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Fatty acid-binding protein, liver (Fatty acid-binding protein 1) (Liver-type fatty acid-binding protein) (L-FABP) (Squalene- and sterol-carrier protein) (SCP) (Z-protein) (p14)

 FABPL_RAT               Reviewed;         127 AA.
P02692;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
22-NOV-2017, entry version 168.
RecName: Full=Fatty acid-binding protein, liver;
AltName: Full=Fatty acid-binding protein 1;
AltName: Full=Liver-type fatty acid-binding protein;
Short=L-FABP;
AltName: Full=Squalene- and sterol-carrier protein;
Short=SCP;
AltName: Full=Z-protein;
AltName: Full=p14;
Name=Fabp1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
PROTEIN SEQUENCE.
PubMed=7084456; DOI=10.1016/0014-5793(82)80521-8;
Takahashi K., Odani S., Ono T.;
"Primary structure of rat liver Z-protein. A low-Mr cytosol protein
that binds sterols, fatty acids and other small molecules.";
FEBS Lett. 140:63-66(1982).
[2]
PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
STRAIN=Wistar; TISSUE=Liver;
PubMed=6641731; DOI=10.1111/j.1432-1033.1983.tb07781.x;
Takahashi K., Odani S., Ono T.;
"Isolation and characterization of the three fractions (DE-I, DE-II
and DE-III) of rat-liver Z-protein and the complete primary structure
of DE-II.";
Eur. J. Biochem. 136:589-601(1983).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6298233;
Gordon J.I., Alpers D.H., Ockner R.K., Strauss A.W.;
"The nucleotide sequence of rat liver fatty acid binding protein
mRNA.";
J. Biol. Chem. 258:3356-3363(1983).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3007511;
Sweetser D.A., Lowe J.B., Gordon J.I.;
"The nucleotide sequence of the rat liver fatty acid-binding protein
gene. Evidence that exon 1 encodes an oligopeptide domain shared by a
family of proteins which bind hydrophobic ligands.";
J. Biol. Chem. 261:5553-5561(1986).
[5]
NUCLEOTIDE SEQUENCE.
PubMed=3840724; DOI=10.1016/0009-3084(85)90063-5;
Gordon J.I., Lowe J.B.;
"Analyzing the structures, functions and evolution of two abundant
gastrointestinal fatty acid binding proteins with recombinant DNA and
computational techniques.";
Chem. Phys. Lipids 38:137-158(1985).
[6]
NUCLEOTIDE SEQUENCE.
PubMed=1898328; DOI=10.1042/bj2780365;
Worrall A.F., Evans C., Wilton D.C.;
"Synthesis of a gene for rat liver fatty-acid-binding protein and its
expression in Escherichia coli.";
Biochem. J. 278:365-368(1991).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-102.
PubMed=3478711; DOI=10.1073/pnas.84.21.7547;
Bassuk J.A., Tsichlis P.N., Sorof S.;
"Liver fatty acid binding protein is the mitosis-associated
polypeptide target of a carcinogen in rat hepatocytes.";
Proc. Natl. Acad. Sci. U.S.A. 84:7547-7551(1987).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 34-127.
PubMed=3838749;
McGuire D.M., Chan L., Smith L.C., Towle H.C., Dempsey M.E.;
"Translational control of the circadian rhythm of liver sterol carrier
protein. Analysis of mRNA sequences with a specific cDNA probe.";
J. Biol. Chem. 260:5435-5439(1985).
[10]
PROTEIN SEQUENCE OF 1-20.
PubMed=1939124;
Myszka D.G., Swenson R.P.;
"Identification by photoaffinity labeling of fatty acid-binding
protein as a potential warfarin receptor in rat liver.";
J. Biol. Chem. 266:20725-20731(1991).
[11]
DEAMIDATION AT ASN-105, AND ISOPEPTIDE BOND AT ASN-105.
PubMed=8117116; DOI=10.1006/abbi.1994.1088;
Odani S., Okazaki Y., Kato C., Uchiumi T., Takahashi Y.;
"On the molecular origin of charge heterogeneity of rat liver fatty
acid-binding protein (Z-protein).";
Arch. Biochem. Biophys. 309:81-84(1994).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-39 AND SER-56,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[13]
FUNCTION.
PubMed=25732850; DOI=10.1016/j.bbalip.2015.02.015;
Huang H., McIntosh A.L., Landrock K.K., Landrock D., Storey S.M.,
Martin G.G., Gupta S., Atshaves B.P., Kier A.B., Schroeder F.;
"Human FABP1 T94A variant enhances cholesterol uptake.";
Biochim. Biophys. Acta 1851:946-955(2015).
