ID   FABPI_MOUSE             Reviewed;         132 AA.
AC   P55050;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 169.
DE   RecName: Full=Fatty acid-binding protein, intestinal;
DE   AltName: Full=Fatty acid-binding protein 2;
DE   AltName: Full=Intestinal-type fatty acid-binding protein;
DE            Short=I-FABP;
GN   Name=Fabp2; Synonyms=Fabpi;
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 [MRNA].
RX   PubMed=1739433; DOI=10.1089/dna.1992.11.31;
RA   Green R.P., Sacchettini J.C., Jackson K.E., Cohn S.M., Gordon J.I.;
RT   "The mouse intestinal fatty acid binding protein gene: nucleotide sequence,
RT   pattern of developmental and regional expression, and proposed structure of
RT   its protein product.";
RL   DNA Cell Biol. 11:31-41(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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   [4]
RP   FUNCTION.
RX   PubMed=11023988; DOI=10.1096/fj.99-0959com;
RA   Vassileva G., Huwyler L., Poirier K., Agellon L.B., Toth M.J.;
RT   "The intestinal fatty acid binding protein is not essential for dietary fat
RT   absorption in mice.";
RL   FASEB J. 14:2040-2046(2000).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=9277406; DOI=10.1152/ajpgi.1997.273.2.g289;
RA   Poirier H., Niot I., Degrace P., Monnot M.C., Bernard A., Besnard P.;
RT   "Fatty acid regulation of fatty acid-binding protein expression in the
RT   small intestine.";
RL   Am. J. Physiol. 273:G289-G295(1997).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: FABPs are thought to play a role in the intracellular
CC       transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is
CC       probably involved in triglyceride-rich lipoprotein synthesis. Binds
CC       saturated long-chain fatty acids with a high affinity, but binds with a
CC       lower affinity to unsaturated long-chain fatty acids. FABP2 may also
CC       help maintain energy homeostasis by functioning as a lipid sensor.
CC       {ECO:0000269|PubMed:11023988}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in the small intestine. Highest
CC       expression levels in the proximal ileum. {ECO:0000269|PubMed:9277406}.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC       ligand in its interior. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000305}.
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DR   EMBL; M65034; AAA37589.1; -; mRNA.
DR   EMBL; AK007995; BAB25397.1; -; mRNA.
DR   EMBL; BC013457; AAH13457.1; -; mRNA.
DR   CCDS; CCDS17813.1; -.
DR   RefSeq; NP_032006.1; NM_007980.3.
DR   AlphaFoldDB; P55050; -.
DR   SMR; P55050; -.
DR   STRING; 10090.ENSMUSP00000023820; -.
DR   iPTMnet; P55050; -.
DR   PhosphoSitePlus; P55050; -.
DR   jPOST; P55050; -.
DR   PaxDb; 10090-ENSMUSP00000023820; -.
DR   PeptideAtlas; P55050; -.
DR   ProteomicsDB; 275582; -.
DR   Antibodypedia; 26669; 642 antibodies from 40 providers.
DR   DNASU; 14079; -.
DR   Ensembl; ENSMUST00000023820.6; ENSMUSP00000023820.6; ENSMUSG00000023057.6.
DR   GeneID; 14079; -.
DR   KEGG; mmu:14079; -.
DR   UCSC; uc008rex.2; mouse.
DR   AGR; MGI:95478; -.
DR   CTD; 2169; -.
DR   MGI; MGI:95478; Fabp2.
DR   VEuPathDB; HostDB:ENSMUSG00000023057; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   GeneTree; ENSGT00800000124172; -.
DR   HOGENOM; CLU_113772_3_0_1; -.
DR   InParanoid; P55050; -.
DR   OMA; GINLMKR; -.
DR   OrthoDB; 2946847at2759; -.
DR   PhylomeDB; P55050; -.
DR   TreeFam; TF316894; -.
DR   Reactome; R-MMU-163560; Triglyceride catabolism.
DR   BioGRID-ORCS; 14079; 0 hits in 78 CRISPR screens.
DR   PRO; PR:P55050; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P55050; Protein.
DR   Bgee; ENSMUSG00000023057; Expressed in small intestine Peyer's patch and 50 other cell types or tissues.
DR   ExpressionAtlas; P55050; baseline and differential.
DR   GO; GO:0045179; C:apical cortex; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005902; C:microvillus; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR   GO; GO:0036041; F:long-chain fatty acid binding; ISO:MGI.
DR   GO; GO:0005324; F:long-chain fatty acid transporter activity; ISO:MGI.
DR   GO; GO:0006631; P:fatty acid metabolic process; ISO:MGI.
DR   GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR   GO; GO:0050892; P:intestinal absorption; ISO:MGI.
DR   GO; GO:0098856; P:intestinal lipid absorption; ISO:MGI.
DR   GO; GO:0015909; P:long-chain fatty acid transport; ISO:MGI.
DR   CDD; cd19445; FABP2; 1.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR031272; FABP2.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   InterPro; IPR031259; ILBP.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   PANTHER; PTHR11955; FATTY ACID BINDING PROTEIN; 1.
DR   PANTHER; PTHR11955:SF89; FATTY ACID-BINDING PROTEIN, INTESTINAL; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; Lipocalins; 1.
DR   PROSITE; PS00214; FABP; 1.
DR   Genevisible; P55050; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Lipid-binding; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02693"
FT   CHAIN           2..132
FT                   /note="Fatty acid-binding protein, intestinal"
FT                   /id="PRO_0000067329"
FT   BINDING         83
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:P02693"
FT   BINDING         83
FT                   /ligand="tetradecanoate"
FT                   /ligand_id="ChEBI:CHEBI:30807"
FT                   /evidence="ECO:0000250|UniProtKB:P02693"
FT   BINDING         107
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:P02693"
FT   BINDING         107
FT                   /ligand="tetradecanoate"
FT                   /ligand_id="ChEBI:CHEBI:30807"
FT                   /evidence="ECO:0000250|UniProtKB:P02693"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P02693"
SQ   SEQUENCE   132 AA;  15126 MW;  E02001EE47267456 CRC64;
     MAFDGTWKVD RNENYEKFME KMGINVMKRK LGAHDNLKLT ITQDGNKFTV KESSNFRNID
     VVFELGVNFP YSLADGTELT GAWTIEGNKL IGKFTRVDNG KELIAVREVS GNELIQTYTY
     EGVEAKRFFK KE
//