S10A7_HUMAN
ID S10A7_HUMAN Reviewed; 101 AA.
AC P31151; Q5SY67; Q6FGE3; Q9H1E2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 4.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Protein S100-A7;
DE AltName: Full=Psoriasin;
DE AltName: Full=S100 calcium-binding protein A7;
GN Name=S100A7; Synonyms=PSOR1, S100A7C;
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], AND VARIANT ASP-28.
RC TISSUE=Keratinocyte;
RX PubMed=1940442; DOI=10.1111/1523-1747.ep12484041;
RA Madsen P., Rasmussen H.H., Leffers H., Honore B., Dejgaard K., Olsen E.,
RA Kiil J., Walbum E., Andersen A.H., Basse B., Lauridsen J.B., Ratz G.P.,
RA Celis A., Vandekerckhove J., Celis J.E.;
RT "Molecular cloning, occurrence, and expression of a novel partially
RT secreted protein 'psoriasin' that is highly up-regulated in psoriatic
RT skin.";
RL J. Invest. Dermatol. 97:701-712(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-28.
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-28.
RC TISSUE=Skin;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89, AND VARIANT ASP-28.
RA Glaeser R., Harder J., Christophers E., Schroeder J.M.;
RT "Genomic organization of human psoriasin (S100A7) gene.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 2-101, MASS SPECTROMETRY, AND ACETYLATION AT SER-2.
RC TISSUE=Psoriatic skin;
RX PubMed=8526920; DOI=10.1006/bbrc.1995.2772;
RA Burgisser D.M., Siegenthaler G., Kuster T., Hellman U., Hunziker P.,
RA Birchler N., Heizmann C.W.;
RT "Amino acid sequence analysis of human S100A7 (psoriasin) by tandem mass
RT spectrometry.";
RL Biochem. Biophys. Res. Commun. 217:257-263(1995).
RN [7]
RP PROTEIN SEQUENCE OF 9-19; 38-48; 50-61; 69-87 AND 89-101.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [8]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=8618345; DOI=10.1016/s0022-5347(01)66118-4;
RA Celis J.E., Rasmussen H.H., Vorum H., Madsen P., Honore B., Wolf H.,
RA Orntoft T.F.;
RT "Bladder squamous cell carcinomas express psoriasin and externalize it to
RT the urine.";
RL J. Urol. 155:2105-2112(1996).
RN [9]
RP INTERACTION WITH RANBP9.
RX PubMed=12421467; DOI=10.1186/1471-2407-2-28;
RA Emberley E.D., Gietz R.D., Campbell J.D., Hayglass K.T., Murphy L.C.,
RA Watson P.H.;
RT "RanBPM interacts with psoriasin in vitro and their expression correlates
RT with specific clinical features in vivo in breast cancer.";
RL BMC Cancer 2:28-28(2002).
RN [10]
RP GENOMIC ORGANIZATION.
RX PubMed=12664160; DOI=10.1007/s00239-002-2410-5;
RA Kulski J.K., Lim C.P., Dunn D.S., Bellgard M.;
RT "Genomic and phylogenetic analysis of the S100A7 (psoriasin) gene
RT duplications within the region of the S100 gene cluster on human chromosome
RT 1q21.";
RL J. Mol. Evol. 56:397-406(2003).
RN [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
RX PubMed=9562557; DOI=10.1016/s0969-2126(98)00049-5;
RA Brodersen D.E., Etzerodt M., Madsen P., Celis J.E., Thoegersen H.C.,
RA Nyborg J., Kjeldgaard M.;
RT "EF-hands at atomic resolution: the structure of human psoriasin (S100A7)
RT solved by MAD phasing.";
RL Structure 6:477-489(1998).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RX PubMed=10026247; DOI=10.1021/bi982483d;
RA Brodersen D.E., Nyborg J., Kjeldgaard M.;
RT "Zinc-binding site of an S100 protein revealed. Two crystal structures of
RT Ca2+-bound human psoriasin (S100A7) in the Zn2+-loaded and Zn2+-free
RT states.";
RL Biochemistry 38:1695-1704(1999).
CC -!- SUBUNIT: Interacts with RANBP9. {ECO:0000269|PubMed:12421467}.
CC -!- INTERACTION:
CC P31151; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-357520, EBI-12357161;
CC P31151; Q96S59: RANBP9; NbExp=3; IntAct=EBI-357520, EBI-636085;
CC P31151; Q5SY68: S100A7L2; NbExp=10; IntAct=EBI-357520, EBI-12006206;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8618345}. Secreted
CC {ECO:0000269|PubMed:8618345}. Note=Secreted by a non-classical
CC secretory pathway.
CC -!- TISSUE SPECIFICITY: Fetal ear, skin, and tongue and human cell lines.
CC Highly up-regulated in psoriatic epidermis. Also highly expressed in
CC the urine of bladder squamous cell carcinoma (SCC) bearing patients.
CC {ECO:0000269|PubMed:8618345}.
CC -!- MASS SPECTROMETRY: Mass=11365; Mass_error=0.7; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8526920};
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/S100A7ID42194ch1q21.html";
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DR EMBL; M86757; AAA60210.1; -; mRNA.
DR EMBL; CR542164; CAG46961.1; -; mRNA.
DR EMBL; AL591704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034687; AAH34687.1; -; mRNA.
DR EMBL; AJ012825; CAC20409.1; -; Genomic_DNA.
DR EMBL; BR000043; FAA00017.1; -; Genomic_DNA.
DR CCDS; CCDS1039.1; -.
DR PIR; A54327; A54327.
