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

 FABPL_HUMAN             Reviewed;         127 AA.
P07148;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
05-DEC-2018, entry version 183.
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;
Name=FABP1; Synonyms=FABPL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ACETYLATION AT MET-1.
PubMed=3838309;
Chan L., Wei C.-F., Li W.-H., Yang C.-Y., Ratner P., Pownall H.,
Gotto A.M. Jr., Smith L.C.;
"Human liver fatty acid binding protein cDNA and amino acid sequence.
Functional and evolutionary implications.";
J. Biol. Chem. 260:2629-2632(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-94.
PubMed=3838313;
Lowe J.B., Boguski M.S., Sweetser D.A., Elshourbagy N.A., Taylor J.M.,
Gordon J.I.;
"Human liver fatty acid binding protein. Isolation of a full length
cDNA and comparative sequence analyses of orthologous and paralogous
proteins.";
J. Biol. Chem. 260:3413-3417(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, Kidney, and Stomach;
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).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; THR-51 AND SER-56,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[6]
FUNCTION, AND CHARACTERIZATION OF VARIANT ALA-94.
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).
[7]
STRUCTURE BY NMR.
PubMed=17536800; DOI=10.1021/ja071442e;
Xu Y., Long D., Yang D.;
"Rapid data collection for protein structure determination by NMR
spectroscopy.";
J. Am. Chem. Soc. 129:7722-7723(2007).
[8]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Structural genomics consortium (SGC);
"Crystal structure of human FABP1.";
Submitted (DEC-2005) to the PDB data bank.
-!- FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake
in hepatocytes (PubMed:25732850). 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:
P21333-2:FLNA; NbExp=3; IntAct=EBI-2115989, EBI-9641086;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- DOMAIN: Forms a beta-barrel structure that accommodates
hydrophobic ligands in its interior.
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M10617; AAA52419.1; -; mRNA.
EMBL; M10050; AAA52418.1; -; mRNA.
EMBL; BC032801; AAH32801.1; -; mRNA.
CCDS; CCDS2001.1; -.
PIR; A22289; FZHUL.
RefSeq; NP_001434.1; NM_001443.2.
UniGene; Hs.380135; -.
PDB; 2F73; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-127.
PDB; 2L67; NMR; -; A=2-127.
PDB; 2L68; NMR; -; A=2-127.
PDB; 2LKK; NMR; -; A=2-127.
PDB; 2PY1; NMR; -; A=1-127.
PDB; 3B2H; X-ray; 1.55 A; A=2-127.
PDB; 3B2I; X-ray; 1.86 A; A=2-127.
PDB; 3B2J; X-ray; 2.00 A; A=2-127.
PDB; 3B2K; X-ray; 1.73 A; A=2-127.
PDB; 3B2L; X-ray; 2.25 A; A=2-127.
PDB; 3STK; X-ray; 1.55 A; A=2-127.
PDB; 3STM; X-ray; 2.22 A; X=2-127.
PDB; 3STN; X-ray; 2.60 A; A=2-127.
PDB; 3VG2; X-ray; 2.40 A; A=2-127.
PDB; 3VG3; X-ray; 2.22 A; A=2-127.
PDB; 3VG4; X-ray; 2.50 A; A=2-127.
PDB; 3VG5; X-ray; 2.00 A; A=2-127.
PDB; 3VG6; X-ray; 2.22 A; A=2-127.
PDB; 3VG7; X-ray; 1.44 A; A=2-127.
PDBsum; 2F73; -.
PDBsum; 2L67; -.
PDBsum; 2L68; -.
PDBsum; 2LKK; -.
PDBsum; 2PY1; -.
PDBsum; 3B2H; -.
PDBsum; 3B2I; -.
PDBsum; 3B2J; -.
PDBsum; 3B2K; -.
PDBsum; 3B2L; -.
PDBsum; 3STK; -.
PDBsum; 3STM; -.
PDBsum; 3STN; -.
PDBsum; 3VG2; -.
PDBsum; 3VG3; -.
PDBsum; 3VG4; -.
PDBsum; 3VG5; -.
PDBsum; 3VG6; -.
PDBsum; 3VG7; -.
ProteinModelPortal; P07148; -.
SMR; P07148; -.
BioGrid; 108466; 8.
IntAct; P07148; 2.
STRING; 9606.ENSP00000295834; -.
BindingDB; P07148; -.
ChEMBL; CHEMBL5421; -.
DrugBank; DB02074; Butenoic Acid.
DrugBank; DB02659; Cholic Acid.
DrugBank; DB04224; Oleic Acid.
DrugBank; DB02216; S-Methylcysteine.
SwissLipids; SLP:000001516; -.
iPTMnet; P07148; -.
PhosphoSitePlus; P07148; -.
BioMuta; FABP1; -.
DMDM; 119808; -.
