ID   FABPI_PIG               Reviewed;         132 AA.
AC   Q45KW7; Q56G53;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 97.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Jiang Y.Z., Li X.W.;
RT   "Sus scrofa fatty acid binding protein 2, intestinal (FABP2).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AY960624; AAX62516.1; -; mRNA.
DR   EMBL; DQ126268; AAZ38898.1; -; Genomic_DNA.
DR   RefSeq; NP_001026950.1; NM_001031780.1.
DR   AlphaFoldDB; Q45KW7; -.
DR   SMR; Q45KW7; -.
DR   STRING; 9823.ENSSSCP00000025576; -.
DR   PaxDb; Q45KW7; -.
DR   PeptideAtlas; Q45KW7; -.
DR   Ensembl; ENSSSCT00000040297; ENSSSCP00000040315; ENSSSCG00000037272.
DR   Ensembl; ENSSSCT00015047140; ENSSSCP00015018645; ENSSSCG00015035376.
DR   Ensembl; ENSSSCT00025099584; ENSSSCP00025043867; ENSSSCG00025072440.
DR   Ensembl; ENSSSCT00030000310; ENSSSCP00030000196; ENSSSCG00030000197.
DR   Ensembl; ENSSSCT00035058651; ENSSSCP00035023579; ENSSSCG00035044137.
DR   Ensembl; ENSSSCT00040073465; ENSSSCP00040031442; ENSSSCG00040054179.
DR   Ensembl; ENSSSCT00045016426; ENSSSCP00045011346; ENSSSCG00045009670.
DR   Ensembl; ENSSSCT00050051410; ENSSSCP00050021573; ENSSSCG00050038128.
DR   Ensembl; ENSSSCT00055028547; ENSSSCP00055022747; ENSSSCG00055014467.
DR   Ensembl; ENSSSCT00060069225; ENSSSCP00060029792; ENSSSCG00060050880.
DR   Ensembl; ENSSSCT00065021537; ENSSSCP00065008727; ENSSSCG00065016241.
DR   Ensembl; ENSSSCT00070044357; ENSSSCP00070037374; ENSSSCG00070022309.
DR   GeneID; 595106; -.
DR   KEGG; ssc:595106; -.
DR   CTD; 2169; -.
DR   VGNC; VGNC:87871; FABP2.
DR   eggNOG; KOG4015; Eukaryota.
DR   GeneTree; ENSGT00800000124172; -.
DR   HOGENOM; CLU_113772_3_0_1; -.
DR   InParanoid; Q45KW7; -.
DR   OMA; VHRSENY; -.
DR   OrthoDB; 1436007at2759; -.
DR   TreeFam; TF316894; -.
DR   Reactome; R-SSC-163560; Triglyceride catabolism.
DR   Proteomes; UP000008227; Chromosome 8.
DR   Proteomes; UP000314985; Chromosome 8.
DR   Bgee; ENSSSCG00000037272; Expressed in duodenum and 2 other tissues.
DR   ExpressionAtlas; Q45KW7; baseline.
DR   Genevisible; Q45KW7; SS.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR   GO; GO:0036041; F:long-chain fatty acid binding; IBA:GO_Central.
DR   GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR   GO; GO:0098856; P:intestinal lipid absorption; IEA:Ensembl.
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   2: Evidence at transcript 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_0000231037"
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   CONFLICT        21
FT                   /note="K -> R (in Ref. 1; AAZ38898)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   132 AA;  15217 MW;  BBDD825EB619B98C CRC64;
     MAFDGAWKID RNENYDKFME KMGINVVKRK LAAHDNLKLI ITQEGNKFTV KESSTFRNIE
     IVFELGVTFN YSLADGTELT GNWNLEGNKL VGKFQRVDNG KELNTVREII GDEMVQTYVY
     EGVEAKRIFK KN