S100G_PIG
ID S100G_PIG Reviewed; 79 AA.
AC P02632;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
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;
DE Contains:
DE RecName: Full=Protein S100-G, minor isoform;
GN Name=S100G; Synonyms=CALB3, S100D;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Yorkshire; TISSUE=Duodenum;
RX PubMed=1391336; DOI=10.1095/biolreprod47.4.503;
RA Jeung E.B., Krisinger J., Dann J.L., Leung P.C.;
RT "Cloning of the porcine calbindin-D9k complementary deoxyribonucleic acid
RT by anchored polymerase chain reaction technique.";
RL Biol. Reprod. 47:503-508(1992).
RN [2]
RP PROTEIN SEQUENCE OF 2-79, ACETYLATION AT SER-2, AND ACETYLATION AT ALA-3
RP (IN MINOR ISOFORM).
RX PubMed=476518; DOI=10.1139/o79-092;
RA Hofmann T., Kawakami M., Hitchman A.J.W., Harrison J.E., Dorrington K.J.;
RT "The amino acid sequence of porcine intestinal calcium-binding protein.";
RL Can. J. Biochem. 57:737-748(1979).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=2775745; DOI=10.1021/bi00440a035;
RA Drakenberg T., Hofmann T., Chazin W.J.;
RT "1H NMR studies of porcine calbindin D9k in solution: sequential resonance
RT assignment, secondary structure, and global fold.";
RL Biochemistry 28:5946-5954(1989).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=1734952; DOI=10.1021/bi00119a009;
RA Akke M., Drakenberg T., Chazin W.J.;
RT "Three-dimensional solution structure of Ca(2+)-loaded porcine calbindin
RT D9k determined by nuclear magnetic resonance spectroscopy.";
RL Biochemistry 31:1011-1020(1992).
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; L13068; AAA81524.1; -; mRNA.
DR PIR; A56802; KLPGI.
DR RefSeq; NP_999305.1; NM_214140.2.
DR PDB; 1CB1; NMR; -; A=2-79.
DR PDB; 1RSW; NMR; -; A=58-69.
DR PDB; 1RSX; NMR; -; A=58-69.
DR PDBsum; 1CB1; -.
DR PDBsum; 1RSW; -.
DR PDBsum; 1RSX; -.
DR AlphaFoldDB; P02632; -.
DR BMRB; P02632; -.
DR SMR; P02632; -.
DR STRING; 9823.ENSSSCP00000012930; -.
DR iPTMnet; P02632; -.
DR PaxDb; P02632; -.
DR PeptideAtlas; P02632; -.
DR Ensembl; ENSSSCT00000049484; ENSSSCP00000044898; ENSSSCG00000012147.
DR Ensembl; ENSSSCT00005017057; ENSSSCP00005010155; ENSSSCG00005011062.
DR Ensembl; ENSSSCT00025106500; ENSSSCP00025047835; ENSSSCG00025076777.
DR Ensembl; ENSSSCT00030094994; ENSSSCP00030043771; ENSSSCG00030067914.
DR Ensembl; ENSSSCT00035037989; ENSSSCP00035015143; ENSSSCG00035028726.
DR Ensembl; ENSSSCT00040019610; ENSSSCP00040008147; ENSSSCG00040014599.
DR Ensembl; ENSSSCT00045036439; ENSSSCP00045025361; ENSSSCG00045021309.
DR Ensembl; ENSSSCT00050082448; ENSSSCP00050035378; ENSSSCG00050060521.
DR Ensembl; ENSSSCT00055005889; ENSSSCP00055004598; ENSSSCG00055003046.
DR Ensembl; ENSSSCT00060107358; ENSSSCP00060047607; ENSSSCG00060077852.
DR Ensembl; ENSSSCT00065084948; ENSSSCP00065037096; ENSSSCG00065061938.
DR Ensembl; ENSSSCT00070040170; ENSSSCP00070033670; ENSSSCG00070020255.
DR GeneID; 397265; -.
DR KEGG; ssc:397265; -.
DR CTD; 795; -.
DR VGNC; VGNC:92548; S100G.
DR eggNOG; ENOG502T3Z3; Eukaryota.
DR GeneTree; ENSGT00530000064238; -.
DR InParanoid; P02632; -.
DR OrthoDB; 1558629at2759; -.
DR EvolutionaryTrace; P02632; -.
DR Proteomes; UP000008227; Chromosome X.
DR Proteomes; UP000314985; Unassembled WGS sequence.
DR Bgee; ENSSSCG00000012147; Expressed in duodenum and 32 other tissues.
DR ExpressionAtlas; P02632; baseline and differential.
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 3D-structure; Acetylation; Calcium; Direct protein sequencing;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Vitamin D.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:476518"
FT CHAIN 2..79
FT /note="Protein S100-G"
FT /id="PRO_0000144029"
FT CHAIN 3..79
FT /note="Protein S100-G, minor isoform"
FT /id="PRO_0000275899"
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:476518"
FT MOD_RES 3
FT /note="N-acetylalanine; in Protein S100-G, minor isoform"
FT /evidence="ECO:0000269|PubMed:476518"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02634"
FT CONFLICT 62
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:1CB1"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1CB1"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:1CB1"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:1CB1"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1CB1"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:1CB1"
SQ SEQUENCE 79 AA; 8929 MW; E8AB53BF23BD2D57 CRC64;
MSAQKSPAEL KSIFEKYAAK EGDPNQLSKE ELKQLIQAEF PSLLKGPRTL DDLFQELDKN
GDGEVSFEEF QVLVKKISQ
