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 02-SEP-2026, entry version 169. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; P02632; -. DR BMRB; P02632; -. DR MDposit; P02632; -. DR SMR; P02632; -. DR FunCoup; P02632; 96. DR STRING; 9823.ENSSSCP00000012930; -. DR iPTMnet; P02632; -. DR PaxDb; 9823-ENSSSCP00000012930; -. DR PeptideAtlas; P02632; -. DR Ensembl; ENSSSCT00000049484.2; ENSSSCP00000044898.1; ENSSSCG00000012147.5. DR Ensembl; ENSSSCT00005017057.1; ENSSSCP00005010155.1; ENSSSCG00005011062.1. DR Ensembl; ENSSSCT00025106500.1; ENSSSCP00025047835.1; ENSSSCG00025076777.1. DR Ensembl; ENSSSCT00030094994.1; ENSSSCP00030043771.1; ENSSSCG00030067914.1. DR Ensembl; ENSSSCT00035037989.1; ENSSSCP00035015143.1; ENSSSCG00035028726.1. DR Ensembl; ENSSSCT00040019610.1; ENSSSCP00040008147.1; ENSSSCG00040014599.1. DR Ensembl; ENSSSCT00045036439.1; ENSSSCP00045025361.1; ENSSSCG00045021309.1. DR Ensembl; ENSSSCT00050082448.1; ENSSSCP00050035378.1; ENSSSCG00050060521.1. DR Ensembl; ENSSSCT00055005889.1; ENSSSCP00055004598.1; ENSSSCG00055003046.1. DR Ensembl; ENSSSCT00060107358.1; ENSSSCP00060047607.1; ENSSSCG00060077852.1. DR Ensembl; ENSSSCT00065084948.1; ENSSSCP00065037096.1; ENSSSCG00065061938.1. DR Ensembl; ENSSSCT00070040170.1; ENSSSCP00070033670.1; ENSSSCG00070020255.1. 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; 26525at2759; -. DR EvolutionaryTrace; P02632; -. DR Proteomes; UP000008227; Chromosome X. DR Bgee; ENSSSCG00000012147; Expressed in duodenum and 32 other cell types or tissues. DR ExpressionAtlas; P02632; baseline and differential. 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 GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR CDD; cd00213; S-100; 1. 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; 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 PDBsum; 1CB1; -. DR PDBsum; 1RSW; -. DR PDBsum; 1RSX; -. 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 //