S10A5_HUMAN
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 03-AUG-2022, entry version 166.
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 PaxDb; P33763; -.
DR PeptideAtlas; P33763; -.
DR PRIDE; P33763; -.
DR Antibodypedia; 34125; 271 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 CTD; 6276; -.
DR DisGeNET; 6276; -.
DR GeneCards; S100A5; -.
DR HGNC; HGNC:10495; S100A5.
DR HPA; ENSG00000196420; Tissue enhanced (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; 1563974at2759; -.
DR PhylomeDB; P33763; -.
DR TreeFam; TF332727; -.
DR PathwayCommons; P33763; -.
DR SignaLink; P33763; -.
DR BioGRID-ORCS; 6276; 9 hits in 1063 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 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 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; IPR028497; S100-A5.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF65; PTHR11639:SF65; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM00054; EFh; 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; 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