ID   FABPL_LITCT             Reviewed;         126 AA.
AC   P0C241;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Fatty acid-binding protein, liver;
DE   AltName: Full=Fatty acid-binding protein 1;
DE   AltName: Full=Liver-type fatty acid-binding protein;
DE            Short=L-FABP;
GN   Name=fabp1;
OS   Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8400;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-126, ACETYLATION AT ALA-2, AND VARIANT SER-17.
RC   TISSUE=Liver;
RX   PubMed=9880806; DOI=10.1093/oxfordjournals.jbchem.a022247;
RA   Baba K., Abe T.K., Tsunasawa S., Odani S.;
RT   "Characterization and primary structure of a fatty acid-binding protein and
RT   its isoforms from the liver of the Amphibia, Rana catesbeiana.";
RL   J. Biochem. 125:115-122(1999).
CC   -!- FUNCTION: Binds free fatty acids and their coenzyme A derivatives,
CC       bilirubin, and some other small molecules in the cytoplasm. May be
CC       involved in intracellular lipid transport (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC       ligands 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   AlphaFoldDB; P0C241; -.
DR   SMR; P0C241; -.
DR   iPTMnet; P0C241; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   InterPro; IPR031259; ILBP.
DR   PANTHER; PTHR11955; PTHR11955; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00214; FABP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Lipid transport;
KW   Lipid-binding; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9880806"
FT   CHAIN           2..126
FT                   /note="Fatty acid-binding protein, liver"
FT                   /id="PRO_0000260300"
FT   BINDING         77
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:9880806"
FT   VARIANT         17
FT                   /note="P -> S (in isoform II)"
FT                   /evidence="ECO:0000269|PubMed:9880806"
SQ   SEQUENCE   126 AA;  13853 MW;  6A2234BA0739CD5B CRC64;
     MAFSGIWNVY SQENYEPFLK AVGVPDDIIK VAKDIKPVIE IQQNGNDFVV TLKTPKNSQS
     NSFTVGQEAE ITSAGGKKFK VTVNLEGGKL ICKSDTFSHI QEVNGDEMVE QITIGSTTLI
     RKSKRS