ID   FABPL_RHASA             Reviewed;         126 AA.
AC   P80856;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 78.
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   Rhamdia sapo (South American catfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Pimelodidae; Rhamdia.
OX   NCBI_TaxID=55673;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-126, AND ACETYLATION AT ALA-2.
RC   TISSUE=Liver;
RX   PubMed=9370361; DOI=10.1111/j.1432-1033.1997.00510.x;
RA   Di Pietro S.M., Dell'Angelica E.C., Veerkamp J.H., Sterin-Speziale N.,
RA   Santome J.A.;
RT   "Amino acid sequence, binding properties and evolutionary relationships of
RT   the basic liver fatty-acid-binding protein from the catfish Rhamdia sapo.";
RL   Eur. J. Biochem. 249:510-517(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 34-53; 58-78 AND 97-122, AND CHARACTERIZATION.
RC   TISSUE=Liver;
RX   PubMed=8829803; DOI=10.1016/0305-0491(95)02074-8;
RA   Di Pietro S.M., Dell'Angelica E.C., Schleicher C.H., Santome J.A.;
RT   "Purification and structural characterization of a fatty acid-binding
RT   protein from the liver of the catfish Rhamdia sapo.";
RL   Comp. Biochem. Physiol. 113B:503-509(1996).
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 this L-FABP binds only one
CC       fatty acid/molecule. Has more affinity for trans-parinaric acid than
CC       for cis-parinaric acid.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Liver.
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; P80856; -.
DR   SMR; P80856; -.
DR   iPTMnet; P80856; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; 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-binding;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9370361"
FT   CHAIN           2..126
FT                   /note="Fatty acid-binding protein, liver"
FT                   /id="PRO_0000067341"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:9370361"
SQ   SEQUENCE   126 AA;  13988 MW;  8E755CE75EBA101A CRC64;
     MAFSGTWQVY AQENYEEFLR AISLPEDVIK LAKDVKPVTE IQQTGNDFVI TSKTPGKSVT
     NSFTIGKEAE ITTMDGRKLK CIVKLEGGKL ISETEKFSHK QEIKGGEMIE TLTVAGTTMV
     RKSKKV