FABP4_HUMAN
ID FABP4_HUMAN Reviewed; 132 AA.
AC P15090; Q6IBA1;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Fatty acid-binding protein, adipocyte;
DE AltName: Full=Adipocyte lipid-binding protein;
DE Short=ALBP;
DE AltName: Full=Adipocyte-type fatty acid-binding protein;
DE Short=A-FABP;
DE Short=AFABP;
DE AltName: Full=Fatty acid-binding protein 4;
GN Name=FABP4;
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].
RX PubMed=2481498; DOI=10.1021/bi00448a003;
RA Baxa C.A., Sha R.S., Buelt M.K., Smith A.J., Matarese V., Chinander L.L.,
RA Boundy K.L., Bernlohr D.A.;
RT "Human adipocyte lipid-binding protein: purification of the protein and
RT cloning of its complementary DNA.";
RL Biochemistry 28:8683-8690(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
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 [9]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-23.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR,
RP AND SUBUNIT.
RX PubMed=15357969; DOI=10.1016/j.bmcl.2004.06.057;
RA Lehmann F., Haile S., Axen E., Medina C., Uppenberg J., Svensson S.,
RA Lundbaeck T., Rondahl L., Barf T.;
RT "Discovery of inhibitors of human adipocyte fatty acid-binding protein, a
RT potential type 2 diabetes target.";
RL Bioorg. Med. Chem. Lett. 14:4445-4448(2004).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH FATTY ACID, SUBUNIT,
RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17077479; DOI=10.1107/s1744309106038656;
RA Marr E., Tardie M., Carty M., Brown Phillips T., Wang I.-K., Soeller W.,
RA Qiu X., Karam G.;
RT "Expression, purification, crystallization and structure of human adipocyte
RT lipid-binding protein (aP2).";
RL Acta Crystallogr. F 62:1058-1060(2006).
CC -!- FUNCTION: Lipid transport protein in adipocytes. Binds both long chain
CC fatty acids and retinoic acid. Delivers long-chain fatty acids and
CC retinoic acid to their cognate receptors in the nucleus.
CC {ECO:0000250|UniProtKB:P04117}.
CC -!- SUBUNIT: Monomer (PubMed:15357969, PubMed:17077479). Homodimer.
CC Interacts with PPARG (By similarity). {ECO:0000250|UniProtKB:P04117,
CC ECO:0000269|PubMed:15357969, ECO:0000269|PubMed:17077479}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04117}. Nucleus
CC {ECO:0000250|UniProtKB:P04117}. Note=Depending on the nature of the
CC ligand, a conformation change exposes a nuclear localization motif and
CC the protein is transported into the nucleus. Subject to constitutive
CC nuclear export. {ECO:0000250|UniProtKB:P04117}.
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; J02874; AAA51689.1; -; mRNA.
DR EMBL; BT006809; AAP35455.1; -; mRNA.
DR EMBL; CR456903; CAG33184.1; -; mRNA.
DR EMBL; CH471068; EAW87092.1; -; Genomic_DNA.
DR EMBL; BC003672; AAH03672.1; -; mRNA.
DR CCDS; CCDS6230.1; -.
DR PIR; A33363; FZHUF.
DR RefSeq; NP_001433.1; NM_001442.2.
DR PDB; 1TOU; X-ray; 2.00 A; A=2-132.
DR PDB; 1TOW; X-ray; 2.00 A; A=2-132.
DR PDB; 2HNX; X-ray; 1.50 A; A=1-132.
DR PDB; 2NNQ; X-ray; 1.80 A; A=2-132.
DR PDB; 3FR2; X-ray; 2.20 A; A=2-132.
DR PDB; 3FR4; X-ray; 2.16 A; A=1-132.
DR PDB; 3FR5; X-ray; 2.20 A; A=2-132.
DR PDB; 3P6C; X-ray; 1.25 A; A=1-132.
DR PDB; 3P6D; X-ray; 1.06 A; A=1-132.
DR PDB; 3P6E; X-ray; 1.08 A; A=1-132.
DR PDB; 3P6F; X-ray; 1.20 A; A=1-132.
DR PDB; 3P6G; X-ray; 1.20 A; A=1-132.
DR PDB; 3P6H; X-ray; 1.15 A; A=1-132.
DR PDB; 3Q6L; X-ray; 1.40 A; A=1-132.
DR PDB; 3RZY; X-ray; 1.08 A; A=1-132.
DR PDB; 4NNS; X-ray; 1.53 A; A=1-132.
