S10A3_MOUSE
ID S10A3_MOUSE Reviewed; 101 AA.
AC P62818; P56566;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein S100-A3;
DE AltName: Full=Protein S-100E;
DE AltName: Full=S100 calcium-binding protein A3;
GN Name=S100a3;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=ICR; TISSUE=Skin;
RX PubMed=9804353; DOI=10.1046/j.1523-1747.1998.00385.x;
RA Kizawa K., Tsuchimoto S., Hashimoto K., Uchiwa H.;
RT "Gene expression of mouse S100A3, a cysteine-rich calcium-binding protein,
RT in developing hair follicle.";
RL J. Invest. Dermatol. 111:879-886(1998).
CC -!- FUNCTION: Binds both calcium and zinc. May be involved in calcium-
CC dependent cuticle cell differentiation, hair shaft and hair cuticular
CC barrier formation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and homotetramer for the citrullinated form.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Skin specific, specifically expressed in cuticle of
CC pelage follicle. {ECO:0000269|PubMed:9804353}.
CC -!- PTM: More than half of the arginine residues undergo citrullination by
CC PAD1 and PAD2. Arg-51 is specifically citrullinated by PAD3 and
CC promotes tetramerization (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; AF087470; AAC64107.1; -; mRNA.
DR EMBL; AF004941; AAC78730.1; -; mRNA.
DR CCDS; CCDS17537.1; -.
DR RefSeq; NP_035440.1; NM_011310.2.
DR RefSeq; XP_006501234.1; XM_006501171.3.
DR RefSeq; XP_006501236.1; XM_006501173.3.
DR RefSeq; XP_006501237.1; XM_006501174.1.
DR RefSeq; XP_006501238.1; XM_006501175.2.
DR RefSeq; XP_006501239.1; XM_006501176.2.
DR RefSeq; XP_011238349.1; XM_011240047.1.
DR RefSeq; XP_017174998.1; XM_017319509.1.
DR AlphaFoldDB; P62818; -.
DR SMR; P62818; -.
DR STRING; 10090.ENSMUSP00000001047; -.
DR PaxDb; P62818; -.
DR PeptideAtlas; P62818; -.
DR PRIDE; P62818; -.
DR ProteomicsDB; 255432; -.
DR Ensembl; ENSMUST00000001047; ENSMUSP00000001047; ENSMUSG00000001021.
DR Ensembl; ENSMUST00000200290; ENSMUSP00000142334; ENSMUSG00000001021.
DR Ensembl; ENSMUST00000200508; ENSMUSP00000142747; ENSMUSG00000001021.
DR GeneID; 20197; -.
DR KEGG; mmu:20197; -.
DR UCSC; uc008qcy.1; mouse.
DR CTD; 6274; -.
DR MGI; MGI:1338849; S100a3.
DR VEuPathDB; HostDB:ENSMUSG00000001021; -.
DR eggNOG; ENOG502SSQB; Eukaryota.
DR GeneTree; ENSGT00940000161959; -.
DR InParanoid; P62818; -.
DR OMA; CVYCHEY; -.
DR PhylomeDB; P62818; -.
DR TreeFam; TF332727; -.
DR BioGRID-ORCS; 20197; 3 hits in 73 CRISPR screens.
DR ChiTaRS; S100a3; mouse.
DR PRO; PR:P62818; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P62818; protein.
DR Bgee; ENSMUSG00000001021; Expressed in lip and 49 other tissues.
DR ExpressionAtlas; P62818; baseline and differential.
DR Genevisible; P62818; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00213; S-100; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR034325; S-100_dom.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028488; S100A3.
DR PANTHER; PTHR11639:SF12; PTHR11639:SF12; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 2: Evidence at transcript level;
KW Calcium; Citrullination; Cytoplasm; Disulfide bond; Metal-binding;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..101
FT /note="Protein S100-A3"
FT /id="PRO_0000143973"
FT DOMAIN 12..47
FT /note="EF-hand 1"
FT DOMAIN 50..85
FT /note="EF-hand 2"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000255"
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"
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"
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"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 51
FT /note="Citrulline; by PAD3"
FT /evidence="ECO:0000250"
FT DISULFID 30..68
FT /evidence="ECO:0000250"
SQ SEQUENCE 101 AA; 11747 MW; EE46EABF16646CCA CRC64;
MTRPLEQAVA AIVCTFQEYA GRCGDKYKIC QSELKELLQK ELPTWTPSEF RECDYNKFMS
VLDTNKDCEV DFGEYVRSLA SLCLYCHEYF KECPPEPPCP Q