[14]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
PubMed=9054409; DOI=10.1074/jbc.272.11.7140;
Thompson J., Winter N., Terwey D., Bratt J., Banaszak L.;
"The crystal structure of the liver fatty acid-binding protein. A
complex with two bound oleates.";
J. Biol. Chem. 272:7140-7150(1997).
[15]
STRUCTURE BY NMR OF APOPROTEIN AND OF COMPLEX WITH OLEATE.
PubMed=17927211; DOI=10.1021/bi701092r;
He Y., Yang X., Wang H., Estephan R., Francis F., Kodukula S.,
Storch J., Stark R.E.;
"Solution-state molecular structure of apo and oleate-liganded liver
fatty acid-binding protein.";
Biochemistry 46:12543-12556(2007).
-!- FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake
in hepatocytes (By similarity). Binds cholesterol
(PubMed:25732850). Binds free fatty acids and their coenzyme A
derivatives, bilirubin, and some other small molecules in the
cytoplasm. May be involved in intracellular lipid transport (By
similarity). {ECO:0000250|UniProtKB:P82289,
ECO:0000269|PubMed:25732850}.
-!- INTERACTION:
P22449:Hnf4a; NbExp=3; IntAct=EBI-1209448, EBI-5261592;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- DOMAIN: Forms a beta-barrel structure that accommodates
hydrophobic ligands in its interior.
-!- PTM: Deamidation and transpeptidation at the beta carboxyl of Asn-
105 forms an isoaspartyl residue found in an isoform of the DE-III
fraction. This rearrangement gives rise to an extra negative
charge carried by the acid form. {ECO:0000269|PubMed:8117116}.
-!- MISCELLANEOUS: There are three fractions of Z-protein: DE-I, DE-II
and DE-III. DE-I is virtually lipid free, DE-II binds palmitic,
stearic, oleic, linoleic and arachidonic acids and DE-III binds
mainly arachidonic acid.
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; V01235; CAA24545.1; -; mRNA.
EMBL; M13501; AAA41140.1; -; Genomic_DNA.
EMBL; M35991; AAA41135.1; -; mRNA.
EMBL; S55929; AAB19788.1; -; Other_DNA.
EMBL; BC086947; AAH86947.1; -; mRNA.
EMBL; M17899; AAA41134.1; -; mRNA.
EMBL; M10951; AAA42119.1; -; mRNA.
PIR; A92416; FZRTL.
PIR; I52354; I52354.
PIR; I52850; I52850.
PIR; I55238; I55238.
RefSeq; NP_036688.1; NM_012556.2.
UniGene; Rn.36412; -.
PDB; 1LFO; X-ray; 2.30 A; A=1-127.
PDB; 2JU3; NMR; -; A=1-127.
PDB; 2JU7; NMR; -; A=1-127.
PDB; 2JU8; NMR; -; A=1-127.
PDBsum; 1LFO; -.
PDBsum; 2JU3; -.
PDBsum; 2JU7; -.
PDBsum; 2JU8; -.
ProteinModelPortal; P02692; -.
SMR; P02692; -.
IntAct; P02692; 2.
MINT; MINT-4567871; -.
STRING; 10116.ENSRNOP00000008841; -.
BindingDB; P02692; -.
ChEMBL; CHEMBL5738; -.
GuidetoPHARMACOLOGY; 2531; -.
SwissLipids; SLP:000001517; -.
iPTMnet; P02692; -.
PhosphoSitePlus; P02692; -.
PaxDb; P02692; -.
PRIDE; P02692; -.
Ensembl; ENSRNOT00000008840; ENSRNOP00000008841; ENSRNOG00000006675.
GeneID; 24360; -.
KEGG; rno:24360; -.
UCSC; RGD:2590; rat.
CTD; 2168; -.
RGD; 2590; Fabp1.
eggNOG; KOG4015; Eukaryota.
eggNOG; ENOG4111US8; LUCA.
GeneTree; ENSGT00390000012034; -.
HOGENOM; HOG000004830; -.
HOVERGEN; HBG005633; -.
InParanoid; P02692; -.
KO; K08750; -.
OMA; FTLGEEC; -.
OrthoDB; EOG091G16BV; -.
PhylomeDB; P02692; -.
TreeFam; TF330348; -.
Reactome; R-RNO-163560; Triglyceride catabolism.
Reactome; R-RNO-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
EvolutionaryTrace; P02692; -.
PRO; PR:P02692; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000006675; -.
Genevisible; P02692; RN.
GO; GO:0045179; C:apical cortex; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005782; C:peroxisomal matrix; IDA:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0016209; F:antioxidant activity; ISO:RGD.
