FABPL_RAT
ID FABPL_RAT Reviewed; 127 AA.
AC P02692;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Fatty acid-binding protein, liver;
DE AltName: Full=Fatty acid-binding protein 1;
DE AltName: Full=Liver-type fatty acid-binding protein;
DE Short=L-FABP;
DE AltName: Full=Squalene- and sterol-carrier protein;
DE Short=SCP;
DE AltName: Full=Z-protein;
DE AltName: Full=p14;
GN Name=Fabp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7084456; DOI=10.1016/0014-5793(82)80521-8;
RA Takahashi K., Odani S., Ono T.;
RT "Primary structure of rat liver Z-protein. A low-Mr cytosol protein that
RT binds sterols, fatty acids and other small molecules.";
RL FEBS Lett. 140:63-66(1982).
RN [2]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=6641731; DOI=10.1111/j.1432-1033.1983.tb07781.x;
RA Takahashi K., Odani S., Ono T.;
RT "Isolation and characterization of the three fractions (DE-I, DE-II and DE-
RT III) of rat-liver Z-protein and the complete primary structure of DE-II.";
RL Eur. J. Biochem. 136:589-601(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6298233; DOI=10.1016/s0021-9258(18)32868-0;
RA Gordon J.I., Alpers D.H., Ockner R.K., Strauss A.W.;
RT "The nucleotide sequence of rat liver fatty acid binding protein mRNA.";
RL J. Biol. Chem. 258:3356-3363(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3007511; DOI=10.1016/s0021-9258(19)57250-7;
RA Sweetser D.A., Lowe J.B., Gordon J.I.;
RT "The nucleotide sequence of the rat liver fatty acid-binding protein gene.
RT Evidence that exon 1 encodes an oligopeptide domain shared by a family of
RT proteins which bind hydrophobic ligands.";
RL J. Biol. Chem. 261:5553-5561(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3840724; DOI=10.1016/0009-3084(85)90063-5;
RA Gordon J.I., Lowe J.B.;
RT "Analyzing the structures, functions and evolution of two abundant
RT gastrointestinal fatty acid binding proteins with recombinant DNA and
RT computational techniques.";
RL Chem. Phys. Lipids 38:137-158(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1898328; DOI=10.1042/bj2780365;
RA Worrall A.F., Evans C., Wilton D.C.;
RT "Synthesis of a gene for rat liver fatty-acid-binding protein and its
RT expression in Escherichia coli.";
RL Biochem. J. 278:365-368(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-102.
RX PubMed=3478711; DOI=10.1073/pnas.84.21.7547;
RA Bassuk J.A., Tsichlis P.N., Sorof S.;
RT "Liver fatty acid binding protein is the mitosis-associated polypeptide
RT target of a carcinogen in rat hepatocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7547-7551(1987).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 34-127.
RX PubMed=3838749; DOI=10.1016/s0021-9258(18)89041-x;
RA McGuire D.M., Chan L., Smith L.C., Towle H.C., Dempsey M.E.;
RT "Translational control of the circadian rhythm of liver sterol carrier
RT protein. Analysis of mRNA sequences with a specific cDNA probe.";
RL J. Biol. Chem. 260:5435-5439(1985).
RN [10]
RP PROTEIN SEQUENCE OF 1-20.
RX PubMed=1939124; DOI=10.1016/s0021-9258(18)54769-4;
RA Myszka D.G., Swenson R.P.;
RT "Identification by photoaffinity labeling of fatty acid-binding protein as
RT a potential warfarin receptor in rat liver.";
RL J. Biol. Chem. 266:20725-20731(1991).
RN [11]
RP DEAMIDATION AT ASN-105, AND ISOPEPTIDE BOND AT ASN-105.
RX PubMed=8117116; DOI=10.1006/abbi.1994.1088;
RA Odani S., Okazaki Y., Kato C., Uchiumi T., Takahashi Y.;
RT "On the molecular origin of charge heterogeneity of rat liver fatty acid-
RT binding protein (Z-protein).";
RL Arch. Biochem. Biophys. 309:81-84(1994).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-39 AND SER-56, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [13]
RP FUNCTION.
