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S1A7A_HUMAN
ID   S1A7A_HUMAN             Reviewed;         101 AA.
AC   Q86SG5; D3DV38; Q5SY69;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Protein S100-A7A;
DE   AltName: Full=S100 calcium-binding protein A15;
DE   AltName: Full=S100 calcium-binding protein A7-like 1;
DE   AltName: Full=S100 calcium-binding protein A7A;
GN   Name=S100A7A; Synonyms=S100A15, S100A7L1;
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 [GENOMIC DNA / MRNA].
RC   TISSUE=Epidermis;
RX   PubMed=12923069; DOI=10.1096/fj.03-0148fje;
RA   Wolf R., Mirmohammadsadegh A., Walz M., Lysa B., Tartler U., Remus R.,
RA   Hengge U., Michel G., Ruzicka T.;
RT   "Molecular cloning and characterization of alternatively spliced mRNA
RT   isoforms from psoriatic skin encoding a novel member of the S100 family.";
RL   FASEB J. 17:1969-1971(2003).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), CALCIUM-BINDING SITES, AND
RP   ZINC-BINDING SITES.
RX   PubMed=22747601; DOI=10.1186/1472-6807-12-16;
RA   Murray J.I., Tonkin M.L., Whiting A.L., Peng F., Farnell B., Cullen J.T.,
RA   Hof F., Boulanger M.J.;
RT   "Structural characterization of S100A15 reveals a novel zinc coordination
RT   site among S100 proteins and altered surface chemistry with functional
RT   implications for receptor binding.";
RL   BMC Struct. Biol. 12:16-16(2012).
CC   -!- FUNCTION: May be involved in epidermal differentiation and inflammation
CC       and might therefore be important for the pathogenesis of psoriasis and
CC       other diseases.
CC   -!- INTERACTION:
CC       Q86SG5; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-13077820, EBI-12357161;
CC       Q86SG5; Q5SY68: S100A7L2; NbExp=8; IntAct=EBI-13077820, EBI-12006206;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Overexpressed in psoriasis.
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR   EMBL; AY189117; AAO40032.1; -; Genomic_DNA.
DR   EMBL; AY189118; AAO40033.1; -; mRNA.
DR   EMBL; AY189119; AAO40034.1; -; mRNA.
DR   EMBL; AL591704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW53328.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53329.1; -; Genomic_DNA.
DR   EMBL; BR000043; FAA00014.1; -; Genomic_DNA.
DR   CCDS; CCDS30872.1; -.
DR   RefSeq; NP_789793.1; NM_176823.3.
DR   PDB; 4AQI; X-ray; 1.70 A; A=1-101.
DR   PDBsum; 4AQI; -.
DR   AlphaFoldDB; Q86SG5; -.
DR   SMR; Q86SG5; -.
DR   BioGRID; 130711; 108.
DR   IntAct; Q86SG5; 14.
DR   STRING; 9606.ENSP00000357718; -.
DR   GlyGen; Q86SG5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q86SG5; -.
DR   PhosphoSitePlus; Q86SG5; -.
DR   BioMuta; S100A7A; -.
DR   DMDM; 37088296; -.
DR   jPOST; Q86SG5; -.
DR   MassIVE; Q86SG5; -.
DR   MaxQB; Q86SG5; -.
DR   PaxDb; Q86SG5; -.
DR   PeptideAtlas; Q86SG5; -.
DR   PRIDE; Q86SG5; -.
DR   ProteomicsDB; 69587; -.
DR   Antibodypedia; 56992; 36 antibodies from 12 providers.
DR   DNASU; 338324; -.
DR   Ensembl; ENST00000329256.2; ENSP00000329008.2; ENSG00000184330.12.
DR   Ensembl; ENST00000368728.2; ENSP00000357717.1; ENSG00000184330.12.
DR   Ensembl; ENST00000368729.9; ENSP00000357718.3; ENSG00000184330.12.
DR   GeneID; 338324; -.
DR   KEGG; hsa:338324; -.
DR   MANE-Select; ENST00000368729.9; ENSP00000357718.3; NM_176823.4; NP_789793.1.
DR   UCSC; uc001fbt.1; human.
DR   CTD; 338324; -.
DR   DisGeNET; 338324; -.
DR   GeneCards; S100A7A; -.
DR   HGNC; HGNC:21657; S100A7A.
DR   HPA; ENSG00000184330; Group enriched (esophagus, lymphoid tissue, skin, vagina).
DR   MIM; 617427; gene.
DR   neXtProt; NX_Q86SG5; -.
DR   OpenTargets; ENSG00000184330; -.
DR   PharmGKB; PA162402333; -.
DR   VEuPathDB; HostDB:ENSG00000184330; -.
DR   eggNOG; ENOG502SZJ5; Eukaryota.
DR   GeneTree; ENSGT00940000163488; -.
DR   HOGENOM; CLU_138624_5_0_1; -.
DR   InParanoid; Q86SG5; -.
DR   OrthoDB; 1486203at2759; -.
DR   PhylomeDB; Q86SG5; -.
DR   TreeFam; TF341148; -.
DR   PathwayCommons; Q86SG5; -.
DR   Reactome; R-HSA-6799990; Metal sequestration by antimicrobial proteins.
DR   SignaLink; Q86SG5; -.
DR   BioGRID-ORCS; 338324; 21 hits in 989 CRISPR screens.
DR   ChiTaRS; S100A7A; human.
DR   GeneWiki; S100A15; -.
DR   GenomeRNAi; 338324; -.
DR   Pharos; Q86SG5; Tbio.
DR   PRO; PR:Q86SG5; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q86SG5; protein.
DR   Bgee; ENSG00000184330; Expressed in penis and 56 other tissues.
DR   Genevisible; Q86SG5; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0043621; F:protein self-association; IDA:MGI.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
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; Calcium; Cytoplasm; Metal-binding; Reference proteome;
KW   Repeat; Zinc.
FT   CHAIN           1..101
FT                   /note="Protein S100-A7A"
FT                   /id="PRO_0000143991"
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                   /ligand_label="1"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
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         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
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                   /ligand_label="1"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   VARIANT         23
FT                   /note="R -> H (in dbSNP:rs55985140)"
FT                   /id="VAR_061048"
FT   VARIANT         84
FT                   /note="A -> T (in dbSNP:rs3006414)"
FT                   /id="VAR_048468"
FT   HELIX           5..20
FT                   /evidence="ECO:0007829|PDB:4AQI"
FT   HELIX           29..39
FT                   /evidence="ECO:0007829|PDB:4AQI"
FT   HELIX           41..49
FT                   /evidence="ECO:0007829|PDB:4AQI"
FT   HELIX           54..62
FT                   /evidence="ECO:0007829|PDB:4AQI"
FT   STRAND          67..70
FT                   /evidence="ECO:0007829|PDB:4AQI"
FT   HELIX           72..90
FT                   /evidence="ECO:0007829|PDB:4AQI"
SQ   SEQUENCE   101 AA;  11305 MW;  A311A921414C9732 CRC64;
     MSNTQAERSI IGMIDMFHKY TGRDGKIEKP SLLTMMKENF PNFLSACDKK GIHYLATVFE
     KKDKNEDKKI DFSEFLSLLG DIAADYHKQS HGAAPCSGGS Q
 
 
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