FABPI_HUMAN
ID FABPI_HUMAN Reviewed; 132 AA.
AC P12104; Q2NKJ1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 184.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2824476; DOI=10.1016/s0021-9258(18)47696-x;
RA Sweetser D.A., Birkenmeier E.H., Klisak I.J., Zollman S., Sparkes R.S.,
RA Mohandas T., Lusis A.J., Gordon J.I.;
RT "The human and rodent intestinal fatty acid binding protein genes. A
RT comparative analysis of their structure, expression, and linkage
RT relationships.";
RL J. Biol. Chem. 262:16060-16071(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-55.
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 TISSUE SPECIFICITY.
RX PubMed=14563446; DOI=10.1016/s0009-9120(03)00096-1;
RA Pelsers M.M.A.L., Namiot Z., Kisielewski W., Namiot A., Januszkiewicz M.,
RA Hermens W.T., Glatz J.F.C.;
RT "Intestinal-type and liver-type fatty acid-binding protein in the
RT intestine. Tissue distribution and clinical utility.";
RL Clin. Biochem. 36:529-535(2003).
RN [5]
RP INDUCTION BY EGF.
RX PubMed=10070036; DOI=10.1152/ajpgi.1999.276.3.g606;
RA Darimont C., Gradoux N., de Pover A.;
RT "Epidermal growth factor regulates fatty acid uptake and metabolism in
RT Caco-2 cells.";
RL Am. J. Physiol. 276:G606-G612(1999).
RN [6]
RP MUTAGENESIS OF LEU-39; GLU-64; LEU-65; VAL-67; LEU-90 AND VAL-123.
RX PubMed=14567680; DOI=10.1021/bi0301688;
RA Rajabzadeh M., Kao J., Frieden C.;
RT "Consequences of single-site mutations in the intestinal fatty acid binding
RT protein.";
RL Biochemistry 42:12192-12199(2003).
RN [7]
RP STRUCTURE BY NMR.
RC TISSUE=Intestine;
RX PubMed=9204553; DOI=10.1023/a:1018666522787;
RA Zhang F., Luecke C., Baier L.J., Sacchettini J.C., Hamilton J.A.;
RT "Solution structure of human intestinal fatty acid binding protein:
RT implications for ligand entry and exit.";
RL J. Biomol. NMR 9:213-228(1997).
RN [8]
RP STRUCTURE BY NMR OF VARIANT THR-55.
RX PubMed=12809489; DOI=10.1021/bi0273617;
RA Zhang F., Luecke C., Baier L.J., Sacchettini J.C., Hamilton J.A.;
RT "Solution structure of human intestinal fatty acid binding protein with a
RT naturally-occurring single amino acid substitution (A54T) that is
RT associated with altered lipid metabolism.";
RL Biochemistry 42:7339-7347(2003).
RN [9]
RP VARIANT THR-55.
RX PubMed=7883976; DOI=10.1172/jci117778;
RA Baier L.J., Sacchettini J.C., Knowler W.C., Eads J., Paolisso G.,
RA Tataranni P.A., Mochizuki H., Bennett P.H., Bogardus C., Prochazka M.;
RT "An amino acid substitution in the human intestinal fatty acid binding
RT protein is associated with increased fatty acid binding, increased fat
RT oxidation, and insulin resistance.";
RL J. Clin. Invest. 95:1281-1287(1995).
RN [10]
RP VARIANT THR-55.
RX PubMed=12899384;
RA Kunsan X., Taisan Z., Weiping J., Duoqi S., Wei D., Jie L., Junxi L.,
RA Rong Z.;
RT "The association of Ala54Thr variant of intestinal fatty acid binding
RT protein gene with general and regional adipose tissue depots.";
RL Chin. Med. Sci. J. 14:46-51(1999).
CC -!- FUNCTION: FABP 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 -!- INTERACTION:
CC P12104; O95994: AGR2; NbExp=6; IntAct=EBI-3905109, EBI-712648;
CC P12104; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-3905109, EBI-750109;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in the small intestine and at much lower
CC levels in the large intestine. Highest expression levels in the
CC jejunum. {ECO:0000269|PubMed:14563446}.
CC -!- INDUCTION: By EGF. {ECO:0000269|PubMed:10070036}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC ligand in its interior.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; M18079; AAA52417.1; -; Genomic_DNA.
DR EMBL; AC092656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069466; AAH69466.1; -; mRNA.
DR EMBL; BC069617; AAH69617.1; -; mRNA.
DR EMBL; BC069625; AAH69625.1; -; mRNA.
DR EMBL; BC069637; AAH69637.1; -; mRNA.
DR EMBL; BC111791; AAI11792.1; -; mRNA.
DR CCDS; CCDS3712.1; -.
DR PIR; A29781; FZHUI.
DR RefSeq; NP_000125.2; NM_000134.3.
DR PDB; 1KZW; NMR; -; A=2-132.
DR PDB; 1KZX; NMR; -; A=2-132.
DR PDB; 2MJI; NMR; -; A=2-132.
DR PDB; 2MO5; NMR; -; A=2-132.
DR PDB; 3AKM; X-ray; 1.90 A; A/B/C/D=2-132.
DR PDB; 3IFB; NMR; -; A=2-132.
DR PDB; 6L7K; NMR; -; A=2-132.
DR PDBsum; 1KZW; -.
DR PDBsum; 1KZX; -.
DR PDBsum; 2MJI; -.
DR PDBsum; 2MO5; -.
DR PDBsum; 3AKM; -.
DR PDBsum; 3IFB; -.
DR PDBsum; 6L7K; -.
DR AlphaFoldDB; P12104; -.
DR BMRB; P12104; -.
