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Fatty acid-binding protein, intestinal (Fatty acid-binding protein 2) (Intestinal-type fatty acid-binding protein) (I-FABP)

 FABPI_HUMAN             Reviewed;         132 AA.
P12104; Q2NKJ1;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
13-FEB-2019, entry version 167.
RecName: Full=Fatty acid-binding protein, intestinal;
AltName: Full=Fatty acid-binding protein 2;
AltName: Full=Intestinal-type fatty acid-binding protein;
Short=I-FABP;
Name=FABP2; Synonyms=FABPI;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2824476;
Sweetser D.A., Birkenmeier E.H., Klisak I.J., Zollman S.,
Sparkes R.S., Mohandas T., Lusis A.J., Gordon J.I.;
"The human and rodent intestinal fatty acid binding protein genes. A
comparative analysis of their structure, expression, and linkage
relationships.";
J. Biol. Chem. 262:16060-16071(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-55.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY.
PubMed=14563446; DOI=10.1016/S0009-9120(03)00096-1;
Pelsers M.M.A.L., Namiot Z., Kisielewski W., Namiot A.,
Januszkiewicz M., Hermens W.T., Glatz J.F.C.;
"Intestinal-type and liver-type fatty acid-binding protein in the
intestine. Tissue distribution and clinical utility.";
Clin. Biochem. 36:529-535(2003).
[5]
INDUCTION BY EGF.
PubMed=10070036;
Darimont C., Gradoux N., de Pover A.;
"Epidermal growth factor regulates fatty acid uptake and metabolism in
Caco-2 cells.";
Am. J. Physiol. 276:G606-G612(1999).
[6]
MUTAGENESIS OF LEU-39; GLU-64; LEU-65; VAL-67; LEU-90 AND VAL-123.
PubMed=14567680; DOI=10.1021/bi0301688;
Rajabzadeh M., Kao J., Frieden C.;
"Consequences of single-site mutations in the intestinal fatty acid
binding protein.";
Biochemistry 42:12192-12199(2003).
[7]
STRUCTURE BY NMR.
TISSUE=Intestine;
PubMed=9204553; DOI=10.1023/A:1018666522787;
Zhang F., Luecke C., Baier L.J., Sacchettini J.C., Hamilton J.A.;
"Solution structure of human intestinal fatty acid binding protein:
implications for ligand entry and exit.";
J. Biomol. NMR 9:213-228(1997).
[8]
STRUCTURE BY NMR OF VARIANT THR-55.
PubMed=12809489; DOI=10.1021/bi0273617;
Zhang F., Luecke C., Baier L.J., Sacchettini J.C., Hamilton J.A.;
"Solution structure of human intestinal fatty acid binding protein
with a naturally-occurring single amino acid substitution (A54T) that
is associated with altered lipid metabolism.";
Biochemistry 42:7339-7347(2003).
[9]
VARIANT THR-55.
PubMed=7883976; DOI=10.1172/JCI117778;
Baier L.J., Sacchettini J.C., Knowler W.C., Eads J., Paolisso G.,
Tataranni P.A., Mochizuki H., Bennett P.H., Bogardus C., Prochazka M.;
"An amino acid substitution in the human intestinal fatty acid binding
protein is associated with increased fatty acid binding, increased fat
oxidation, and insulin resistance.";
J. Clin. Invest. 95:1281-1287(1995).
[10]
VARIANT THR-55.
PubMed=12899384;
Kunsan X., Taisan Z., Weiping J., Duoqi S., Wei D., Jie L., Junxi L.,
Rong Z.;
"The association of Ala54Thr variant of intestinal fatty acid binding
protein gene with general and regional adipose tissue depots.";
Chin. Med. Sci. J. 14:46-51(1999).
-!- FUNCTION: FABP are thought to play a role in the intracellular
transport of long-chain fatty acids and their acyl-CoA esters.
