FABP6_RAT
ID FABP6_RAT Reviewed; 128 AA.
AC P80020;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Gastrotropin;
DE Short=GT;
DE AltName: Full=14 kDa bile acid-binding protein;
DE AltName: Full=Fatty acid-binding protein 6;
DE AltName: Full=I-BABP;
DE AltName: Full=Ileal lipid-binding protein;
DE Short=ILBP;
DE AltName: Full=Intestinal 15 kDa protein;
DE Short=I-15P;
GN Name=Fabp6; Synonyms=Ilbp, Illbp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8422242; DOI=10.1006/bbrc.1993.1027;
RA Fujii H., Nomura M., Kanda T., Amano O., Iseki S., Hatakeyama K., Ono T.;
RT "Cloning of a cDNA encoding rat intestinal 15 kDa protein and its tissue
RT distribution.";
RL Biochem. Biophys. Res. Commun. 190:175-180(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], BILE ACID-BINDING, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Ileum;
RX PubMed=8197128; DOI=10.1073/pnas.91.11.4741;
RA Gong Y.Z., Everett E.T., Schwartz D.A., Norris J.S., Wilson F.A.;
RT "Molecular cloning, tissue distribution, and expression of a 14-kDa bile
RT acid-binding protein from rat ileal cytosol.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4741-4745(1994).
RN [3]
RP PROTEIN SEQUENCE OF 2-128, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Intestinal mucosa;
RX PubMed=2029905; DOI=10.1111/j.1432-1033.1991.tb15968.x;
RA Kanda T., Odani S., Tomoi M., Matsubara Y., Ono T.;
RT "Primary structure of a 15-kDa protein from rat intestinal epithelium.
RT Sequence similarity to fatty-acid-binding proteins.";
RL Eur. J. Biochem. 197:759-768(1991).
RN [4]
RP PROTEIN SEQUENCE OF 21-31; 88-103 AND 109-128.
RC TISSUE=Ileum;
RX PubMed=2059206; DOI=10.1016/0006-291x(91)90659-u;
RA Vodenlich A.D. Jr., Gong Y.-Z., Geoghegan K.F., Lin M.C., Lanzetti A.J.,
RA Wilson F.A.;
RT "Identification of the 14 kDa bile acid transport protein of rat ileal
RT cytosol as gastrotropin.";
RL Biochem. Biophys. Res. Commun. 177:1147-1154(1991).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P10289, ECO:0000250|UniProtKB:P51162,
CC ECO:0000269|PubMed:8197128}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2029905,
CC ECO:0000269|PubMed:8197128}. Membrane; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P50119}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P50119}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in ileum; also expressed in
CC ovary. {ECO:0000269|PubMed:2029905, ECO:0000269|PubMed:8197128}.
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; S52878; AAB24948.1; -; mRNA.
DR EMBL; L22788; AAA57155.1; -; mRNA.
DR PIR; JC1413; JC1413.
DR RefSeq; NP_058794.1; NM_017098.1.
DR AlphaFoldDB; P80020; -.
DR SMR; P80020; -.
DR STRING; 10116.ENSRNOP00000005205; -.
DR iPTMnet; P80020; -.
DR PaxDb; P80020; -.
DR GeneID; 25440; -.
DR KEGG; rno:25440; -.
DR UCSC; RGD:2592; rat.
DR CTD; 2172; -.
DR RGD; 2592; Fabp6.
DR eggNOG; KOG4015; Eukaryota.
DR InParanoid; P80020; -.
DR PhylomeDB; P80020; -.
DR Reactome; R-RNO-159418; Recycling of bile acids and salts.
DR Reactome; R-RNO-163560; Triglyceride catabolism.
DR PRO; PR:P80020; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; IEP:RGD.
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 Acetylation; Cytoplasm; Direct protein sequencing; Lipid transport;
KW Lipid-binding; Membrane; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2029905"
FT CHAIN 2..128
FT /note="Gastrotropin"
FT /id="PRO_0000067384"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2029905"
FT CONFLICT 16..17
FT /note="DE -> ED (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 26..27
FT /note="DE -> ED (in Ref. 2; AAB24948/AAA57155)"
FT /evidence="ECO:0000305"
FT CONFLICT 26..27
FT /note="DE -> GD (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 14544 MW; 66580FC781DE4B3D CRC64;
MAFTGKYEFE SEKNYDEFMK RLGLPDEVIE RGRNFKIITE VQQDGENFTW SQSYSGGNIM
SNKFTIGKEC EMQTMGGKKF KATVKMEGGK VVADFPNYHQ TSEVVGDKLV EISTIGDVTY
ERVSKRVA
