FABP6_MOUSE
ID FABP6_MOUSE Reviewed; 128 AA.
AC P51162; Q5SRT9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
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=Illbp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DBA/2J; TISSUE=Liver;
RX PubMed=8089185; DOI=10.1083/jcb.126.6.1547;
RA Crossman M.W., Hauft S.M., Gordon J.I.;
RT "The mouse ileal lipid-binding protein gene: a model for studying axial
RT patterning during gut morphogenesis.";
RL J. Cell Biol. 126:1547-1564(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=23251388; DOI=10.1371/journal.pone.0050810;
RA Praslickova D., Torchia E.C., Sugiyama M.G., Magrane E.J., Zwicker B.L.,
RA Kolodzieyski L., Agellon L.B.;
RT "The ileal lipid binding protein is required for efficient absorption and
RT transport of bile acids in the distal portion of the murine small
RT intestine.";
RL PLoS ONE 7:E50810-E50810(2012).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=25754072; DOI=10.1262/jrd.2014-139;
RA Duggavathi R., Siddappa D., Schuermann Y., Pansera M., Menard I.J.,
RA Praslickova D., Agellon L.B.;
RT "The fatty acid binding protein 6 gene (Fabp6) is expressed in murine
RT granulosa cells and is involved in ovulatory response to
RT superstimulation.";
RL J. Reprod. Dev. 61:237-240(2015).
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 (PubMed:23251388).
CC Stimulates gastric acid and pepsinogen secretion (By similarity).
CC {ECO:0000250|UniProtKB:P10289, ECO:0000269|PubMed:23251388}.
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 -!- TISSUE SPECIFICITY: Expressed in ovary granulosa and luteal cells.
CC {ECO:0000269|PubMed:25754072}.
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; U00938; AAC27352.1; -; Genomic_DNA.
DR EMBL; AL670472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466575; EDL33855.1; -; Genomic_DNA.
DR EMBL; BC119289; AAI19290.1; -; mRNA.
DR EMBL; BC120767; AAI20768.1; -; mRNA.
DR CCDS; CCDS24560.1; -.
DR PIR; A54797; A54797.
DR RefSeq; NP_032401.1; NM_008375.2.
DR AlphaFoldDB; P51162; -.
DR SMR; P51162; -.
DR BioGRID; 200650; 1.
DR IntAct; P51162; 1.
DR STRING; 10090.ENSMUSP00000020672; -.
DR PhosphoSitePlus; P51162; -.
DR MaxQB; P51162; -.
DR PaxDb; P51162; -.
DR PeptideAtlas; P51162; -.
DR PRIDE; P51162; -.
DR ProteomicsDB; 271548; -.
DR Antibodypedia; 1989; 246 antibodies from 30 providers.
DR DNASU; 16204; -.
DR Ensembl; ENSMUST00000020672; ENSMUSP00000020672; ENSMUSG00000020405.
DR GeneID; 16204; -.
DR KEGG; mmu:16204; -.
DR UCSC; uc007imt.2; mouse.
DR CTD; 2172; -.
DR MGI; MGI:96565; Fabp6.
DR VEuPathDB; HostDB:ENSMUSG00000020405; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000157139; -.
DR HOGENOM; CLU_113772_4_0_1; -.
DR InParanoid; P51162; -.
DR OMA; CEMQTMG; -.
DR OrthoDB; 1440574at2759; -.
DR PhylomeDB; P51162; -.
DR TreeFam; TF330348; -.
DR Reactome; R-MMU-159418; Recycling of bile acids and salts.
DR Reactome; R-MMU-163560; Triglyceride catabolism.
DR BioGRID-ORCS; 16204; 2 hits in 77 CRISPR screens.
DR PRO; PR:P51162; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P51162; protein.
DR Bgee; ENSMUSG00000020405; Expressed in crypt of Lieberkuhn of small intestine and 49 other tissues.
DR Genevisible; P51162; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0008206; P:bile acid metabolic process; TAS:MGI.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Lipid transport; Lipid-binding; Membrane;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P10289"
FT CHAIN 2..128
FT /note="Gastrotropin"
FT /id="PRO_0000067381"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P10289"
SQ SEQUENCE 128 AA; 14486 MW; 9FF64BDD0AFA2909 CRC64;
MAFSGKYEFE SEKNYDEFMK RLGLPGDVIE RGRNFKIITE VQQDGQDFTW SQSYSGGNIM
SNKFTIGKEC EMQTMGGKKF KATVKMEGGK VVAEFPNYHQ TSEVVGDKLV EISTIGDVTY
ERVSKRLA
