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Database: UniProt
Entry: P33763
LinkDB: P33763
Original site: P33763 
ID   S10A5_HUMAN             Reviewed;          92 AA.
AC   P33763; Q52LE7; Q5RHS3;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 2.
DT   24-JAN-2024, entry version 174.
DE   RecName: Full=Protein S100-A5;
DE   AltName: Full=Protein S-100D;
DE   AltName: Full=S100 calcium-binding protein A5;
GN   Name=S100A5; Synonyms=S100D;
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] (ISOFORM 1).
RC   TISSUE=Kidney;
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   [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., 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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   FUNCTION.
RX   PubMed=10882717; DOI=10.1074/jbc.m002260200;
RA   Schaefer B.W., Fritschy J.-M., Murmann P., Troxler H., Durussel I.,
RA   Heizmann C.W., Cox J.A.;
RT   "Brain S100A5 is a novel calcium-, zinc-, and copper ion-binding protein of
RT   the EF-hand superfamily.";
RL   J. Biol. Chem. 275:30623-30630(2000).
RN   [6]
RP   STRUCTURE BY NMR IN COMPLEX WITH CALCIUM IONS, AND SUBUNIT.
RX   PubMed=19536568; DOI=10.1007/s00775-009-0553-1;
RA   Bertini I., Das Gupta S., Hu X., Karavelas T., Luchinat C., Parigi G.,
RA   Yuan J.;
RT   "Solution structure and dynamics of S100A5 in the apo and Ca2+-bound
RT   states.";
RL   J. Biol. Inorg. Chem. 14:1097-1107(2009).
CC   -!- FUNCTION: Binds calcium, zinc and copper. One subunit can
CC       simultaneously bind 2 calcium ions or 2 copper ions plus 1 zinc ion.
CC       Calcium and copper ions compete for the same binding sites.
CC       {ECO:0000269|PubMed:10882717}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19536568}.
CC   -!- INTERACTION:
CC       P33763; Q9HB71: CACYBP; NbExp=3; IntAct=EBI-7211732, EBI-1047302;
CC       P33763; P52907: CAPZA1; NbExp=2; IntAct=EBI-7211732, EBI-355586;
CC       P33763; O15151: MDM4; NbExp=2; IntAct=EBI-7211732, EBI-398437;
CC       P33763; P35579: MYH9; NbExp=2; IntAct=EBI-7211732, EBI-350338;
CC       P33763; P32418: SLC8A1; NbExp=2; IntAct=EBI-7211732, EBI-2682189;
CC       P33763; P04637: TP53; NbExp=2; IntAct=EBI-7211732, EBI-366083;
CC       P33763; Q8TD43: TRPM4; NbExp=3; IntAct=EBI-7211732, EBI-11723041;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P33763-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P33763-2; Sequence=VSP_055506;
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA79472.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA79475.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA79479.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z18954; CAA79479.1; ALT_INIT; mRNA.
DR   EMBL; Z18949; CAA79472.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z18950; CAA79475.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BX470102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW53317.1; -; Genomic_DNA.
DR   EMBL; BC093955; AAH93955.1; -; mRNA.
DR   EMBL; BC093957; AAH93957.1; -; mRNA.
DR   CCDS; CCDS1041.2; -. [P33763-1]
DR   RefSeq; NP_002953.2; NM_002962.1. [P33763-1]
DR   RefSeq; XP_016857519.1; XM_017002030.1.
DR   RefSeq; XP_016857520.1; XM_017002031.1. [P33763-1]
DR   RefSeq; XP_016857521.1; XM_017002032.1. [P33763-1]
DR   PDB; 2KAX; NMR; -; A/B=1-92.
DR   PDB; 2KAY; NMR; -; A/B=1-92.
DR   PDB; 4DIR; X-ray; 2.60 A; A/B=1-92.
DR   PDB; 6WN7; X-ray; 1.25 A; A/B/C/D/E/F=1-92.
DR   PDBsum; 2KAX; -.
DR   PDBsum; 2KAY; -.
DR   PDBsum; 4DIR; -.
DR   PDBsum; 6WN7; -.
DR   AlphaFoldDB; P33763; -.
DR   BMRB; P33763; -.
DR   SMR; P33763; -.
DR   BioGRID; 112184; 1.
DR   IntAct; P33763; 10.
DR   MINT; P33763; -.
DR   STRING; 9606.ENSP00000357707; -.
DR   iPTMnet; P33763; -.
DR   PhosphoSitePlus; P33763; -.