RX PubMed=25732850; DOI=10.1016/j.bbalip.2015.02.015;
RA Huang H., McIntosh A.L., Landrock K.K., Landrock D., Storey S.M.,
RA Martin G.G., Gupta S., Atshaves B.P., Kier A.B., Schroeder F.;
RT "Human FABP1 T94A variant enhances cholesterol uptake.";
RL Biochim. Biophys. Acta 1851:946-955(2015).
RN [14] {ECO:0007744|PDB:1LFO}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH OLEATE.
RX PubMed=9054409; DOI=10.1074/jbc.272.11.7140;
RA Thompson J., Winter N., Terwey D., Bratt J., Banaszak L.;
RT "The crystal structure of the liver fatty acid-binding protein. A complex
RT with two bound oleates.";
RL J. Biol. Chem. 272:7140-7150(1997).
RN [15]
RP STRUCTURE BY NMR OF APOPROTEIN AND OF COMPLEX WITH OLEATE.
RX PubMed=17927211; DOI=10.1021/bi701092r;
RA He Y., Yang X., Wang H., Estephan R., Francis F., Kodukula S., Storch J.,
RA Stark R.E.;
RT "Solution-state molecular structure of apo and oleate-liganded liver fatty
RT acid-binding protein.";
RL Biochemistry 46:12543-12556(2007).
CC -!- FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake in
CC hepatocytes (By similarity). Binds cholesterol (PubMed:25732850). Binds
CC free fatty acids and their coenzyme A derivatives, bilirubin, and some
CC other small molecules in the cytoplasm. May be involved in
CC intracellular lipid transport (By similarity).
CC {ECO:0000250|UniProtKB:P82289, ECO:0000269|PubMed:25732850}.
CC -!- INTERACTION:
CC P02692; P22449: Hnf4a; NbExp=3; IntAct=EBI-1209448, EBI-5261592;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior.
CC -!- PTM: Deamidation and transpeptidation at the beta carboxyl of Asn-105
CC forms an isoaspartyl residue found in an isoform of the DE-III
CC fraction. This rearrangement gives rise to an extra negative charge
CC carried by the acid form. {ECO:0000269|PubMed:8117116}.
CC -!- MISCELLANEOUS: There are three fractions of Z-protein: DE-I, DE-II and
CC DE-III. DE-I is virtually lipid free, DE-II binds palmitic, stearic,
CC oleic, linoleic and arachidonic acids and DE-III binds mainly
CC arachidonic acid.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; V01235; CAA24545.1; -; mRNA.
DR EMBL; M13501; AAA41140.1; -; Genomic_DNA.
DR EMBL; M35991; AAA41135.1; -; mRNA.
DR EMBL; S55929; AAB19788.1; -; Other_DNA.
DR EMBL; BC086947; AAH86947.1; -; mRNA.
DR EMBL; M17899; AAA41134.1; -; mRNA.
DR EMBL; M10951; AAA42119.1; -; mRNA.
DR PIR; A92416; FZRTL.
DR PIR; I52354; I52354.
DR PIR; I52850; I52850.
DR PIR; I55238; I55238.
DR RefSeq; NP_036688.1; NM_012556.2.
DR PDB; 1LFO; X-ray; 2.30 A; A=1-127.
DR PDB; 2JU3; NMR; -; A=1-127.
DR PDB; 2JU7; NMR; -; A=1-127.
DR PDB; 2JU8; NMR; -; A=1-127.
DR PDBsum; 1LFO; -.
DR PDBsum; 2JU3; -.
DR PDBsum; 2JU7; -.
DR PDBsum; 2JU8; -.
DR AlphaFoldDB; P02692; -.
DR BMRB; P02692; -.
DR PCDDB; P02692; -.
DR SMR; P02692; -.
