ID   FABPL_GINCI             Reviewed;         132 AA.
AC   P80049;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Fatty acid-binding protein, liver;
DE   AltName: Full=Liver-type fatty acid-binding protein;
DE            Short=L-FABP;
OS   Ginglymostoma cirratum (Nurse shark) (Squalus cirratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes;
OC   Ginglymostomatidae; Ginglymostoma.
OX   NCBI_TaxID=7801;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT VAL-1.
RC   TISSUE=Liver;
RX   PubMed=1735421; DOI=10.1111/j.1432-1033.1992.tb16553.x;
RA   Medzihradszky K.F., Gibson B.W., Kaur S., Yu Z., Medzihradszky D.,
RA   Burlingame A.L., Bass N.M.;
RT   "The primary structure of fatty-acid-binding protein from nurse shark
RT   liver. Structural and evolutionary relationship to the mammalian fatty-
RT   acid-binding protein family.";
RL   Eur. J. Biochem. 203:327-339(1992).
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 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   PIR; S20297; S20297.
DR   AlphaFoldDB; P80049; -.
DR   SMR; P80049; -.
DR   iPTMnet; P80049; -.
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   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   PANTHER; PTHR11955; PTHR11955; 1.
DR   Pfam; PF00061; Lipocalin; 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   Phosphoprotein; Transport.
FT   CHAIN           1..132
FT                   /note="Fatty acid-binding protein, liver"
FT                   /id="PRO_0000067346"
FT   MOD_RES         1
FT                   /note="N-acetylvaline"
FT                   /evidence="ECO:0000269|PubMed:1735421"
FT   MOD_RES         19
FT                   /note="Phosphotyrosine; by Tyr-kinases"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   132 AA;  15079 MW;  2AFDEA2C0BE2095F CRC64;
     VEAFLGSWKL QKSHNFDEYM KNLDVSLAQR KVATTVKPKT IISLDGDVIT IKTESTFKST
     NIQFKLAEEF DETTADNRTT KTTVKLENGK LVQTQRWDGK ETTLVRELQD GKLILTCTMG
     DVVCTREYVR EQ