FABPL_HUMAN
ID FABPL_HUMAN Reviewed; 127 AA.
AC P07148;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 202.
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;
GN Name=FABP1; Synonyms=FABPL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ACETYLATION AT MET-1.
RX PubMed=3838309; DOI=10.1016/s0021-9258(18)89406-6;
RA Chan L., Wei C.-F., Li W.-H., Yang C.-Y., Ratner P., Pownall H.,
RA Gotto A.M. Jr., Smith L.C.;
RT "Human liver fatty acid binding protein cDNA and amino acid sequence.
RT Functional and evolutionary implications.";
RL J. Biol. Chem. 260:2629-2632(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-94.
RX PubMed=3838313; DOI=10.1016/s0021-9258(19)83637-2;
RA Lowe J.B., Boguski M.S., Sweetser D.A., Elshourbagy N.A., Taylor J.M.,
RA Gordon J.I.;
RT "Human liver fatty acid binding protein. Isolation of a full length cDNA
RT and comparative sequence analyses of orthologous and paralogous proteins.";
RL J. Biol. Chem. 260:3413-3417(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, Kidney, and Stomach;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; THR-51 AND SER-56, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
RP FUNCTION, AND CHARACTERIZATION OF VARIANT ALA-94.
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 [7]
RP STRUCTURE BY NMR.
RX PubMed=17536800; DOI=10.1021/ja071442e;
RA Xu Y., Long D., Yang D.;
RT "Rapid data collection for protein structure determination by NMR
RT spectroscopy.";
RL J. Am. Chem. Soc. 129:7722-7723(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RG Structural genomics consortium (SGC);
RT "Crystal structure of human FABP1.";
RL Submitted (DEC-2005) to the PDB data bank.
CC -!- FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake in
CC hepatocytes (PubMed:25732850). Binds cholesterol (PubMed:25732850).
CC Binds free fatty acids and their coenzyme A derivatives, bilirubin, and
CC some 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 P07148; P21333-2: FLNA; NbExp=3; IntAct=EBI-2115989, EBI-9641086;
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 EMBL; M10617; AAA52419.1; -; mRNA.
DR EMBL; M10050; AAA52418.1; -; mRNA.
DR EMBL; BC032801; AAH32801.1; -; mRNA.
DR CCDS; CCDS2001.1; -.
DR PIR; A22289; FZHUL.
DR RefSeq; NP_001434.1; NM_001443.2.
DR PDB; 2F73; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-127.
DR PDB; 2L67; NMR; -; A=2-127.
DR PDB; 2L68; NMR; -; A=2-127.
DR PDB; 2LKK; NMR; -; A=2-127.
DR PDB; 2PY1; NMR; -; A=1-127.
DR PDB; 3B2H; X-ray; 1.55 A; A=2-127.
DR PDB; 3B2I; X-ray; 1.86 A; A=2-127.
DR PDB; 3B2J; X-ray; 2.00 A; A=2-127.
DR PDB; 3B2K; X-ray; 1.73 A; A=2-127.
DR PDB; 3B2L; X-ray; 2.25 A; A=2-127.
DR PDB; 3STK; X-ray; 1.55 A; A=2-127.
DR PDB; 3STM; X-ray; 2.22 A; X=2-127.
DR PDB; 3STN; X-ray; 2.60 A; A=2-127.
DR PDB; 3VG2; X-ray; 2.40 A; A=2-127.
DR PDB; 3VG3; X-ray; 2.22 A; A=2-127.
DR PDB; 3VG4; X-ray; 2.50 A; A=2-127.
DR PDB; 3VG5; X-ray; 2.00 A; A=2-127.
DR PDB; 3VG6; X-ray; 2.22 A; A=2-127.
DR PDB; 3VG7; X-ray; 1.44 A; A=2-127.
DR PDB; 6DO6; NMR; -; A=1-127.
DR PDB; 6DO7; NMR; -; A=1-127.
DR PDB; 6DRG; NMR; -; A=1-127.
DR PDB; 6MP4; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-127.
DR PDBsum; 2F73; -.
DR PDBsum; 2L67; -.
DR PDBsum; 2L68; -.
DR PDBsum; 2LKK; -.
DR PDBsum; 2PY1; -.
DR PDBsum; 3B2H; -.
DR PDBsum; 3B2I; -.
DR PDBsum; 3B2J; -.
DR PDBsum; 3B2K; -.
DR PDBsum; 3B2L; -.
DR PDBsum; 3STK; -.
DR PDBsum; 3STM; -.
DR PDBsum; 3STN; -.
DR PDBsum; 3VG2; -.
DR PDBsum; 3VG3; -.
DR PDBsum; 3VG4; -.
DR PDBsum; 3VG5; -.
DR PDBsum; 3VG6; -.
DR PDBsum; 3VG7; -.
DR PDBsum; 6DO6; -.
DR PDBsum; 6DO7; -.
