ID   FABPL_LEPPA             Reviewed;         125 AA.
AC   P82289;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Fatty acid-binding protein, liver;
DE   AltName: Full=Fatty acid-binding protein 1;
DE   AltName: Full=Liver basic fatty acid-binding protein;
DE            Short=Lb-FABP;
DE            Short=Liver basic FABP;
DE   AltName: Full=Liver-type fatty acid-binding protein;
DE            Short=L-FABP;
GN   Name=fabp1;
OS   Lepidosiren paradoxus (South American lungfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Dipnomorpha; Ceratodontiformes; Lepidosirenoidei; Lepidosirenidae;
OC   Lepidosiren.
OX   NCBI_TaxID=7883;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP   DISULFIDE BOND, AND ACETYLATION AT ALA-1.
RC   TISSUE=Liver;
RX   PubMed=11361145; DOI=10.1006/abbi.2001.2277;
RA   Di Pietro S.M., Santome J.A.;
RT   "Structural and biochemical characterization of the lungfish (Lepidosiren
RT   paradoxa) liver basic fatty acid binding protein.";
RL   Arch. Biochem. Biophys. 388:81-90(2001).
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. Binds one trans-parinaric
CC       acid molecule or two cis-parinaric acid molecules. Affinity for
CC       mono- and polyunsaturated fatty acids is higher than that for saturated
CC       ones. Affinity for fatty acid coenzyme A derivatives, lysophosphatidic
CC       acid, lysophospholipds, retinoids, bilirubin and bile salts is similar
CC       to or higher than that for fatty acids. Affinity for prostaglandins,
CC       peroxisomal proliferators, bezafibrate and clofibrate is moderate to
CC       low. {ECO:0000269|PubMed:11361145}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11361145}.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC       ligands in its interior. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=13495; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11361145};
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P82289; -.
DR   SMR; P82289; -.
DR   iPTMnet; P82289; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR   GO; GO:0019841; F:retinol 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; Disulfide bond;
KW   Lipid transport; Lipid-binding; Retinol-binding; Transport; Vitamin A.
FT   CHAIN           1..125
FT                   /note="Fatty acid-binding protein, liver"
FT                   /id="PRO_0000067349"
FT   MOD_RES         1
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:11361145"
FT   DISULFID        80..91
FT                   /evidence="ECO:0000269|PubMed:11361145"
SQ   SEQUENCE   125 AA;  13904 MW;  16726151E8D064D5 CRC64;
     AFSGTWQVYA QENYEAFLKV IGVAEDIIPH AKEIKPTIEI QQSGNSFTVT STAQKKSTTN
     TFTIGKEAEI TTMNGNKLRC TINMEDGKLV CKTEKFSHIQ EVQGEEMIET LTSGSATLIR
     RSRKV