ID   FABP2_AMBME             Reviewed;         126 AA.
AC   P81400;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Fatty acid-binding protein 2, liver;
DE   AltName: Full=Liver basic FABP;
DE            Short=LB-FABP;
DE   AltName: Full=Liver-type fatty acid-binding protein;
DE            Short=L-FABP;
OS   Ambystoma mexicanum (Axolotl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Caudata; Salamandroidea; Ambystomatidae; Ambystoma.
OX   NCBI_TaxID=8296;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-126.
RC   TISSUE=Liver;
RX   PubMed=9914484; DOI=10.1046/j.1432-1327.1999.00015.x;
RA   Di Pietro S.M., Veerkamp J.H., Santome J.A.;
RT   "Isolation, amino acid sequence determination and binding properties of two
RT   fatty-acid-binding proteins from axolotl (Ambistoma mexicanum) liver.
RT   Evolutionary relationship.";
RL   Eur. J. Biochem. 259:127-134(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CHOLATE AND OLEATE.
RX   PubMed=16555310; DOI=10.1002/prot.20961;
RA   Capaldi S., Guariento M., Perduca M., Di Pietro S.M., Santome J.A.,
RA   Monaco H.L.;
RT   "Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding
RT   protein bound to cholic and oleic acid.";
RL   Proteins 64:79-88(2006).
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). The
CC       specificity of axolotl L-FABP differs from that of LB-FABP. Binds 2
CC       ligands per protein molecule. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC       ligands in its interior.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000305}.
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DR   PDB; 2FT9; X-ray; 2.50 A; A=2-126.
DR   PDB; 2FTB; X-ray; 2.00 A; A=2-126.
DR   PDBsum; 2FT9; -.
DR   PDBsum; 2FTB; -.
DR   AlphaFoldDB; P81400; -.
DR   SMR; P81400; -.
DR   EvolutionaryTrace; P81400; -.
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   3D-structure; Cytoplasm; Direct protein sequencing; Lipid-binding;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9914484"
FT   CHAIN           2..126
FT                   /note="Fatty acid-binding protein 2, liver"
FT                   /id="PRO_0000067344"
FT   BINDING         54..56
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /ligand_label="1"
FT   BINDING         99..101
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /ligand_label="2"
FT   BINDING         121
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16555310"
FT   STRAND          5..13
FT                   /evidence="ECO:0007829|PDB:2FTB"
FT   HELIX           15..22
FT                   /evidence="ECO:0007829|PDB:2FTB"
FT   HELIX           26..32
FT                   /evidence="ECO:0007829|PDB:2FTB"
FT   STRAND          38..53
FT                   /evidence="ECO:0007829|PDB:2FTB"
FT   STRAND          58..64
FT                   /evidence="ECO:0007829|PDB:2FTB"
FT   STRAND          69..72
FT                   /evidence="ECO:0007829|PDB:2FTB"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:2FT9"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:2FTB"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:2FTB"
FT   STRAND          89..93
FT                   /evidence="ECO:0007829|PDB:2FTB"
FT   STRAND          95..104
FT                   /evidence="ECO:0007829|PDB:2FTB"
FT   STRAND          107..114
FT                   /evidence="ECO:0007829|PDB:2FTB"
FT   STRAND          117..125
FT                   /evidence="ECO:0007829|PDB:2FTB"
SQ   SEQUENCE   126 AA;  13875 MW;  130A84C12D0EB1AF CRC64;
     MPFNGTWQVY SQENYEAFLR AVGLPEDIIN VAKDINPIIE IQQNGDNFVV TSKTPNQSVT
     NSFTIGKEAE ITSMGGKKIK CTVVLEGGKL VSKTDQFSHI QEVKGNEMVE TLTVGGATLI
     RRSKRV