DR PDB; 4NNT; X-ray; 1.53 A; A=1-132.
DR PDB; 5D45; X-ray; 1.65 A; A=1-132.
DR PDB; 5D47; X-ray; 1.70 A; A=1-132.
DR PDB; 5D48; X-ray; 1.81 A; A=1-132.
DR PDB; 5D4A; X-ray; 1.70 A; A=1-132.
DR PDB; 5EDB; X-ray; 1.18 A; A=1-132.
DR PDB; 5EDC; X-ray; 1.29 A; A=1-132.
DR PDB; 5HZ6; X-ray; 1.14 A; A=4-132.
DR PDB; 5HZ8; X-ray; 1.12 A; A=1-132.
DR PDB; 5Y0F; X-ray; 1.54 A; A=1-132.
DR PDB; 5Y0G; X-ray; 1.54 A; A=1-132.
DR PDB; 5Y0X; X-ray; 1.60 A; A=1-132.
DR PDB; 5Y12; X-ray; 1.75 A; A=1-132.
DR PDB; 5Y13; X-ray; 1.75 A; A=1-132.
DR PDB; 6AYL; X-ray; 1.86 A; A=1-132.
DR PDB; 6LJS; X-ray; 1.75 A; A=1-132.
DR PDB; 6LJT; X-ray; 1.45 A; A=1-132.
DR PDB; 6LJU; X-ray; 1.50 A; A=1-132.
DR PDB; 6LJV; X-ray; 1.40 A; A=1-132.
DR PDB; 6LJW; X-ray; 1.40 A; A=1-132.
DR PDB; 6LJX; X-ray; 1.75 A; A=1-132.
DR PDBsum; 1TOU; -.
DR PDBsum; 1TOW; -.
DR PDBsum; 2HNX; -.
DR PDBsum; 2NNQ; -.
DR PDBsum; 3FR2; -.
DR PDBsum; 3FR4; -.
DR PDBsum; 3FR5; -.
DR PDBsum; 3P6C; -.
DR PDBsum; 3P6D; -.
DR PDBsum; 3P6E; -.
DR PDBsum; 3P6F; -.
DR PDBsum; 3P6G; -.
DR PDBsum; 3P6H; -.
DR PDBsum; 3Q6L; -.
DR PDBsum; 3RZY; -.
DR PDBsum; 4NNS; -.
DR PDBsum; 4NNT; -.
DR PDBsum; 5D45; -.
DR PDBsum; 5D47; -.
DR PDBsum; 5D48; -.
DR PDBsum; 5D4A; -.
DR PDBsum; 5EDB; -.
DR PDBsum; 5EDC; -.
DR PDBsum; 5HZ6; -.
DR PDBsum; 5HZ8; -.
DR PDBsum; 5Y0F; -.
DR PDBsum; 5Y0G; -.
DR PDBsum; 5Y0X; -.
DR PDBsum; 5Y12; -.
DR PDBsum; 5Y13; -.
DR PDBsum; 6AYL; -.
DR PDBsum; 6LJS; -.
DR PDBsum; 6LJT; -.
DR PDBsum; 6LJU; -.
DR PDBsum; 6LJV; -.
DR PDBsum; 6LJW; -.
DR PDBsum; 6LJX; -.
DR AlphaFoldDB; P15090; -.
DR SMR; P15090; -.
DR BioGRID; 108465; 40.
DR IntAct; P15090; 10.
DR MINT; P15090; -.
DR STRING; 9606.ENSP00000256104; -.
DR BindingDB; P15090; -.
DR ChEMBL; CHEMBL2083; -.
DR DrugBank; DB08607; (5R)-5-(4-{[(2R)-6-HYDROXY-2,5,7,8-TETRAMETHYL-3,4-DIHYDRO-2H-CHROMEN-2-YL]METHOXY}BENZYL)-1,3-THIAZOLIDINE-2,4-DIONE.
DR DrugBank; DB02776; 1-Hexadecanosulfonic Acid.
DR DrugBank; DB03009; 2-{[2-Oxo-2-(1-piperidinyl)ethyl]sulfanyl}-6-(trifluoromethyl)-4(1H)-pyrimidinone.
DR DrugBank; DB02153; 3-sulfino-L-alanine.
DR DrugBank; DB07945; 5-(3-carbamoylbenzyl)-5,6,7,8,9,10-hexahydrocyclohepta[b]indole-4-carboxylic acid.
DR DrugBank; DB04474; 8-anilinonaphthalene-1-sulfonic acid.