SWISS-2DPAGE; P07148; -.
PaxDb; P07148; -.
PeptideAtlas; P07148; -.
PRIDE; P07148; -.
ProteomicsDB; 51959; -.
DNASU; 2168; -.
Ensembl; ENST00000295834; ENSP00000295834; ENSG00000163586.
GeneID; 2168; -.
KEGG; hsa:2168; -.
CTD; 2168; -.
DisGeNET; 2168; -.
EuPathDB; HostDB:ENSG00000163586.9; -.
GeneCards; FABP1; -.
HGNC; HGNC:3555; FABP1.
HPA; CAB002305; -.
HPA; HPA028275; -.
MIM; 134650; gene.
neXtProt; NX_P07148; -.
OpenTargets; ENSG00000163586; -.
PharmGKB; PA27956; -.
eggNOG; KOG4015; Eukaryota.
eggNOG; ENOG4111US8; LUCA.
GeneTree; ENSGT00940000155135; -.
HOVERGEN; HBG005633; -.
InParanoid; P07148; -.
KO; K08750; -.
OMA; FTLGEEC; -.
OrthoDB; EOG091G16BV; -.
PhylomeDB; P07148; -.
TreeFam; TF330348; -.
Reactome; R-HSA-163560; Triglyceride catabolism.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
ChiTaRS; FABP1; human.
EvolutionaryTrace; P07148; -.
GeneWiki; FABP1; -.
GenomeRNAi; 2168; -.
PRO; PR:P07148; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000163586; Expressed in 105 organ(s), highest expression level in colonic mucosa.
CleanEx; HS_FABP1; -.
ExpressionAtlas; P07148; baseline and differential.
Genevisible; P07148; HS.
GO; GO:0045179; C:apical cortex; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
GO; GO:0032052; F:bile acid binding; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0008144; F:drug binding; IEA:Ensembl.
GO; GO:0005504; F:fatty acid binding; IEA:Ensembl.
GO; GO:0005324; F:long-chain fatty acid transporter activity; IEA:Ensembl.
GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0050892; P:intestinal absorption; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IEA:Ensembl.
GO; GO:0051345; P:positive regulation of hydrolase activity; IEA:Ensembl.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0019433; P:triglyceride catabolic process; TAS:Reactome.
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;
Lipid-binding; Phosphoprotein; Polymorphism; Reference proteome;
Transport.
CHAIN 1 127 Fatty acid-binding protein, liver.
/FTId=PRO_0000067334.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:3838309}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
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:0000250|UniProtKB:P02692}.
MOD_RES 46 46 N6-succinyllysine.
{ECO:0000250|UniProtKB:P12710}.
MOD_RES 51 51 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 57 57 N6-succinyllysine.
{ECO:0000250|UniProtKB:P12710}.
MOD_RES 78 78 N6-succinyllysine.
{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 121 121 N6-succinyllysine.
{ECO:0000250|UniProtKB:P12710}.
VARIANT 54 54 A -> T (in dbSNP:rs1801273).
/FTId=VAR_014662.
VARIANT 94 94 T -> A (polymorphism; increases the
binding for cholesterol; increases high
density lipoprotein (HDL)- and low
density lipoprotein (LDL)-mediated
cholesterol uptake; dbSNP:rs2241883).
{ECO:0000269|PubMed:3838313}.
/FTId=VAR_022093.
STRAND 5 14 {ECO:0000244|PDB:3VG7}.
HELIX 15 21 {ECO:0000244|PDB:3VG7}.
HELIX 26 32 {ECO:0000244|PDB:3VG7}.
STRAND 38 44 {ECO:0000244|PDB:3VG7}.
STRAND 47 54 {ECO:0000244|PDB:3VG7}.
STRAND 57 64 {ECO:0000244|PDB:3VG7}.
STRAND 67 72 {ECO:0000244|PDB:3VG7}.
STRAND 74 76 {ECO:0000244|PDB:3B2L}.
STRAND 78 82 {ECO:0000244|PDB:3VG7}.
STRAND 84 87 {ECO:0000244|PDB:3VG7}.
STRAND 90 95 {ECO:0000244|PDB:3VG7}.
STRAND 98 105 {ECO:0000244|PDB:3VG7}.
STRAND 108 115 {ECO:0000244|PDB:3VG7}.
STRAND 118 126 {ECO:0000244|PDB:3VG7}.
SEQUENCE 127 AA; 14208 MW; 065DCEFB08DAB6B6 CRC64;
MSFSGKYQLQ SQENFEAFMK AIGLPEELIQ KGKDIKGVSE IVQNGKHFKF TITAGSKVIQ
NEFTVGEECE LETMTGEKVK TVVQLEGDNK LVTTFKNIKS VTELNGDIIT NTMTLGDIVF
KRISKRI


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