GO; GO:0032052; F:bile acid binding; IMP:RGD.
GO; GO:0003682; F:chromatin binding; ISO:RGD.
GO; GO:0008144; F:drug binding; IPI:RGD.
GO; GO:0005504; F:fatty acid binding; IDA:RGD.
GO; GO:0005324; F:long-chain fatty acid transporter activity; IMP:RGD.
GO; GO:0051978; F:lysophospholipid transporter activity; IC:RGD.
GO; GO:0005543; F:phospholipid binding; IMP:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:RGD.
GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
GO; GO:0050892; P:intestinal absorption; IDA:RGD.
GO; GO:0015909; P:long-chain fatty acid transport; IMP:RGD.
GO; GO:0000278; P:mitotic cell cycle; TAS:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IEP:RGD.
GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IDA:RGD.
GO; GO:0051345; P:positive regulation of hydrolase activity; IDA:RGD.
GO; GO:0006810; P:transport; IEP:RGD.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR000463; Fatty_acid-bd.
InterPro; IPR031259; ILBP.
InterPro; IPR031276; Lb-FABP.
PANTHER; PTHR11955; PTHR11955; 1.
PANTHER; PTHR11955:SF96; PTHR11955:SF96; 1.
PRINTS; PR00178; FATTYACIDBP.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00214; FABP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; Lipid-binding;
Phosphoprotein; Reference proteome; Transport.
CHAIN 1 127 Fatty acid-binding protein, liver.
/FTId=PRO_0000067337.
REGION 54 56 Fatty acid 1 binding.
BINDING 31 31 Fatty acid 1.
{ECO:0000269|PubMed:9054409}.
BINDING 39 39 Fatty acid 2.
{ECO:0000269|PubMed:9054409}.
BINDING 122 122 Fatty acid 2.
{ECO:0000269|PubMed:9054409}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:6641731,
ECO:0000269|PubMed:7084456}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 31 31 N6-succinyllysine.
{ECO:0000250|UniProtKB:P12710}.
MOD_RES 36 36 N6-succinyllysine.
{ECO:0000250|UniProtKB:P12710}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 46 46 N6-succinyllysine.
{ECO:0000250|UniProtKB:P12710}.
MOD_RES 51 51 Phosphothreonine.
{ECO:0000250|UniProtKB:P07148}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 57 57 N6-succinyllysine.
{ECO:0000250|UniProtKB:P12710}.
MOD_RES 78 78 N6-succinyllysine.
{ECO:0000250|UniProtKB:P12710}.
MOD_RES 84 84 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P12710}.
MOD_RES 84 84 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P12710}.
MOD_RES 90 90 N6-succinyllysine.
{ECO:0000250|UniProtKB:P12710}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000250|UniProtKB:P12710}.
MOD_RES 105 105 Deamidated asparagine; alternate.
{ECO:0000269|PubMed:8117116}.
MOD_RES 121 121 N6-succinyllysine.
{ECO:0000250|UniProtKB:P12710}.
CROSSLNK 105 106 Isoaspartyl glycine isopeptide (Asn-Gly);
alternate.
STRAND 5 14 {ECO:0000244|PDB:1LFO}.
HELIX 15 21 {ECO:0000244|PDB:1LFO}.
HELIX 26 32 {ECO:0000244|PDB:1LFO}.
STRAND 38 44 {ECO:0000244|PDB:1LFO}.
STRAND 47 54 {ECO:0000244|PDB:1LFO}.
STRAND 57 64 {ECO:0000244|PDB:1LFO}.
STRAND 67 72 {ECO:0000244|PDB:1LFO}.
STRAND 74 76 {ECO:0000244|PDB:2JU7}.
STRAND 78 82 {ECO:0000244|PDB:1LFO}.
STRAND 84 86 {ECO:0000244|PDB:1LFO}.
TURN 87 89 {ECO:0000244|PDB:1LFO}.
STRAND 90 95 {ECO:0000244|PDB:1LFO}.
STRAND 98 105 {ECO:0000244|PDB:1LFO}.
STRAND 108 115 {ECO:0000244|PDB:1LFO}.
STRAND 118 127 {ECO:0000244|PDB:1LFO}.
SEQUENCE 127 AA; 14273 MW; 08C7F59A99FE0D3A CRC64;
MNFSGKYQVQ SQENFEPFMK AMGLPEDLIQ KGKDIKGVSE IVHEGKKVKL TITYGSKVIH
NEFTLGEECE LETMTGEKVK AVVKMEGDNK MVTTFKGIKS VTEFNGDTIT NTMTLGDIVY
KRVSKRI


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