ID   S100G_BOVIN             Reviewed;          79 AA.
AC   P02633; Q17Q94;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 174.
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; Synonyms=CALB3, S100D;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2710141; DOI=10.1210/mend-3-2-427;
RA   Kumar R., Wieben E., Beecher S.J.;
RT   "The molecular cloning of the complementary deoxyribonucleic acid for
RT   bovine vitamin D-dependent calcium-binding protein: structure of the full-
RT   length protein and evidence for homologies with other calcium-binding
RT   proteins of the troponin-C superfamily of proteins.";
RL   Mol. Endocrinol. 3:427-432(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Placenta;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 5-79.
RX   PubMed=7240164; DOI=10.1016/s0021-9258(19)69257-4;
RA   Fullmer C.S., Wasserman R.H.;
RT   "The amino acid sequence of bovine intestinal calcium-binding protein.";
RL   J. Biol. Chem. 256:5669-5674(1981).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND ACETYLATION AT SER-2.
RX   PubMed=7312031; DOI=10.1038/294327a0;
RA   Szebenyi D.M.E., Obendorf S.K., Moffat K.;
RT   "Structure of vitamin D-dependent calcium-binding protein from bovine
RT   intestine.";
RL   Nature 294:327-332(1981).
RN   [5]
RP   X-RAY STRUCTURE REFINEMENT.
RX   PubMed=3722173; DOI=10.1016/s0021-9258(19)84447-2;
RA   Szebenyi D.M.E., Moffat K.;
RT   "The refined structure of vitamin D-dependent calcium-binding protein from
RT   bovine intestine. Molecular details, ion binding, and implications for the
RT   structure of other calcium-binding proteins.";
RL   J. Biol. Chem. 261:8761-8777(1986).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   PubMed=9194174; DOI=10.1002/pro.5560060602;
RA   Andersson M., Malmendal A., Linse S., Ivarsson I., Forsen S.,
RA   Svensson L.A.;
RT   "Structural basis for the negative allostery between Ca(2+)- and Mg(2+)-
RT   binding in the intracellular Ca(2+)-receptor calbindin D9k.";
RL   Protein Sci. 6:1139-1147(1997).
RN   [7]
RP   STRUCTURE BY NMR.
RX   PubMed=2350544; DOI=10.1021/bi00470a020;
RA   Kordel J., Forsen S., Drakenberg T., Chazin W.J.;
RT   "The rate and structural consequences of proline cis-trans isomerization in
RT   calbindin D9k: NMR studies of the minor (cis-Pro43) isoform and the
RT   Pro43Gly mutant.";
RL   Biochemistry 29:4400-4409(1990).
RN   [8]
RP   STRUCTURE BY NMR.
RX   PubMed=2200514; DOI=10.1021/bi00476a016;
RA   Skelton N.J., Forsen S., Chazin W.J.;
RT   "1H NMR resonance assignments, secondary structure, and global fold of Apo
RT   bovine calbindin D9k.";
RL   Biochemistry 29:5752-5761(1990).
RN   [9]
RP   STRUCTURE BY NMR.
RX   PubMed=2067016; DOI=10.1016/0022-2836(91)90389-n;
RA   Akke M., Forsen S., Chazin W.J.;
RT   "Molecular basis for co-operativity in Ca2+ binding to calbindin D9k. 1H
RT   nuclear magnetic resonance studies of (Cd2+)1-bovine calbindin D9k.";
RL   J. Mol. Biol. 220:173-189(1991).
RN   [10]
RP   STRUCTURE BY NMR.
RX   PubMed=7666423; DOI=10.1006/jmbi.1995.0478;
RA   Akke M., Forsen S., Chazin W.J.;
RT   "Solution structure of (Cd2+)1-calbindin D9k reveals details of the
RT   stepwise structural changes along the Apo-->(Ca2+)II1-->(Ca2+)I,II2 binding
RT   pathway.";
RL   J. Mol. Biol. 252:102-121(1995).
RN   [11]
RP   STRUCTURE BY NMR.
RX   PubMed=9390401; DOI=10.1023/a:1018383102870;
RA   Kordel J., Pearlman D.A., Chazin W.J.;
RT   "Protein solution structure calculations in solution: solvated molecular
RT   dynamics refinement of calbindin D9k.";
RL   J. Biomol. NMR 10:231-243(1997).
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR   EMBL; M18344; AAA30420.1; -; mRNA.
DR   EMBL; BC118480; AAI18481.1; -; mRNA.
DR   PIR; A40151; KLBOI.
DR   RefSeq; NP_776682.1; NM_174257.3.
DR   PDB; 1B1G; NMR; -; A=5-79.
DR   PDB; 1BOC; NMR; -; A=5-79.
