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Protein S100-A7 (Psoriasin) (S100 calcium-binding protein A7)

 S10A7_HUMAN             Reviewed;         101 AA.
P31151; Q5SY67; Q6FGE3; Q9H1E2;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 4.
25-OCT-2017, entry version 178.
RecName: Full=Protein S100-A7;
AltName: Full=Psoriasin;
AltName: Full=S100 calcium-binding protein A7;
Name=S100A7; Synonyms=PSOR1, S100A7C;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-28.
TISSUE=Keratinocyte;
PubMed=1940442; DOI=10.1111/1523-1747.ep12484041;
Madsen P., Rasmussen H.H., Leffers H., Honore B., Dejgaard K.,
Olsen E., Kiil J., Walbum E., Andersen A.H., Basse B., Lauridsen J.B.,
Ratz G.P., Celis A., Vandekerckhove J., Celis J.E.;
"Molecular cloning, occurrence, and expression of a novel partially
secreted protein 'psoriasin' that is highly up-regulated in psoriatic
skin.";
J. Invest. Dermatol. 97:701-712(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-28.
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-28.
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89, AND VARIANT ASP-28.
Glaeser R., Harder J., Christophers E., Schroeder J.M.;
"Genomic organization of human psoriasin (S100A7) gene.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 2-101, MASS SPECTROMETRY, AND ACETYLATION AT
SER-2.
TISSUE=Psoriatic skin;
PubMed=8526920; DOI=10.1006/bbrc.1995.2772;
Burgisser D.M., Siegenthaler G., Kuster T., Hellman U., Hunziker P.,
Birchler N., Heizmann C.W.;
"Amino acid sequence analysis of human S100A7 (psoriasin) by tandem
mass spectrometry.";
Biochem. Biophys. Res. Commun. 217:257-263(1995).
[7]
PROTEIN SEQUENCE OF 9-19; 38-48; 50-61; 69-87 AND 89-101.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[8]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=8618345; DOI=10.1016/S0022-5347(01)66118-4;
Celis J.E., Rasmussen H.H., Vorum H., Madsen P., Honore B., Wolf H.,
Orntoft T.F.;
"Bladder squamous cell carcinomas express psoriasin and externalize it
to the urine.";
J. Urol. 155:2105-2112(1996).
[9]
INTERACTION WITH RANBP9.
PubMed=12421467; DOI=10.1186/1471-2407-2-28;
Emberley E.D., Gietz R.D., Campbell J.D., Hayglass K.T., Murphy L.C.,
Watson P.H.;
"RanBPM interacts with psoriasin in vitro and their expression
correlates with specific clinical features in vivo in breast cancer.";
BMC Cancer 2:28-28(2002).
[10]
GENOMIC ORGANIZATION.
PubMed=12664160; DOI=10.1007/s00239-002-2410-5;
Kulski J.K., Lim C.P., Dunn D.S., Bellgard M.;
"Genomic and phylogenetic analysis of the S100A7 (psoriasin) gene
duplications within the region of the S100 gene cluster on human
chromosome 1q21.";
J. Mol. Evol. 56:397-406(2003).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
PubMed=9562557; DOI=10.1016/S0969-2126(98)00049-5;
Brodersen D.E., Etzerodt M., Madsen P., Celis J.E., Thoegersen H.C.,
Nyborg J., Kjeldgaard M.;
"EF-hands at atomic resolution: the structure of human psoriasin
(S100A7) solved by MAD phasing.";
Structure 6:477-489(1998).
[13]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
PubMed=10026247; DOI=10.1021/bi982483d;
Brodersen D.E., Nyborg J., Kjeldgaard M.;
"Zinc-binding site of an S100 protein revealed. Two crystal structures
of Ca2+-bound human psoriasin (S100A7) in the Zn2+-loaded and Zn2+-
free states.";
Biochemistry 38:1695-1704(1999).
-!- SUBUNIT: Interacts with RANBP9. {ECO:0000269|PubMed:12421467}.
-!- INTERACTION:
Q96S59:RANBP9; NbExp=3; IntAct=EBI-357520, EBI-636085;
Q5SY68:S100A7L2; NbExp=4; IntAct=EBI-357520, EBI-12006206;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8618345}.
Secreted {ECO:0000269|PubMed:8618345}. Note=Secreted by a non-
classical secretory pathway.
-!- TISSUE SPECIFICITY: Fetal ear, skin, and tongue and human cell
lines. Highly up-regulated in psoriatic epidermis. Also highly
expressed in the urine of bladder squamous cell carcinoma (SCC)
bearing patients. {ECO:0000269|PubMed:8618345}.
-!- MASS SPECTROMETRY: Mass=11365; Mass_error=0.7;
Method=Electrospray; Range=2-101;
Evidence={ECO:0000269|PubMed:8526920};
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/S100A7ID42194ch1q21.html";
-----------------------------------------------------------------------
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EMBL; M86757; AAA60210.1; -; mRNA.
EMBL; CR542164; CAG46961.1; -; mRNA.
EMBL; AL591704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC034687; AAH34687.1; -; mRNA.
EMBL; AJ012825; CAC20409.1; -; Genomic_DNA.
EMBL; BR000043; FAA00017.1; -; Genomic_DNA.
CCDS; CCDS1039.1; -.
PIR; A54327; A54327.
RefSeq; NP_002954.2; NM_002963.3.
UniGene; Hs.112408; -.
PDB; 1PSR; X-ray; 1.05 A; A/B=2-101.
PDB; 2PSR; X-ray; 2.05 A; A=2-101.
