FABP6_PIG
ID FABP6_PIG Reviewed; 128 AA.
AC P10289;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Gastrotropin;
DE Short=GT;
DE AltName: Full=Fatty acid-binding protein 6;
DE AltName: Full=Ileal lipid-binding protein;
DE Short=ILBP;
DE AltName: Full=Porcine ileal peptide;
DE Short=PIP;
GN Name=FABP6; Synonyms=ILBP, ILLBP;
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].
RX PubMed=2584215; DOI=10.1016/s0021-9258(19)47054-3;
RA Gantz I., Nothwehr S.F., Lucey M., Sacchettini J.C., Delvalle J.,
RA Banaszak L.J., Naud M., Gordon J.I., Yamada T.;
RT "Gastrotropin: not an enterooxyntin but a member of a family of cytoplasmic
RT hydrophobic ligand binding proteins.";
RL J. Biol. Chem. 264:20248-20254(1989).
RN [2]
RP PROTEIN SEQUENCE OF 2-128, ACETYLATION AT ALA-2, AND FUNCTION.
RX PubMed=3049572; DOI=10.1016/s0021-9258(18)68204-3;
RA Walz D.A., Wider M.D., Snow J.W., Dass C., Desiderio D.M.;
RT "The complete amino acid sequence of porcine gastrotropin, an ileal protein
RT which stimulates gastric acid and pepsinogen secretion.";
RL J. Biol. Chem. 263:14189-14195(1988).
RN [3]
RP STRUCTURE BY NMR IN COMPLEX WITH BILE ACID.
RX PubMed=8805562; DOI=10.1016/s0969-2126(96)00086-x;
RA Luecke C., Zhang F., Rueterjans H., Hamilton J.A., Sacchettini J.C.;
RT "Flexibility is a likely determinant of binding specificity in the case of
RT ileal lipid binding protein.";
RL Structure 4:785-800(1996).
RN [4]
RP STRUCTURE BY NMR, BILE ACID-BINDING, AND DOMAIN.
RX PubMed=10806391; DOI=10.1046/j.1432-1327.2000.01307.x;
RA Luecke C., Zhang F., Hamilton J.A., Sacchettini J.C., Rueterjans H.;
RT "Solution structure of ileal lipid binding protein in complex with
RT glycocholate.";
RL Eur. J. Biochem. 267:2929-2938(2000).
CC -!- FUNCTION: Binds to bile acids and is involved in enterohepatic bile
CC acid metabolism. Required for efficient apical to basolateral transport
CC of conjugated bile acids in ileal enterocytes (By similarity).
CC Stimulates gastric acid and pepsinogen secretion.
CC {ECO:0000250|UniProtKB:P51162, ECO:0000269|PubMed:10806391,
CC ECO:0000269|PubMed:3049572}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P50119}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P50119}.
CC -!- TISSUE SPECIFICITY: Found exclusively in the ileum and to a lesser
CC extent in distal jejunum.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC ligand in its interior. Can bind at least two ligands per molecule,
CC however, the stoichiometry is debated. {ECO:0000250|UniProtKB:P51161,
CC ECO:0000269|PubMed:10806391}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA77657.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J05136; AAA77657.1; ALT_INIT; mRNA.
DR PIR; A32675; A32675.
DR RefSeq; NP_999380.2; NM_214215.2.
DR PDB; 1EAL; NMR; -; A=2-128.
DR PDB; 1EIO; NMR; -; A=2-128.
DR PDBsum; 1EAL; -.
DR PDBsum; 1EIO; -.
DR AlphaFoldDB; P10289; -.
DR BMRB; P10289; -.
DR SMR; P10289; -.
DR STRING; 9823.ENSSSCP00000018050; -.
DR iPTMnet; P10289; -.
DR PaxDb; P10289; -.
DR PeptideAtlas; P10289; -.
DR GeneID; 397423; -.
DR KEGG; ssc:397423; -.
DR CTD; 2172; -.
DR eggNOG; KOG4015; Eukaryota.
DR InParanoid; P10289; -.
DR OrthoDB; 1440574at2759; -.
DR EvolutionaryTrace; P10289; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Lipid transport; Lipid-binding; Membrane; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3049572"
FT CHAIN 2..128
FT /note="Gastrotropin"
FT /id="PRO_0000067382"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:3049572"
FT CONFLICT 119
FT /note="T -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:1EAL"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:1EAL"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:1EAL"
FT STRAND 37..53
FT /evidence="ECO:0007829|PDB:1EAL"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1EAL"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:1EAL"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1EAL"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1EAL"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1EAL"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1EAL"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:1EAL"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1EAL"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:1EAL"
SQ SEQUENCE 128 AA; 14219 MW; 849D5A446731C3CA CRC64;
MAFTGKYEIE SEKNYDEFMK RLALPSDAID KARNLKIISE VKQDGQNFTW SQQYPGGHSI
TNTFTIGKEC DIETIGGKKF KATVQMEGGK VVVNSPNYHH TAEIVDGKLV EVSTVGGVTY
ERVSKKLA