DR IntAct; P02692; 4.
DR MINT; P02692; -.
DR STRING; 10116.ENSRNOP00000008841; -.
DR BindingDB; P02692; -.
DR ChEMBL; CHEMBL5738; -.
DR DrugCentral; P02692; -.
DR GuidetoPHARMACOLOGY; 2531; -.
DR SwissLipids; SLP:000001517; -.
DR CarbonylDB; P02692; -.
DR iPTMnet; P02692; -.
DR PhosphoSitePlus; P02692; -.
DR PaxDb; P02692; -.
DR PRIDE; P02692; -.
DR DNASU; 24360; -.
DR Ensembl; ENSRNOT00000008840; ENSRNOP00000008841; ENSRNOG00000006675.
DR GeneID; 24360; -.
DR KEGG; rno:24360; -.
DR UCSC; RGD:2590; rat.
DR CTD; 2168; -.
DR RGD; 2590; Fabp1.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000155135; -.
DR HOGENOM; CLU_113772_4_2_1; -.
DR InParanoid; P02692; -.
DR OMA; DTITNTM; -.
DR OrthoDB; 1440574at2759; -.
DR PhylomeDB; P02692; -.
DR TreeFam; TF330348; -.
DR Reactome; R-RNO-163560; Triglyceride catabolism.
DR Reactome; R-RNO-189483; Heme degradation.
DR Reactome; R-RNO-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR EvolutionaryTrace; P02692; -.
DR PRO; PR:P02692; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000006675; Expressed in jejunum and 18 other tissues.
DR Genevisible; P02692; RN.
DR GO; GO:0045179; C:apical cortex; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0016209; F:antioxidant activity; ISO:RGD.
DR GO; GO:0032052; F:bile acid binding; IMP:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0005504; F:fatty acid binding; IDA:RGD.
DR GO; GO:1901363; F:heterocyclic compound binding; IDA:RGD.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IMP:RGD.
DR GO; GO:0051978; F:lysophospholipid:sodium symporter activity; IC:RGD.
DR GO; GO:0070538; F:oleic acid binding; IPI:RGD.
DR GO; GO:0005543; F:phospholipid binding; IMP:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0050892; P:intestinal absorption; IDA:RGD.
DR GO; GO:0015909; P:long-chain fatty acid transport; IMP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IDA:RGD.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; IDA:RGD.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR031276; Lb-FABP.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF96; PTHR11955:SF96; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Lipid-binding; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..127
FT /note="Fatty acid-binding protein, liver"
FT /id="PRO_0000067337"
FT BINDING 31
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:9054409,
FT ECO:0007744|PDB:1LFO"
FT BINDING 39
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:9054409,
FT ECO:0007744|PDB:1LFO"
FT BINDING 54..56
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:9054409,
FT ECO:0007744|PDB:1LFO"
FT BINDING 122
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:9054409,
FT ECO:0007744|PDB:1LFO"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:6641731,
FT ECO:0000269|PubMed:7084456"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 31
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 36
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 46
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07148"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 78
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 84
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 84
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 90
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 105
FT /note="Deamidated asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:8117116"
FT MOD_RES 121
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT CROSSLNK 105..106
FT /note="Isoaspartyl glycine isopeptide (Asn-Gly); alternate"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:1LFO"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:1LFO"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:1LFO"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:1LFO"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:1LFO"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:1LFO"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1LFO"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2JU7"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1LFO"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1LFO"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1LFO"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1LFO"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:1LFO"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1LFO"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:1LFO"
SQ SEQUENCE 127 AA; 14273 MW; 08C7F59A99FE0D3A CRC64;
MNFSGKYQVQ SQENFEPFMK AMGLPEDLIQ KGKDIKGVSE IVHEGKKVKL TITYGSKVIH
NEFTLGEECE LETMTGEKVK AVVKMEGDNK MVTTFKGIKS VTEFNGDTIT NTMTLGDIVY
KRVSKRI
