S10A5_MOUSE
ID S10A5_MOUSE Reviewed; 93 AA.
AC P63084; O88945; P82540;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9920416; DOI=10.1016/s0167-4889(98)00137-2;
RA Ridinger K., Ilg E.C., Niggli F.K., Heizmann C.W., Schaefer B.W.;
RT "Clustered organization of S100 genes in human and mouse.";
RL Biochim. Biophys. Acta 1448:254-263(1998).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; AF087469; AAC64106.1; -; mRNA.
DR CCDS; CCDS38505.1; -.
DR RefSeq; NP_035442.1; NM_011312.2.
DR RefSeq; XP_006501242.1; XM_006501179.1.
DR RefSeq; XP_006501243.1; XM_006501180.2.
DR RefSeq; XP_006501244.1; XM_006501181.2.
DR AlphaFoldDB; P63084; -.
DR SMR; P63084; -.
DR STRING; 10090.ENSMUSP00000102952; -.
DR PhosphoSitePlus; P63084; -.
DR EPD; P63084; -.
DR PaxDb; P63084; -.
DR PeptideAtlas; P63084; -.
DR PRIDE; P63084; -.
DR ProteomicsDB; 256554; -.
DR ABCD; P63084; 1 sequenced antibody.
DR Antibodypedia; 34125; 271 antibodies from 29 providers.
DR DNASU; 20199; -.
DR Ensembl; ENSMUST00000001049; ENSMUSP00000001049; ENSMUSG00000001023.
DR Ensembl; ENSMUST00000107329; ENSMUSP00000102952; ENSMUSG00000001023.
DR GeneID; 20199; -.
DR KEGG; mmu:20199; -.
DR UCSC; uc008qda.1; mouse.
DR CTD; 6276; -.
DR MGI; MGI:1338915; S100a5.
DR VEuPathDB; HostDB:ENSMUSG00000001023; -.
DR eggNOG; ENOG502S40V; Eukaryota.
DR GeneTree; ENSGT00940000161986; -.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; P63084; -.
DR OMA; HAVMETP; -.
DR OrthoDB; 1563974at2759; -.
DR PhylomeDB; P63084; -.
DR TreeFam; TF332727; -.
DR BioGRID-ORCS; 20199; 0 hits in 75 CRISPR screens.
DR PRO; PR:P63084; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P63084; protein.
DR Bgee; ENSMUSG00000001023; Expressed in olfactory epithelium and 35 other tissues.
DR ExpressionAtlas; P63084; baseline and differential.
DR Genevisible; P63084; MM.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS: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; 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 3: Inferred from homology;
KW Calcium; Copper; Metal-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..93
FT /note="Protein S100-A5"
FT /id="PRO_0000143981"
FT DOMAIN 12..47
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 48..83
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 61
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 63
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 65
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 67
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 72
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"
SQ SEQUENCE 93 AA; 10812 MW; 9A922E1898D202A4 CRC64;
METPLEKALT TMVTTFHKYS GREGSKLTLS RKELKELIKT ELSLAEKMKE SSIDNLMKSL
DKNSDQEIDF KEYSVFLTTL CMAYNDFFLE DNK