DR   BioMuta; S100A5; -.
DR   DMDM; 20178321; -.
DR   MassIVE; P33763; -.
DR   PaxDb; 9606-ENSP00000357707; -.
DR   PeptideAtlas; P33763; -.
DR   ProteomicsDB; 54923; -. [P33763-1]
DR   Antibodypedia; 34125; 289 antibodies from 29 providers.
DR   DNASU; 6276; -.
DR   Ensembl; ENST00000368717.3; ENSP00000357706.2; ENSG00000196420.8. [P33763-1]
DR   Ensembl; ENST00000368718.5; ENSP00000357707.1; ENSG00000196420.8. [P33763-1]
DR   GeneID; 6276; -.
DR   KEGG; hsa:6276; -.
DR   MANE-Select; ENST00000368717.3; ENSP00000357706.2; NM_001394232.1; NP_001381161.1.
DR   UCSC; uc001fbx.3; human. [P33763-1]
DR   AGR; HGNC:10495; -.
DR   CTD; 6276; -.
DR   DisGeNET; 6276; -.
DR   GeneCards; S100A5; -.
DR   HGNC; HGNC:10495; S100A5.
DR   HPA; ENSG00000196420; Tissue enhanced (kidney, skin, thyroid gland).
DR   MIM; 176991; gene.
DR   neXtProt; NX_P33763; -.
DR   OpenTargets; ENSG00000196420; -.
DR   PharmGKB; PA34907; -.
DR   VEuPathDB; HostDB:ENSG00000196420; -.
DR   eggNOG; ENOG502S40V; Eukaryota.
DR   GeneTree; ENSGT00940000161986; -.
DR   HOGENOM; CLU_138624_2_0_1; -.
DR   InParanoid; P33763; -.
DR   OMA; HAVMETP; -.
DR   OrthoDB; 4575435at2759; -.
DR   PhylomeDB; P33763; -.
DR   TreeFam; TF332727; -.
DR   PathwayCommons; P33763; -.
DR   SignaLink; P33763; -.
DR   BioGRID-ORCS; 6276; 10 hits in 1139 CRISPR screens.
DR   EvolutionaryTrace; P33763; -.
DR   GeneWiki; S100A5; -.
DR   GenomeRNAi; 6276; -.
DR   Pharos; P33763; Tbio.
DR   PRO; PR:P33763; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P33763; Protein.
DR   Bgee; ENSG00000196420; Expressed in granulocyte and 96 other cell types or tissues.
DR   Genevisible; P33763; HS.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
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:0005507; F:copper ion binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   CDD; cd00213; S-100; 1.
DR   DisProt; DP01552; -.
DR   Gene3D; 1.10.238.10; EF-hand; 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   PANTHER; PTHR11639:SF65; PROTEIN S100-A5; 1.
DR   PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 1.
DR   Pfam; PF01023; S_100; 1.
DR   SMART; SM00054; EFh; 1.
DR   SMART; SM01394; S_100; 1.
DR   SUPFAM; SSF47473; EF-hand; 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; Alternative splicing; Calcium; Copper; Metal-binding;
KW   Reference proteome; Repeat; Zinc.
FT   CHAIN           1..92
FT                   /note="Protein S100-A5"
FT                   /id="PRO_0000143980"
FT   DOMAIN          12..47
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          47..82
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         60
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         62
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         64
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         66
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         71
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   VAR_SEQ         1
FT                   /note="M -> MPAAWILWAHSHSELHTVM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055506"
FT   VARIANT         54
FT                   /note="D -> G (in dbSNP:rs3795393)"
FT                   /id="VAR_001305"
FT   HELIX           4..20
FT                   /evidence="ECO:0007829|PDB:6WN7"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:6WN7"
FT   STRAND          26..30
FT                   /evidence="ECO:0007829|PDB:2KAX"
FT   HELIX           31..41
FT                   /evidence="ECO:0007829|PDB:6WN7"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:2KAX"
FT   HELIX           51..59
FT                   /evidence="ECO:0007829|PDB:6WN7"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:2KAX"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:6WN7"
FT   HELIX           69..85
FT                   /evidence="ECO:0007829|PDB:6WN7"
SQ   SEQUENCE   92 AA;  10744 MW;  49C2B1DAEC481561 CRC64;
     METPLEKALT TMVTTFHKYS GREGSKLTLS RKELKELIKK ELCLGEMKES SIDDLMKSLD
     KNSDQEIDFK EYSVFLTMLC MAYNDFFLED NK
//
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