FABP2 is probably involved in triglyceride-rich lipoprotein
synthesis. Binds saturated long-chain fatty acids with a high
affinity, but binds with a lower affinity to unsaturated long-
chain fatty acids. FABP2 may also help maintain energy homeostasis
by functioning as a lipid sensor.
-!- INTERACTION:
O95994:AGR2; NbExp=6; IntAct=EBI-3905109, EBI-712648;
Q9NYB0:TERF2IP; NbExp=2; IntAct=EBI-3905109, EBI-750109;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Expressed in the small intestine and at much
lower levels in the large intestine. Highest expression levels in
the jejunum. {ECO:0000269|PubMed:14563446}.
-!- INDUCTION: By EGF. {ECO:0000269|PubMed:10070036}.
-!- DOMAIN: Forms a beta-barrel structure that accommodates the
hydrophobic ligand in its interior.
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M18079; AAA52417.1; -; Genomic_DNA.
EMBL; AC092656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC069466; AAH69466.1; -; mRNA.
EMBL; BC069617; AAH69617.1; -; mRNA.
EMBL; BC069625; AAH69625.1; -; mRNA.
EMBL; BC069637; AAH69637.1; -; mRNA.
EMBL; BC111791; AAI11792.1; -; mRNA.
CCDS; CCDS3712.1; -.
PIR; A29781; FZHUI.
RefSeq; NP_000125.2; NM_000134.3.
UniGene; Hs.282265; -.
PDB; 1KZW; NMR; -; A=2-132.
PDB; 1KZX; NMR; -; A=2-132.
PDB; 2MJI; NMR; -; A=2-132.
PDB; 2MO5; NMR; -; A=2-132.
PDB; 3AKM; X-ray; 1.90 A; A/B/C/D=2-132.
PDB; 3IFB; NMR; -; A=2-132.
PDBsum; 1KZW; -.
PDBsum; 1KZX; -.
PDBsum; 2MJI; -.
PDBsum; 2MO5; -.
PDBsum; 3AKM; -.
PDBsum; 3IFB; -.
ProteinModelPortal; P12104; -.
SMR; P12104; -.
BioGrid; 108467; 3.
IntAct; P12104; 3.
STRING; 9606.ENSP00000274024; -.
BindingDB; P12104; -.
ChEMBL; CHEMBL4879; -.
DrugBank; DB04557; Arachidonic Acid.
DrugBank; DB00783; Estradiol.
DrugBank; DB01050; Ibuprofen.
DrugBank; DB08231; MYRISTIC ACID.
DrugBank; DB03796; Palmitic Acid.
DrugBank; DB01138; Sulfinpyrazone.
SwissLipids; SLP:000001520; -.
iPTMnet; P12104; -.
PhosphoSitePlus; P12104; -.
BioMuta; FABP2; -.
DMDM; 119805; -.
jPOST; P12104; -.
PaxDb; P12104; -.
PeptideAtlas; P12104; -.
PRIDE; P12104; -.
ProteomicsDB; 52825; -.
DNASU; 2169; -.
Ensembl; ENST00000274024; ENSP00000274024; ENSG00000145384.
GeneID; 2169; -.
KEGG; hsa:2169; -.
UCSC; uc003icw.4; human.
CTD; 2169; -.
DisGeNET; 2169; -.
EuPathDB; HostDB:ENSG00000145384.3; -.
GeneCards; FABP2; -.
H-InvDB; HIX0004469; -.
HGNC; HGNC:3556; FABP2.
HPA; CAB047325; -.
HPA; CAB047326; -.
HPA; HPA034607; -.
MIM; 134640; gene.
neXtProt; NX_P12104; -.
PharmGKB; PA27957; -.
eggNOG; KOG4015; Eukaryota.
eggNOG; ENOG4111US8; LUCA.
HOGENOM; HOG000004829; -.
HOVERGEN; HBG005633; -.
InParanoid; P12104; -.
KO; K08751; -.
OrthoDB; 1436007at2759; -.
PhylomeDB; P12104; -.
TreeFam; TF316894; -.