PDB; 2WND; X-ray; 1.60 A; A=2-97.
PDB; 2WOR; X-ray; 1.70 A; A=2-101.
PDB; 2WOS; X-ray; 1.70 A; A=2-101.
PDB; 3PSR; X-ray; 2.50 A; A/B=2-101.
PDB; 4AQJ; X-ray; 1.60 A; A=1-101.
PDBsum; 1PSR; -.
PDBsum; 2PSR; -.
PDBsum; 2WND; -.
PDBsum; 2WOR; -.
PDBsum; 2WOS; -.
PDBsum; 3PSR; -.
PDBsum; 4AQJ; -.
ProteinModelPortal; P31151; -.
SMR; P31151; -.
BioGrid; 112186; 51.
IntAct; P31151; 21.
MINT; MINT-1156620; -.
STRING; 9606.ENSP00000357711; -.
DrugBank; DB04474; 1-Anilino-8-Naphthalene Sulfonate.
iPTMnet; P31151; -.
PhosphoSitePlus; P31151; -.
BioMuta; S100A7; -.
DMDM; 172046820; -.
UCD-2DPAGE; P31151; -.
EPD; P31151; -.
MaxQB; P31151; -.
PaxDb; P31151; -.
PeptideAtlas; P31151; -.
PRIDE; P31151; -.
TopDownProteomics; P31151; -.
DNASU; 6278; -.
Ensembl; ENST00000368722; ENSP00000357711; ENSG00000143556.
Ensembl; ENST00000368723; ENSP00000357712; ENSG00000143556.
GeneID; 6278; -.
KEGG; hsa:6278; -.
UCSC; uc001fbv.2; human.
CTD; 6278; -.
DisGeNET; 6278; -.
EuPathDB; HostDB:ENSG00000143556.8; -.
GeneCards; S100A7; -.
H-InvDB; HIX0200006; -.
HGNC; HGNC:10497; S100A7.
HPA; CAB001453; -.
HPA; CAB033766; -.
HPA; HPA006997; -.
MIM; 600353; gene.
neXtProt; NX_P31151; -.
OpenTargets; ENSG00000143556; -.
PharmGKB; PA34909; -.
eggNOG; ENOG410JEQ8; Eukaryota.
eggNOG; ENOG41114XT; LUCA.
GeneTree; ENSGT00390000017320; -.
HOGENOM; HOG000154231; -.
HOVERGEN; HBG095357; -.
InParanoid; P31151; -.
KO; K21126; -.
OMA; SHGAPAC; -.
OrthoDB; EOG091G0Y5T; -.
PhylomeDB; P31151; -.
TreeFam; TF341148; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6799990; Metal sequestration by antimicrobial proteins.
EvolutionaryTrace; P31151; -.
GeneWiki; S100A7; -.
GenomeRNAi; 6278; -.
PRO; PR:P31151; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143556; -.
CleanEx; HS_S100A7; -.
Genevisible; P31151; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; NAS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0050786; F:RAGE receptor binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
GO; GO:0001525; P:angiogenesis; NAS:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IMP:UniProtKB.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
GO; GO:0030216; P:keratinocyte differentiation; NAS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0071624; P:positive regulation of granulocyte chemotaxis; IDA:UniProtKB.
GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:UniProtKB.
GO; GO:0010820; P:positive regulation of T cell chemotaxis; IDA:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:UniProtKB.
GO; GO:0000302; P:response to reactive oxygen species; IDA:UniProtKB.
GO; GO:0051238; P:sequestering of metal ion; IDA:UniProtKB.
CDD; cd00213; S-100; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR034325; S-100_dom.
InterPro; IPR001751; S100/CaBP-9k_CS.
InterPro; IPR013787; S100_Ca-bd_sub.
InterPro; IPR028477; S100A7.
PANTHER; PTHR11639:SF64; PTHR11639:SF64; 1.
Pfam; PF01023; S_100; 1.
SMART; SM01394; S_100; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 1.
PROSITE; PS00303; S100_CABP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Metal-binding;
Polymorphism; Reference proteome; Repeat; Secreted; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8526920}.
CHAIN 2 101 Protein S100-A7.
/FTId=PRO_0000143990.
DOMAIN 13 48 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 50 85 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 63 74 2; high affinity.
METAL 18 18 Zinc.
METAL 25 25 Zinc.
METAL 87 87 Zinc.
METAL 91 91 Zinc.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:8526920}.
DISULFID 47 96
VARIANT 28 28 E -> D (in dbSNP:rs3014837).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1940442,
ECO:0000269|Ref.2, ECO:0000269|Ref.5}.
/FTId=VAR_039118.
HELIX 5 19 {ECO:0000244|PDB:1PSR}.
HELIX 29 39 {ECO:0000244|PDB:1PSR}.
HELIX 41 49 {ECO:0000244|PDB:1PSR}.
HELIX 54 56 {ECO:0000244|PDB:1PSR}.
HELIX 58 62 {ECO:0000244|PDB:1PSR}.
STRAND 67 70 {ECO:0000244|PDB:2WND}.
HELIX 72 89 {ECO:0000244|PDB:1PSR}.
TURN 90 92 {ECO:0000244|PDB:1PSR}.
SEQUENCE 101 AA; 11471 MW; 02C4CE39BF140971 CRC64;
MSNTQAERSI IGMIDMFHKY TRRDDKIEKP SLLTMMKENF PNFLSACDKK GTNYLADVFE
KKDKNEDKKI DFSEFLSLLG DIATDYHKQS HGAAPCSGGS Q


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