DR SMR; P12104; -.
DR BioGRID; 108467; 45.
DR IntAct; P12104; 3.
DR STRING; 9606.ENSP00000274024; -.
DR BindingDB; P12104; -.
DR ChEMBL; CHEMBL4879; -.
DR DrugBank; DB04557; Arachidonic Acid.
DR DrugBank; DB09213; Dexibuprofen.
DR DrugBank; DB00783; Estradiol.
DR DrugBank; DB13952; Estradiol acetate.
DR DrugBank; DB13953; Estradiol benzoate.
DR DrugBank; DB13954; Estradiol cypionate.
DR DrugBank; DB13955; Estradiol dienanthate.
DR DrugBank; DB13956; Estradiol valerate.
DR DrugBank; DB01050; Ibuprofen.
DR DrugBank; DB08231; Myristic acid.
DR DrugBank; DB03796; Palmitic Acid.
DR DrugBank; DB01138; Sulfinpyrazone.
DR DrugCentral; P12104; -.
DR SwissLipids; SLP:000001520; -.
DR iPTMnet; P12104; -.
DR PhosphoSitePlus; P12104; -.
DR BioMuta; FABP2; -.
DR DMDM; 119805; -.
DR jPOST; P12104; -.
DR MassIVE; P12104; -.
DR PaxDb; P12104; -.
DR PeptideAtlas; P12104; -.
DR PRIDE; P12104; -.
DR ProteomicsDB; 52825; -.
DR Antibodypedia; 26669; 593 antibodies from 40 providers.
DR CPTC; P12104; 2 antibodies.
DR DNASU; 2169; -.
DR Ensembl; ENST00000274024.4; ENSP00000274024.3; ENSG00000145384.4.
DR GeneID; 2169; -.
DR KEGG; hsa:2169; -.
DR UCSC; uc003icw.4; human.
DR CTD; 2169; -.
DR DisGeNET; 2169; -.
DR GeneCards; FABP2; -.
DR HGNC; HGNC:3556; FABP2.
DR HPA; ENSG00000145384; Tissue enriched (intestine).
DR MIM; 134640; gene.
DR neXtProt; NX_P12104; -.
DR PharmGKB; PA27957; -.
DR VEuPathDB; HostDB:ENSG00000145384; -.
DR eggNOG; KOG4015; Eukaryota.
DR HOGENOM; CLU_113772_3_0_1; -.
DR InParanoid; P12104; -.
DR OrthoDB; 1436007at2759; -.
DR PhylomeDB; P12104; -.
DR TreeFam; TF316894; -.
DR PathwayCommons; P12104; -.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR SignaLink; P12104; -.
DR SIGNOR; P12104; -.
DR BioGRID-ORCS; 2169; 15 hits in 1034 CRISPR screens.
DR ChiTaRS; FABP2; human.
DR EvolutionaryTrace; P12104; -.
DR GeneWiki; FABP2; -.
DR GenomeRNAi; 2169; -.
DR Pharos; P12104; Tchem.
DR PRO; PR:P12104; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P12104; protein.
DR Bgee; ENSG00000145384; Expressed in mucosa of transverse colon and 60 other tissues.
DR Genevisible; P12104; HS.
DR GO; GO:0045179; C:apical cortex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0036041; F:long-chain fatty acid binding; IDA:GO_Central.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IEA:Ensembl.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0098856; P:intestinal lipid absorption; IMP:GO_Central.
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; PTHR11955; 1.
DR PANTHER; PTHR11955:SF89; PTHR11955:SF89; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Lipid-binding; Reference proteome;
KW 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_0000067328"
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"
FT VARIANT 55
FT /note="A -> T (found in 29% of the population; associated
FT with increased plasma insulin concentration, increased fat
FT oxidation and insulin resistance; 2-fold greater affinity
FT for long-chain fatty acids; dbSNP:rs1799883)"
FT /evidence="ECO:0000269|PubMed:12809489,
FT ECO:0000269|PubMed:12899384, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7883976"
FT /id="VAR_002379"
FT MUTAGEN 39
FT /note="L->G: Reduced stability."
FT /evidence="ECO:0000269|PubMed:14567680"
FT MUTAGEN 64
FT /note="E->G: Localized reduction in stability."
FT /evidence="ECO:0000269|PubMed:14567680"
FT MUTAGEN 65
FT /note="L->A: Reduced stability."
FT /evidence="ECO:0000269|PubMed:14567680"
FT MUTAGEN 65
FT /note="L->G: Reduced stability."
FT /evidence="ECO:0000269|PubMed:14567680"
FT MUTAGEN 67
FT /note="V->G: Localized reduction in stability."
FT /evidence="ECO:0000269|PubMed:14567680"
FT MUTAGEN 90
FT /note="L->G: Reduced stability."
FT /evidence="ECO:0000269|PubMed:14567680"
FT MUTAGEN 123
FT /note="V->G: Reduced stability."
FT /evidence="ECO:0000269|PubMed:14567680"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:3AKM"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:3AKM"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:3AKM"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:3IFB"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:3AKM"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:3AKM"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:3AKM"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3AKM"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1KZW"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:3AKM"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:3AKM"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:3AKM"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:3AKM"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:3AKM"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:3AKM"
SQ SEQUENCE 132 AA; 15207 MW; 68330E3D81792CAF CRC64;
MAFDSTWKVD RSENYDKFME KMGVNIVKRK LAAHDNLKLT ITQEGNKFTV KESSAFRNIE
VVFELGVTFN YNLADGTELR GTWSLEGNKL IGKFKRTDNG NELNTVREII GDELVQTYVY
EGVEAKRIFK KD
