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Fatty acid-binding protein, liver (Fatty acid-binding protein 1) (Liver basic FABP) (Lb-FABP) (Liver-type fatty acid-binding protein) (L-FABP)

 FABPL_RHIAE             Reviewed;         126 AA.
P83409;
10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 84.
RecName: Full=Fatty acid-binding protein, liver;
AltName: Full=Fatty acid-binding protein 1;
AltName: Full=Liver basic FABP;
Short=Lb-FABP;
AltName: Full=Liver-type fatty acid-binding protein;
Short=L-FABP;
Name=fabp1;
Rhinella arenarum (Argentine common toad) (Bufo arenarum).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae;
Rhinella.
NCBI_TaxID=38577;
[1]
PROTEIN SEQUENCE OF 2-126, FUNCTION, SUBUNIT, ACETYLATION AT ALA-2,
MASS SPECTROMETRY, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
TISSUE=Hepatocyte;
PubMed=12846568; DOI=10.1021/bi034213n;
Di Pietro S.M., Corsico B., Perduca M., Monaco H.L., Santome J.A.;
"Structural and biochemical characterization of toad liver fatty acid-
binding protein.";
Biochemistry 42:8192-8203(2003).
-!- FUNCTION: Involved in intracellular lipid transport. Binds free
fatty acids and their coenzyme A derivatives, lysophospholipids,
prostaglandins, retinoids, bilirubin and some other small
molecules. {ECO:0000269|PubMed:12846568}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12846568}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- DOMAIN: Forms a beta-barrel structure that accommodates
hydrophobic ligands in its interior.
-!- MASS SPECTROMETRY: Mass=13987; Method=Electrospray; Range=2-126;
Evidence={ECO:0000269|PubMed:12846568};
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
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PDB; 1P6P; X-ray; 2.50 A; A=2-126.
PDBsum; 1P6P; -.
ProteinModelPortal; P83409; -.
SMR; P83409; -.
iPTMnet; P83409; -.
HOVERGEN; HBG005633; -.
EvolutionaryTrace; P83409; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0005215; F:transporter activity; IEA:InterPro.
GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR000463; Fatty_acid-bd.
InterPro; IPR031259; ILBP.
PANTHER; PTHR11955; PTHR11955; 1.
PRINTS; PR00178; FATTYACIDBP.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00214; FABP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
Lipid transport; Lipid-binding; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12846568}.
CHAIN 2 126 Fatty acid-binding protein, liver.
/FTId=PRO_0000067340.
BINDING 57 57 Cholate 1. {ECO:0000250}.
BINDING 77 77 Cholate 2. {ECO:0000250}.
BINDING 99 99 Cholate 2. {ECO:0000250}.
BINDING 101 101 Cholate 2. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:12846568}.
STRAND 5 14 {ECO:0000244|PDB:1P6P}.
HELIX 15 22 {ECO:0000244|PDB:1P6P}.
HELIX 26 32 {ECO:0000244|PDB:1P6P}.
STRAND 38 43 {ECO:0000244|PDB:1P6P}.
STRAND 45 54 {ECO:0000244|PDB:1P6P}.
STRAND 57 64 {ECO:0000244|PDB:1P6P}.
STRAND 69 71 {ECO:0000244|PDB:1P6P}.
TURN 73 75 {ECO:0000244|PDB:1P6P}.
STRAND 79 85 {ECO:0000244|PDB:1P6P}.
STRAND 87 93 {ECO:0000244|PDB:1P6P}.
STRAND 95 104 {ECO:0000244|PDB:1P6P}.
STRAND 107 114 {ECO:0000244|PDB:1P6P}.
STRAND 117 125 {ECO:0000244|PDB:1P6P}.
SEQUENCE 126 AA; 14080 MW; CD7D1FEA68C7BF4F CRC64;
MAFNGTWNVY AQENYENFLR TVGLPEDIIK VAKDVNPVIE IEQNGNEFVV TSKTPKQTHS
NSFTVGKESE ITSMDGKKIK VTVQLEGGKL ICKSDKFSHI QEVNGDEMVE KITIGSSTLT
RKSKRV


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