Reactome; R-HSA-163560; Triglyceride catabolism.
ChiTaRS; FABP2; human.
EvolutionaryTrace; P12104; -.
GeneWiki; FABP2; -.
GenomeRNAi; 2169; -.
PRO; PR:P12104; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000145384; Expressed in 90 organ(s), highest expression level in intestine.
Genevisible; P12104; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005504; F:fatty acid binding; TAS:ProtInc.
GO; GO:0036041; F:long-chain fatty acid binding; IDA:GO_Central.
GO; GO:0098856; P:intestinal lipid absorption; IMP:GO_Central.
GO; GO:0019433; P:triglyceride catabolic process; TAS:Reactome.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR031272; FABP2.
InterPro; IPR000463; Fatty_acid-bd.
InterPro; IPR031259; ILBP.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
PANTHER; PTHR11955; PTHR11955; 1.
PANTHER; PTHR11955:SF89; PTHR11955:SF89; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR00178; FATTYACIDBP.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00214; FABP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Lipid-binding; Polymorphism; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P02693}.
CHAIN 2 132 Fatty acid-binding protein, intestinal.
/FTId=PRO_0000067328.
BINDING 83 83 Fatty acid. {ECO:0000250}.
BINDING 107 107 Fatty acid. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P02693}.
VARIANT 55 55 A -> T (found in 29% of the population;
associated with increased plasma insulin
concentration, increased fat oxidation
and insulin resistance; 2-fold greater
affinity for long-chain fatty acids;
dbSNP:rs1799883).
{ECO:0000269|PubMed:12809489,
ECO:0000269|PubMed:12899384,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7883976}.
/FTId=VAR_002379.
MUTAGEN 39 39 L->G: Reduced stability.
{ECO:0000269|PubMed:14567680}.
MUTAGEN 64 64 E->G: Localized reduction in stability.
{ECO:0000269|PubMed:14567680}.
MUTAGEN 65 65 L->A: Reduced stability.
{ECO:0000269|PubMed:14567680}.
MUTAGEN 65 65 L->G: Reduced stability.
{ECO:0000269|PubMed:14567680}.
MUTAGEN 67 67 V->G: Localized reduction in stability.
{ECO:0000269|PubMed:14567680}.
MUTAGEN 90 90 L->G: Reduced stability.
{ECO:0000269|PubMed:14567680}.
MUTAGEN 123 123 V->G: Reduced stability.
{ECO:0000269|PubMed:14567680}.
STRAND 5 14 {ECO:0000244|PDB:3AKM}.
HELIX 15 22 {ECO:0000244|PDB:3AKM}.
HELIX 26 32 {ECO:0000244|PDB:3AKM}.
TURN 33 35 {ECO:0000244|PDB:3IFB}.
STRAND 38 44 {ECO:0000244|PDB:3AKM}.
STRAND 47 53 {ECO:0000244|PDB:3AKM}.
STRAND 58 64 {ECO:0000244|PDB:3AKM}.
STRAND 69 72 {ECO:0000244|PDB:3AKM}.
STRAND 74 76 {ECO:0000244|PDB:1KZW}.
STRAND 78 86 {ECO:0000244|PDB:3AKM}.
STRAND 89 96 {ECO:0000244|PDB:3AKM}.
TURN 97 99 {ECO:0000244|PDB:3AKM}.
STRAND 102 110 {ECO:0000244|PDB:3AKM}.
STRAND 113 120 {ECO:0000244|PDB:3AKM}.
STRAND 123 131 {ECO:0000244|PDB:3AKM}.
SEQUENCE 132 AA; 15207 MW; 68330E3D81792CAF CRC64;
MAFDSTWKVD RSENYDKFME KMGVNIVKRK LAAHDNLKLT ITQEGNKFTV KESSAFRNIE
VVFELGVTFN YNLADGTELR GTWSLEGNKL IGKFKRTDNG NELNTVREII GDELVQTYVY
EGVEAKRIFK KD


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