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   24-JAN-2024, entry version 155.
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; 10116-ENSRNOP00000005622; -.
DR   GeneID; 24249; -.
DR   KEGG; rno:24249; -.
DR   UCSC; RGD:2253; rat.
DR   AGR; RGD:2253; -.
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   OrthoDB; 4248222at2759; -.
DR   PhylomeDB; P02634; -.
DR   PRO; PR:P02634; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000004222; Expressed in duodenum and 16 other cell types or tissues.
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   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   CDD; cd00213; S-100; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 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   PANTHER; PTHR11639:SF73; PROTEIN S100-G; 1.
DR   PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 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; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS00303; S100_CABP; 1.
DR   Genevisible; P02634; RN.
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
//