S100G_HORSE
ID S100G_HORSE Reviewed; 79 AA.
AC Q865V3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Protein S100-G;
DE AltName: Full=Calbindin-D9k;
DE AltName: Full=S100 calcium-binding protein G;
DE AltName: Full=Vitamin D-dependent calcium-binding protein, intestinal;
DE Short=CABP;
GN Name=S100G;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Toribio R.E., Rourke K.M., Levine A.L., Kohn C.W., Rosol T.J.;
RT "Molecular cloning of the cDNA for Equus caballus calbindin-D9k.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; AY229893; AAO73439.1; -; mRNA.
DR RefSeq; NP_001075359.1; NM_001081890.1.
DR RefSeq; XP_005613996.1; XM_005613939.2.
DR RefSeq; XP_005613997.1; XM_005613940.2.
DR AlphaFoldDB; Q865V3; -.
DR SMR; Q865V3; -.
DR STRING; 9796.ENSECAP00000015147; -.
DR PaxDb; Q865V3; -.
DR Ensembl; ENSECAT00000018564; ENSECAP00000015147; ENSECAG00000017623.
DR GeneID; 100033995; -.
DR KEGG; ecb:100033995; -.
DR CTD; 795; -.
DR VGNC; VGNC:55532; S100G.
DR GeneTree; ENSGT00530000064238; -.
DR InParanoid; Q865V3; -.
DR OrthoDB; 1558629at2759; -.
DR Proteomes; UP000002281; Chromosome X.
DR Bgee; ENSECAG00000017623; Expressed in adult mammalian kidney and 17 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0005499; F:vitamin D binding; IEA:UniProtKB-KW.
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; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028489; S100G.
DR PANTHER; PTHR11639:SF73; PTHR11639:SF73; 1.
DR Pfam; PF00036; EF-hand_1; 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 Acetylation; Calcium; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Vitamin D.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02633"
FT CHAIN 2..79
FT /note="Protein S100-G"
FT /id="PRO_0000273721"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 45..79
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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:0000305"
FT BINDING 31
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 58
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 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 69
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 MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P02633"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02634"
SQ SEQUENCE 79 AA; 8942 MW; 68FA97879E519B1C CRC64;
MSVKKSPEEL KKIFEKYAAK EGDPDQLSKE ELKLLIQNEL PALLKGSSSI DDLFKELDKN
GDGEVSFEEF QVLVKKISQ
