S100G_RAT
ID S100G_RAT Reviewed; 79 AA.
AC P02634; P51964;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein S100-G;
DE AltName: Full=9 kDa CaBP;
DE AltName: Full=Calbindin-D9k;
DE AltName: Full=Cholecalcin;
DE AltName: Full=S100 calcium-binding protein G;
DE AltName: Full=Vitamin D-dependent calcium-binding protein, intestinal;
DE Short=CABP;
GN Name=S100g; Synonyms=Calb3, S100d;
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 [GENOMIC DNA].
RX PubMed=3345761; DOI=10.1111/j.1432-1033.1988.tb13853.x;
RA Perret C., Lomri N., Gouhier N., Auffray C., Thomasset M.;
RT "The rat vitamin-D-dependent calcium-binding protein (9-kDa CaBP) gene.
RT Complete nucleotide sequence and structural organization.";
RL Eur. J. Biochem. 172:43-51(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3476932; DOI=10.1073/pnas.84.17.6108;
RA Darwish H.M., Krisinger J., Strom M., Deluca H.F.;
RT "Molecular cloning of the cDNA and chromosomal gene for vitamin D-dependent
RT calcium-binding protein of rat intestine.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6108-6111(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3194402; DOI=10.1073/pnas.85.23.8988;
RA Krisinger J., Darwish H., Maeda N., Deluca H.F.;
RT "Structure and nucleotide sequence of the rat intestinal vitamin D-
RT dependent calcium binding protein gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:8988-8992(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 PROTEIN SEQUENCE OF 2-79, AND ACETYLATION AT SER-2.
RX PubMed=3741407; DOI=10.1042/bj2350585;
RA McManus J.P., Watson D.C., Yaguchi M.;
RT "The purification and complete amino acid sequence of the 9000-Mr Ca2+-
RT binding protein from rat placenta. Identity with the vitamin D-dependent
RT intestinal Ca2+-binding protein.";
RL Biochem. J. 235:585-595(1986).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-79.
RX PubMed=6315698; DOI=10.1016/s0021-9258(17)43941-x;
RA Desplan C., Heidmann O., Lillie J.W., Auffray C., Thomasset M.;
RT "Sequence of rat intestinal vitamin D-dependent calcium-binding protein
RT derived from a cDNA clone. Evolutionary implications.";
RL J. Biol. Chem. 258:13502-13505(1983).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-71.
RX PubMed=7750504; DOI=10.1210/endo.136.6.7750504;
RA Zanello S.B., Boland R.L., Norman A.W.;
RT "cDNA sequence identity of a vitamin D-dependent calcium-binding protein in
RT the chick to calbindin D-9K.";
RL Endocrinology 136:2784-2787(1995).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-47, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- MISCELLANEOUS: The synthesis of this protein in the absorptive cells of
CC the rat duodenum is vitamin D3-dependent.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from chick.
CC {ECO:0000305|PubMed:7750504}.
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DR EMBL; X16635; CAA34627.1; -; Genomic_DNA.
DR EMBL; K00994; AAA40843.1; -; mRNA.
DR EMBL; J02954; AAA42333.1; -; mRNA.
DR EMBL; BC059153; AAH59153.1; -; mRNA.
DR EMBL; J04133; AAA40853.1; -; Genomic_DNA.
DR EMBL; S78183; AAD14276.1; -; mRNA.
DR PIR; A31258; KLRTI.
DR RefSeq; NP_036653.1; NM_012521.2.
DR RefSeq; XP_006256950.1; XM_006256888.3.
DR AlphaFoldDB; P02634; -.
DR SMR; P02634; -.
DR STRING; 10116.ENSRNOP00000005622; -.
DR iPTMnet; P02634; -.
DR PhosphoSitePlus; P02634; -.
DR PaxDb; P02634; -.
DR GeneID; 24249; -.
DR KEGG; rno:24249; -.
DR UCSC; RGD:2253; rat.
DR CTD; 795; -.
DR RGD; 2253; S100g.
DR VEuPathDB; HostDB:ENSRNOG00000004222; -.
DR eggNOG; ENOG502T3Z3; Eukaryota.
DR HOGENOM; CLU_138624_4_0_1; -.
DR InParanoid; P02634; -.
DR OMA; QKYAAKE; -.
DR OrthoDB; 1558629at2759; -.
DR PhylomeDB; P02634; -.
DR PRO; PR:P02634; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000004222; Expressed in duodenum and 16 other tissues.
DR Genevisible; P02634; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Calcium; Direct protein sequencing; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Vitamin D.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3741407"
FT CHAIN 2..79
FT /note="Protein S100-G"
FT /id="PRO_0000144030"
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:0000269|PubMed:3741407"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 2..3
FT /note="SA -> AS (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="S -> N (in Ref. 6; AAA40843)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="K -> KQ (in Ref. 3; AAA40853)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="K -> E (in Ref. 6; AAA40843)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="G -> D (in Ref. 6; AAA40843)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 79 AA; 9038 MW; 3566BD81668704C6 CRC64;
MSAKKSPEEM KSIFQKYAAK EGDPNQLSKE ELKLLIQSEF PSLLKASSTL DNLFKELDKN
GDGEVSYEEF EVFFKKLSQ
