ID   FABP6_RABIT             Reviewed;         128 AA.
AC   P50119;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 102.
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, ILLBP;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=New Zealand white; TISSUE=Liver;
RX   PubMed=8774740; DOI=10.1111/j.1432-1033.1996.0887u.x;
RA   Stengelin S., Apel S., Becker W., Maier M., Rosenberger J., Bewersdorf U.,
RA   Girbig F., Weyland C., Wess G., Kramer W.;
RT   "The rabbit ileal lipid-binding protein. Gene cloning and functional
RT   expression of the recombinant protein.";
RL   Eur. J. Biochem. 239:887-896(1996).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9370354; DOI=10.1111/j.1432-1033.1997.00456.x;
RA   Kramer W., Wess G., Bewersdorf U., Corsiero D., Girbig F., Weyland C.,
RA   Stengelin S., Enhsen A., Bock K., Kleine H., Le Dreau M.A., Schaefer H.L.;
RT   "Topological photoaffinity labeling of the rabbit ileal Na+/bile-salt-
RT   cotransport system.";
RL   Eur. J. Biochem. 249:456-464(1997).
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:0000269|PubMed:8774740}. Membrane;
CC       Peripheral membrane protein {ECO:0000269|PubMed:8774740}; Cytoplasmic
CC       side {ECO:0000269|PubMed:9370354}. Note=Associated with ileal brush
CC       border membranes. {ECO:0000269|PubMed:8774740}.
CC   -!- TISSUE SPECIFICITY: Expressed in ileum. {ECO:0000269|PubMed:8774740}.
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; Z54345; CAA91158.1; -; Genomic_DNA.
DR   RefSeq; XP_008253566.1; XM_008255344.2.
DR   AlphaFoldDB; P50119; -.
DR   SMR; P50119; -.
DR   STRING; 9986.ENSOCUP00000004716; -.
DR   Ensembl; ENSOCUT00000005434; ENSOCUP00000004716; ENSOCUG00000005435.
DR   GeneID; 100352143; -.
DR   KEGG; ocu:100352143; -.
DR   CTD; 2172; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   GeneTree; ENSGT00940000157139; -.
DR   InParanoid; P50119; -.
DR   OrthoDB; 1440574at2759; -.
DR   Proteomes; UP000001811; Chromosome 3.
DR   Bgee; ENSOCUG00000005435; Expressed in blood and 1 other tissue.
DR   ExpressionAtlas; P50119; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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   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_0000067383"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P10289"
SQ   SEQUENCE   128 AA;  14404 MW;  DFB34B41B74272CD CRC64;
     MAFTGKFEME SEKNYDEFMK LLGLPSDVVE KSRNIKIVTE IKQDGQDFTW SHHYSGGQIM
     TNKFTIGKES EIQTFGGKKF KAVVNMEGGK VVANFPNYQH TSEIKGDKLV EVSSIGGVTY
     ERVSKRLA