ID   FABPL_RHIAE             Reviewed;         126 AA.
AC   P83409;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Fatty acid-binding protein, liver;
DE   AltName: Full=Fatty acid-binding protein 1;
DE   AltName: Full=Liver basic FABP;
DE            Short=Lb-FABP;
DE   AltName: Full=Liver-type fatty acid-binding protein;
DE            Short=L-FABP;
GN   Name=fabp1;
OS   Rhinella arenarum (Argentine common toad) (Bufo arenarum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Rhinella.
OX   NCBI_TaxID=38577;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-126, FUNCTION, SUBUNIT, ACETYLATION AT ALA-2, MASS
RP   SPECTROMETRY, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC   TISSUE=Hepatocyte;
RX   PubMed=12846568; DOI=10.1021/bi034213n;
RA   Di Pietro S.M., Corsico B., Perduca M., Monaco H.L., Santome J.A.;
RT   "Structural and biochemical characterization of toad liver fatty acid-
RT   binding protein.";
RL   Biochemistry 42:8192-8203(2003).
CC   -!- FUNCTION: Involved in intracellular lipid transport. Binds free fatty
CC       acids and their coenzyme A derivatives, lysophospholipids,
CC       prostaglandins, retinoids, bilirubin and some other small molecules.
CC       {ECO:0000269|PubMed:12846568}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12846568}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC       ligands in its interior.
CC   -!- MASS SPECTROMETRY: Mass=13987; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12846568};
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000305}.
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DR   PDB; 1P6P; X-ray; 2.50 A; A=2-126.
DR   PDBsum; 1P6P; -.
DR   AlphaFoldDB; P83409; -.
DR   SMR; P83409; -.
DR   iPTMnet; P83409; -.
DR   EvolutionaryTrace; P83409; -.
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   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Lipid transport; Lipid-binding; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12846568"
FT   CHAIN           2..126
FT                   /note="Fatty acid-binding protein, liver"
FT                   /id="PRO_0000067340"
FT   BINDING         57
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:12846568"
FT   STRAND          5..14
FT                   /evidence="ECO:0007829|PDB:1P6P"
FT   HELIX           15..22
FT                   /evidence="ECO:0007829|PDB:1P6P"
FT   HELIX           26..32
FT                   /evidence="ECO:0007829|PDB:1P6P"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:1P6P"
FT   STRAND          45..54
FT                   /evidence="ECO:0007829|PDB:1P6P"
FT   STRAND          57..64
FT                   /evidence="ECO:0007829|PDB:1P6P"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:1P6P"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:1P6P"
FT   STRAND          79..85
FT                   /evidence="ECO:0007829|PDB:1P6P"
FT   STRAND          87..93
FT                   /evidence="ECO:0007829|PDB:1P6P"
FT   STRAND          95..104
FT                   /evidence="ECO:0007829|PDB:1P6P"
FT   STRAND          107..114
FT                   /evidence="ECO:0007829|PDB:1P6P"
FT   STRAND          117..125
FT                   /evidence="ECO:0007829|PDB:1P6P"
SQ   SEQUENCE   126 AA;  14080 MW;  CD7D1FEA68C7BF4F CRC64;
     MAFNGTWNVY AQENYENFLR TVGLPEDIIK VAKDVNPVIE IEQNGNEFVV TSKTPKQTHS
     NSFTVGKESE ITSMDGKKIK VTVQLEGGKL ICKSDKFSHI QEVNGDEMVE KITIGSSTLT
     RKSKRV