DR DrugBank; DB07283; 9-benzyl-2,3,4,9-tetrahydro-1H-carbazole-8-carboxylic acid.
DR DrugBank; DB04557; Arachidonic Acid.
DR DrugBank; DB03851; Carbazole Butanoic Acid.
DR DrugBank; DB04437; Cysteine-Methylene-Carbamoyl-1,10-Phenanthroline.
DR DrugBank; DB04224; Oleic Acid.
DR DrugBank; DB03796; Palmitic Acid.
DR DrugBank; DB03766; Propanoic acid.
DR DrugCentral; P15090; -.
DR GuidetoPHARMACOLOGY; 2534; -.
DR iPTMnet; P15090; -.
DR PhosphoSitePlus; P15090; -.
DR SwissPalm; P15090; -.
DR BioMuta; FABP4; -.
DR DMDM; 119781; -.
DR UCD-2DPAGE; P15090; -.
DR jPOST; P15090; -.
DR MassIVE; P15090; -.
DR MaxQB; P15090; -.
DR PaxDb; P15090; -.
DR PeptideAtlas; P15090; -.
DR PRIDE; P15090; -.
DR ProteomicsDB; 53106; -.
DR ABCD; P15090; 2 sequenced antibodies.
DR Antibodypedia; 994; 839 antibodies from 46 providers.
DR DNASU; 2167; -.
DR Ensembl; ENST00000256104.5; ENSP00000256104.4; ENSG00000170323.9.
DR GeneID; 2167; -.
DR KEGG; hsa:2167; -.
DR MANE-Select; ENST00000256104.5; ENSP00000256104.4; NM_001442.3; NP_001433.1.
DR UCSC; uc003ycd.3; human.
DR CTD; 2167; -.
DR DisGeNET; 2167; -.
DR GeneCards; FABP4; -.
DR HGNC; HGNC:3559; FABP4.
DR HPA; ENSG00000170323; Group enriched (adipose tissue, breast).
DR MIM; 600434; gene.
DR neXtProt; NX_P15090; -.
DR OpenTargets; ENSG00000170323; -.
DR PharmGKB; PA27960; -.
DR VEuPathDB; HostDB:ENSG00000170323; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000160340; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; P15090; -.
DR OMA; LTAKCIM; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; P15090; -.
DR TreeFam; TF316894; -.
DR PathwayCommons; P15090; -.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; P15090; -.
DR SIGNOR; P15090; -.
DR BioGRID-ORCS; 2167; 16 hits in 1061 CRISPR screens.
DR ChiTaRS; FABP4; human.
DR EvolutionaryTrace; P15090; -.
DR GeneWiki; Adipocyte_protein_2; -.
DR GenomeRNAi; 2167; -.
DR Pharos; P15090; Tchem.
DR PRO; PR:P15090; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P15090; protein.
DR Bgee; ENSG00000170323; Expressed in adipose tissue of abdominal region and 162 other tissues.
DR ExpressionAtlas; P15090; baseline and differential.
DR Genevisible; P15090; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0051427; F:hormone receptor binding; IEA:Ensembl.
DR GO; GO:0036041; F:long-chain fatty acid binding; ISS:UniProtKB.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISS:UniProtKB.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0015909; P:long-chain fatty acid transport; ISS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0050872; P:white fat cell differentiation; IEA:Ensembl.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR033073; FABP4.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF83; PTHR11955:SF83; 1.
DR Pfam; PF00061; Lipocalin; 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 Lipid-binding; Nucleus; Phosphoprotein; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..132
FT /note="Fatty acid-binding protein, adipocyte"
FT /id="PRO_0000067366"
FT MOTIF 22..32
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT BINDING 127..129
FT /ligand="a fatty acid"
FT /ligand_id="ChEBI:CHEBI:28868"
FT MOD_RES 2
FT /note="N-acetylcysteine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04117"
FT MOD_RES 20
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250"
FT VARIANT 23
FT /note="E -> D (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1319351179)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036320"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:3P6D"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:3P6D"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:3P6D"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:3P6D"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:3P6D"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:3P6D"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:3P6D"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:3P6D"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6AYL"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:3P6D"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:3P6D"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:3P6D"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:3P6D"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:3P6D"
SQ SEQUENCE 132 AA; 14719 MW; 819D788FF4BF7235 CRC64;
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDVI TIKSESTFKN
TEISFILGQE FDEVTADDRK VKSTITLDGG VLVHVQKWDG KSTTIKRKRE DDKLVVECVM
KGVTSTRVYE RA
