S100G_BOVIN
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 03-AUG-2022, entry version 158.
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 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; -.
DR AlphaFoldDB; P02633; -.
DR BMRB; P02633; -.
DR SMR; P02633; -.
DR STRING; 9913.ENSBTAP00000022630; -.
DR iPTMnet; P02633; -.
DR PaxDb; P02633; -.
DR Ensembl; ENSBTAT00000022630; ENSBTAP00000022630; ENSBTAG00000017020.
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; 1558629at2759; -.
DR TreeFam; TF332727; -.
DR EvolutionaryTrace; P02633; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000017020; Expressed in placenta and 91 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:0005499; F:vitamin D binding; IEA:UniProtKB-KW.
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 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 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..48
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
