ID   FABPI_XENLA             Reviewed;         132 AA.
AC   Q91775;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Intestine;
RX   PubMed=8293885; DOI=10.1006/dbio.1994.1006;
RA   Shi Y.B., Hayes W.P.;
RT   "Thyroid hormone-dependent regulation of the intestinal fatty acid-binding
RT   protein gene during amphibian metamorphosis.";
RL   Dev. Biol. 161:48-58(1994).
CC   -!- FUNCTION: FABP are thought to play a role in the intracellular
CC       transport of long-chain fatty acids and their acyl-CoA esters.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; L19946; AAC38012.1; -; mRNA.
DR   PIR; I51450; I51450.
DR   RefSeq; NP_001079346.1; NM_001085877.1.
DR   AlphaFoldDB; Q91775; -.
DR   SMR; Q91775; -.
DR   GeneID; 378690; -.
DR   KEGG; xla:378690; -.
DR   CTD; 378690; -.
DR   Xenbase; XB-GENE-864901; fabp2.L.
DR   OMA; MMKRKLG; -.
DR   OrthoDB; 1436007at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 378690; Expressed in intestine and 9 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005504; F:fatty acid binding; IEA:InterPro.
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"
FT   CHAIN           2..132
FT                   /note="Fatty acid-binding protein, intestinal"
FT                   /id="PRO_0000067331"
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"
SQ   SEQUENCE   132 AA;  15252 MW;  B2CA47C79B6D8AD9 CRC64;
     MAFDGTWKVD RSENYEKFME VMGVNIVKRK LGAHDNLKVI IQQDGNNFTV KESSTFRNIE
     IKFTLAQPFE YSLADGTELN GAWFLQDNQL LGTFTRKDNG KVLQTTRQII GDELVQTYEY
     EGTESKRIFK RG