DR   PDB; 1BOD; NMR; -; A=5-79.
DR   PDB; 1CDN; NMR; -; A=5-79.
DR   PDB; 1CLB; NMR; -; A=5-79.
DR   PDB; 1D1O; NMR; -; A=5-79.
DR   PDB; 1HT9; X-ray; 1.76 A; A/B=5-79.
DR   PDB; 1IG5; X-ray; 1.50 A; A=5-79.
DR   PDB; 1IGV; X-ray; 1.85 A; A=5-79.
DR   PDB; 1KCY; NMR; -; A=5-79.
DR   PDB; 1KQV; NMR; -; A=1-79.
DR   PDB; 1KSM; NMR; -; A=1-79.
DR   PDB; 1N65; NMR; -; A=5-79.
DR   PDB; 1QX2; X-ray; 1.44 A; A/B=5-79.
DR   PDB; 1RT0; NMR; -; A=58-69.
DR   PDB; 2BCA; NMR; -; A=5-79.
DR   PDB; 2BCB; NMR; -; A=5-79.
DR   PDB; 2MAZ; NMR; -; A=5-79.
DR   PDB; 3ICB; X-ray; 2.30 A; A=5-79.
DR   PDB; 4ICB; X-ray; 1.60 A; A=5-79.
DR   AlphaFoldDB; P02633; -.
DR   BMRB; P02633; -.
DR   MDposit; P02633; -.
DR   SMR; P02633; -.
DR   FunCoup; P02633; 5.
DR   STRING; 9913.ENSBTAP00000022630; -.
DR   iPTMnet; P02633; -.
DR   PaxDb; 9913-ENSBTAP00000022630; -.
DR   Ensembl; ENSBTAT00000022630.5; ENSBTAP00000022630.3; ENSBTAG00000017020.5.
DR   Ensembl; ENSBTAT00085022638; ENSBTAP00085032131; ENSBTAG00085018487.
DR   GeneID; 281658; -.
DR   KEGG; bta:281658; -.
DR   CTD; 795; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017020; -.
DR   VGNC; VGNC:34249; S100G.
DR   eggNOG; ENOG502T3Z3; Eukaryota.
DR   GeneTree; ENSGT00530000064238; -.
DR   HOGENOM; CLU_138624_4_0_1; -.
DR   InParanoid; P02633; -.
DR   OMA; QKYAAKE; -.
DR   OrthoDB; 26525at2759; -.
DR   EvolutionaryTrace; P02633; -.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000017020; Expressed in placenta and 91 other cell types or 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:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR   FunFam; 1.10.238.10:FF:000236; Protein S100; 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; 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   PDBsum; 1B1G; -.
DR   PDBsum; 1BOC; -.
DR   PDBsum; 1BOD; -.
DR   PDBsum; 1CDN; -.
DR   PDBsum; 1CLB; -.
DR   PDBsum; 1D1O; -.
DR   PDBsum; 1HT9; -.
DR   PDBsum; 1IG5; -.
DR   PDBsum; 1IGV; -.
DR   PDBsum; 1KCY; -.
DR   PDBsum; 1KQV; -.
DR   PDBsum; 1KSM; -.
DR   PDBsum; 1N65; -.
DR   PDBsum; 1QX2; -.
DR   PDBsum; 1RT0; -.
DR   PDBsum; 2BCA; -.
DR   PDBsum; 2BCB; -.
DR   PDBsum; 2MAZ; -.
DR   PDBsum; 3ICB; -.
DR   PDBsum; 4ICB; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Calcium; Direct protein sequencing;
KW   Metal-binding; Phosphoprotein; Reference proteome; Repeat; Vitamin D.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..79
FT                   /note="Protein S100-G"
FT                   /id="PRO_0000144026"
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:7312031"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02634"
FT   HELIX           7..18
FT                   /evidence="ECO:0007829|PDB:1QX2"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:1QX2"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:1QX2"
FT   HELIX           29..39
FT                   /evidence="ECO:0007829|PDB:1QX2"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:1QX2"
FT   STRAND          45..47
FT                   /evidence="ECO:0007829|PDB:4ICB"
FT   HELIX           50..57
FT                   /evidence="ECO:0007829|PDB:1QX2"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:1B1G"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:1QX2"
FT   HELIX           67..77
FT                   /evidence="ECO:0007829|PDB:1QX2"
SQ   SEQUENCE   79 AA;  8918 MW;  80A5B2AA11D4E74B CRC64;
     MSAKKSPEEL KGIFEKYAAK EGDPNQLSKE ELKLLLQTEF PSLLKGPSTL DELFEELDKN
     GDGEVSFEEF QVLVKKISQ
//