. van Heyningen, V.; Emslie, E.; Dorin, J. R.: Related calcium binding
proteins map to the same sub-region of chromosome 1q and to an extended
region of synteny on mouse chromosome 3. (Abstract) Cytogenet. Cell
Genet. 51: 1095, 1989.
*FIELD* CN
Patricia A. Hartz - updated: 7/17/2009
Patricia A. Hartz - updated: 10/17/2006
Alan F. Scott - updated: 12/7/1995
*FIELD* CD
Victor A. McKusick: 6/2/1989
*FIELD* ED
mgross: 08/19/2009
terry: 7/17/2009
mgross: 6/17/2008
wwang: 10/19/2006
terry: 10/17/2006
mark: 4/22/1996
mark: 6/15/1995
carol: 1/23/1995
supermim: 3/16/1992
carol: 12/4/1990
carol: 12/3/1990
carol: 11/28/1990