ID   FABP6_BOVIN             Reviewed;         128 AA.
AC   Q3T0Z2;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
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;
GN   Name=FABP6; Synonyms=ILBP;
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 [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. Stimulates gastric acid
CC       and pepsinogen secretion (By similarity).
CC       {ECO:0000250|UniProtKB:P10289, ECO:0000250|UniProtKB:P51162}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P80020}.
CC       Membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:P50119};
CC       Cytoplasmic side {ECO:0000250|UniProtKB:P50119}.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC       ligands in its interior. Can bind at least two ligands per molecule,
CC       however, the stoichiometry is debated. {ECO:0000250|UniProtKB:P10289,
CC       ECO:0000250|UniProtKB:P51161}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000305}.
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DR   EMBL; BC102199; AAI02200.1; -; mRNA.
DR   RefSeq; NP_001069143.1; NM_001075675.2.
DR   AlphaFoldDB; Q3T0Z2; -.
DR   SMR; Q3T0Z2; -.
DR   STRING; 9913.ENSBTAP00000014054; -.
DR   PaxDb; Q3T0Z2; -.
DR   GeneID; 514650; -.
DR   KEGG; bta:514650; -.
DR   CTD; 2172; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   HOGENOM; CLU_113772_4_0_1; -.
DR   InParanoid; Q3T0Z2; -.
DR   OrthoDB; 1440574at2759; -.
DR   TreeFam; TF330348; -.
DR   Proteomes; UP000009136; 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.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Lipid-binding; Membrane; Reference proteome;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P10289"
FT   CHAIN           2..128
FT                   /note="Gastrotropin"
FT                   /id="PRO_0000274030"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P10289"
SQ   SEQUENCE   128 AA;  14460 MW;  F5D4FA128C3D9A4C CRC64;
     MAFTGKYETE SEKNYDEFMK RLGLSSDRIE KGRNFKVISE IQQDGQNFTW SQHYPGGHSI
     SNNFTIGKET EMETVGNKKF KVTVKMEGGK VVVDSANYHH TVEIVDGKLV EVSTFGGVIY
     ERVSKKVA