S10A3_RAT
ID S10A3_RAT Reviewed; 101 AA.
AC P62819; P56566;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein S100-A3;
DE AltName: Full=Protein S-100E;
DE AltName: Full=S100 calcium-binding protein A3;
GN Name=S100a3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Hair follicle;
RA Ito M., Kizawa K.;
RT "Expression of S100 genes in hair follicle epithelium.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 58-66, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
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 -!- 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; AF140231; AAK28305.1; -; mRNA.
DR RefSeq; NP_446133.1; NM_053681.1.
DR RefSeq; XP_006232621.1; XM_006232559.3.
DR RefSeq; XP_006232622.1; XM_006232560.3.
DR RefSeq; XP_006232625.1; XM_006232563.3.
DR RefSeq; XP_017446066.1; XM_017590577.1.
DR RefSeq; XP_017446067.1; XM_017590578.1.
DR RefSeq; XP_017446068.1; XM_017590579.1.
DR RefSeq; XP_017446069.1; XM_017590580.1.
DR AlphaFoldDB; P62819; -.
DR SMR; P62819; -.
DR STRING; 10116.ENSRNOP00000016034; -.
DR PaxDb; P62819; -.
DR GeneID; 114216; -.
DR KEGG; rno:114216; -.
DR UCSC; RGD:620260; rat.
DR CTD; 6274; -.
DR RGD; 620260; S100a3.
DR VEuPathDB; HostDB:ENSRNOG00000012008; -.
DR eggNOG; ENOG502SSQB; Eukaryota.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; P62819; -.
DR PhylomeDB; P62819; -.
DR TreeFam; TF332727; -.
DR PRO; PR:P62819; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000012008; Expressed in thymus and 16 other tissues.
DR ExpressionAtlas; P62819; baseline and differential.
DR Genevisible; P62819; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Calcium; Citrullination; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Metal-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..101
FT /note="Protein S100-A3"
FT /id="PRO_0000143974"
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