DR PDBsum; 6DRG; -.
DR PDBsum; 6MP4; -.
DR AlphaFoldDB; P07148; -.
DR BMRB; P07148; -.
DR PCDDB; P07148; -.
DR SMR; P07148; -.
DR BioGRID; 108466; 8.
DR IntAct; P07148; 6.
DR STRING; 9606.ENSP00000295834; -.
DR BindingDB; P07148; -.
DR ChEMBL; CHEMBL5421; -.
DR DrugBank; DB02074; Butenoic Acid.
DR DrugBank; DB02659; Cholic Acid.
DR DrugBank; DB04224; Oleic Acid.
DR DrugBank; DB02216; S-Methylcysteine.
DR DrugCentral; P07148; -.
DR SwissLipids; SLP:000001516; -.
DR iPTMnet; P07148; -.
DR PhosphoSitePlus; P07148; -.
DR BioMuta; FABP1; -.
DR DMDM; 119808; -.
DR SWISS-2DPAGE; P07148; -.
DR jPOST; P07148; -.
DR MassIVE; P07148; -.
DR PaxDb; P07148; -.
DR PeptideAtlas; P07148; -.
DR PRIDE; P07148; -.
DR ProteomicsDB; 51959; -.
DR Antibodypedia; 3707; 640 antibodies from 40 providers.
DR DNASU; 2168; -.
DR Ensembl; ENST00000295834.8; ENSP00000295834.3; ENSG00000163586.10.
DR GeneID; 2168; -.
DR KEGG; hsa:2168; -.
DR MANE-Select; ENST00000295834.8; ENSP00000295834.3; NM_001443.3; NP_001434.1.
DR CTD; 2168; -.
DR DisGeNET; 2168; -.
DR GeneCards; FABP1; -.
DR HGNC; HGNC:3555; FABP1.
DR HPA; ENSG00000163586; Group enriched (intestine, liver).
DR MIM; 134650; gene.
DR neXtProt; NX_P07148; -.
DR OpenTargets; ENSG00000163586; -.
DR PharmGKB; PA27956; -.
DR VEuPathDB; HostDB:ENSG00000163586; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000155135; -.
DR HOGENOM; CLU_113772_4_2_1; -.
DR InParanoid; P07148; -.
DR OMA; DTITNTM; -.
DR OrthoDB; 1440574at2759; -.
DR PhylomeDB; P07148; -.
DR TreeFam; TF330348; -.
DR PathwayCommons; P07148; -.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR Reactome; R-HSA-189483; Heme degradation.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR SignaLink; P07148; -.
DR SIGNOR; P07148; -.
DR BioGRID-ORCS; 2168; 7 hits in 1068 CRISPR screens.
DR ChiTaRS; FABP1; human.
DR EvolutionaryTrace; P07148; -.
DR GeneWiki; FABP1; -.
DR GenomeRNAi; 2168; -.
DR Pharos; P07148; Tchem.
DR PRO; PR:P07148; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P07148; protein.
DR Bgee; ENSG00000163586; Expressed in mucosa of transverse colon and 103 other tissues.
DR ExpressionAtlas; P07148; baseline and differential.
DR Genevisible; P07148; HS.
DR GO; GO:0045179; C:apical cortex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
DR GO; GO:0032052; F:bile acid binding; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:1901363; F:heterocyclic compound binding; IEA:Ensembl.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IEA:Ensembl.
DR GO; GO:0070538; F:oleic acid binding; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0050892; P:intestinal absorption; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IEA:Ensembl.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; IEA:Ensembl.
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; Lipid-binding; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..127
FT /note="Fatty acid-binding protein, liver"
FT /id="PRO_0000067334"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:3838309"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
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:0000250|UniProtKB:P02692"
FT MOD_RES 46
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
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 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 121
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT VARIANT 54
FT /note="A -> T (in dbSNP:rs1801273)"
FT /id="VAR_014662"
FT VARIANT 94
FT /note="T -> A (increases the binding for cholesterol;
FT increases high density lipoprotein (HDL)- and low density
FT lipoprotein (LDL)-mediated cholesterol uptake;
FT dbSNP:rs2241883)"
FT /evidence="ECO:0000269|PubMed:3838313"
FT /id="VAR_022093"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:3VG7"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:3VG7"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:3VG7"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:3VG7"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:3VG7"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:3VG7"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3VG7"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:3B2L"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3VG7"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:3VG7"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:3VG7"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:3VG7"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:3VG7"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:3VG7"
SQ SEQUENCE 127 AA; 14208 MW; 065DCEFB08DAB6B6 CRC64;
MSFSGKYQLQ SQENFEAFMK AIGLPEELIQ KGKDIKGVSE IVQNGKHFKF TITAGSKVIQ
NEFTVGEECE LETMTGEKVK TVVQLEGDNK LVTTFKNIKS VTELNGDIIT NTMTLGDIVF
KRISKRI