DR RefSeq; NP_002954.2; NM_002963.3.
DR PDB; 1PSR; X-ray; 1.05 A; A/B=2-101.
DR PDB; 2PSR; X-ray; 2.05 A; A=2-101.
DR PDB; 2WND; X-ray; 1.60 A; A=2-97.
DR PDB; 2WOR; X-ray; 1.70 A; A=2-101.
DR PDB; 2WOS; X-ray; 1.70 A; A=2-101.
DR PDB; 3PSR; X-ray; 2.50 A; A/B=2-101.
DR PDB; 4AQJ; X-ray; 1.60 A; A=1-101.
DR PDBsum; 1PSR; -.
DR PDBsum; 2PSR; -.
DR PDBsum; 2WND; -.
DR PDBsum; 2WOR; -.
DR PDBsum; 2WOS; -.
DR PDBsum; 3PSR; -.
DR PDBsum; 4AQJ; -.
DR AlphaFoldDB; P31151; -.
DR SMR; P31151; -.
DR BioGRID; 112186; 181.
DR IntAct; P31151; 55.
DR MINT; P31151; -.
DR STRING; 9606.ENSP00000357712; -.
DR DrugBank; DB04474; 8-anilinonaphthalene-1-sulfonic acid.
DR DrugBank; DB09213; Dexibuprofen.
DR DrugBank; DB01050; Ibuprofen.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR GlyGen; P31151; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P31151; -.
DR PhosphoSitePlus; P31151; -.
DR BioMuta; S100A7; -.
DR DMDM; 172046820; -.
DR UCD-2DPAGE; P31151; -.
DR EPD; P31151; -.
DR jPOST; P31151; -.
DR MassIVE; P31151; -.
DR MaxQB; P31151; -.
DR PaxDb; P31151; -.
DR PeptideAtlas; P31151; -.
DR PRIDE; P31151; -.
DR ProteomicsDB; 54761; -.
DR TopDownProteomics; P31151; -.
DR Antibodypedia; 1683; 592 antibodies from 42 providers.
DR CPTC; P31151; 1 antibody.
DR DNASU; 6278; -.
DR Ensembl; ENST00000368722.5; ENSP00000357711.1; ENSG00000143556.9.
DR Ensembl; ENST00000368723.4; ENSP00000357712.3; ENSG00000143556.9.
DR GeneID; 6278; -.
DR KEGG; hsa:6278; -.
DR MANE-Select; ENST00000368723.4; ENSP00000357712.3; NM_002963.4; NP_002954.2.
DR UCSC; uc001fbv.2; human.
DR CTD; 6278; -.
DR DisGeNET; 6278; -.
DR GeneCards; S100A7; -.
DR HGNC; HGNC:10497; S100A7.
DR HPA; ENSG00000143556; Group enriched (esophagus, lymphoid tissue, skin, vagina).
DR MIM; 600353; gene.
DR neXtProt; NX_P31151; -.
DR OpenTargets; ENSG00000143556; -.
DR PharmGKB; PA34909; -.
DR VEuPathDB; HostDB:ENSG00000143556; -.
DR eggNOG; ENOG502SZJ5; Eukaryota.
DR GeneTree; ENSGT00940000163488; -.
DR HOGENOM; CLU_138624_5_0_1; -.
DR InParanoid; P31151; -.
DR OMA; FHNDTRH; -.
DR OrthoDB; 1486203at2759; -.
DR PhylomeDB; P31151; -.
DR TreeFam; TF341148; -.
DR PathwayCommons; P31151; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6799990; Metal sequestration by antimicrobial proteins.
DR SignaLink; P31151; -.
DR BioGRID-ORCS; 6278; 8 hits in 1005 CRISPR screens.
DR EvolutionaryTrace; P31151; -.
DR GeneWiki; S100A7; -.
DR GenomeRNAi; 6278; -.
DR Pharos; P31151; Tbio.
DR PRO; PR:P31151; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P31151; protein.
DR Bgee; ENSG00000143556; Expressed in skin of abdomen and 90 other tissues.
DR Genevisible; P31151; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0050786; F:RAGE receptor binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; NAS:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; NAS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0071624; P:positive regulation of granulocyte chemotaxis; IDA:UniProtKB.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:UniProtKB.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; IDA:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:UniProtKB.
DR GO; GO:0000302; P:response to reactive oxygen species; IDA:UniProtKB.
DR GO; GO:0051238; P:sequestering of metal ion; 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; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028477; S100A7.
DR PANTHER; PTHR11639:SF128; PTHR11639:SF128; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Metal-binding; Reference proteome; Repeat; Secreted; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8526920"
FT CHAIN 2..101
FT /note="Protein S100-A7"
FT /id="PRO_0000143990"
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 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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_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_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_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_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:8526920"
FT DISULFID 47..96
FT VARIANT 28
FT /note="E -> D (in dbSNP:rs3014837)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:1940442, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.5"
FT /id="VAR_039118"
FT HELIX 5..19
FT /evidence="ECO:0007829|PDB:1PSR"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:1PSR"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:1PSR"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1PSR"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:1PSR"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2WND"
FT HELIX 72..89
FT /evidence="ECO:0007829|PDB:1PSR"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1PSR"
SQ SEQUENCE 101 AA; 11471 MW; 02C4CE39BF140971 CRC64;
MSNTQAERSI IGMIDMFHKY TRRDDKIEKP SLLTMMKENF PNFLSACDKK GTNYLADVFE
KKDKNEDKKI DFSEFLSLLG DIATDYHKQS HGAAPCSGGS Q
