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 27-MAR-2024, entry version 218. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7FVU; X-ray; 1.24 A; A=3-132. DR PDB; 7FVV; X-ray; 1.08 A; A=1-132. DR PDB; 7FVW; X-ray; 1.04 A; A=1-132. DR PDB; 7FVX; X-ray; 1.05 A; A=1-132. DR PDB; 7FVY; X-ray; 1.00 A; A=1-132. DR PDB; 7FVZ; X-ray; 1.12 A; A=1-132. DR PDB; 7FW0; X-ray; 1.12 A; A=1-132. DR PDB; 7FW1; X-ray; 1.26 A; A=1-132. DR PDB; 7FW2; X-ray; 1.12 A; A=1-132. DR PDB; 7FW3; X-ray; 1.08 A; A=1-132. DR PDB; 7FW4; X-ray; 1.44 A; A=1-132. DR PDB; 7FW5; X-ray; 1.15 A; A=1-132. DR PDB; 7FW6; X-ray; 1.04 A; A=1-132. DR PDB; 7FW7; X-ray; 1.06 A; A=1-132. DR PDB; 7FW8; X-ray; 1.16 A; A=1-132. DR PDB; 7FW9; X-ray; 1.00 A; A=1-132. DR PDB; 7FWA; X-ray; 1.07 A; A=1-132. DR PDB; 7FWB; X-ray; 1.12 A; A=1-132. DR PDB; 7FWC; X-ray; 1.12 A; A=1-132. DR PDB; 7FWD; X-ray; 1.12 A; A=1-132. DR PDB; 7FWE; X-ray; 1.05 A; A=1-132. DR PDB; 7FWF; X-ray; 1.24 A; A=1-132. DR PDB; 7FWG; X-ray; 1.13 A; A=1-132. DR PDB; 7FWH; X-ray; 1.12 A; A=1-132. DR PDB; 7FWJ; X-ray; 1.08 A; A=1-132. DR PDB; 7FWK; X-ray; 0.95 A; A=1-132. DR PDB; 7FWL; X-ray; 1.12 A; A=1-132. DR PDB; 7FWM; X-ray; 1.17 A; A=1-132. DR PDB; 7FWN; X-ray; 1.12 A; A=1-132. DR PDB; 7FWO; X-ray; 1.12 A; A=1-132. DR PDB; 7FWP; X-ray; 1.03 A; A=1-132. DR PDB; 7FWQ; X-ray; 1.20 A; A=1-132. DR PDB; 7FWR; X-ray; 1.12 A; A=1-132. DR PDB; 7FWS; X-ray; 1.10 A; A=1-132. DR PDB; 7FWU; X-ray; 1.01 A; A=1-132. DR PDB; 7FWV; X-ray; 1.45 A; A=1-132. DR PDB; 7FWW; X-ray; 1.05 A; A=1-132. DR PDB; 7FWX; X-ray; 1.13 A; A=1-132. DR PDB; 7FWY; X-ray; 1.12 A; A=1-132. DR PDB; 7FWZ; X-ray; 1.12 A; A=1-132. DR PDB; 7FX0; X-ray; 1.03 A; A=1-132. DR PDB; 7FX1; X-ray; 0.99 A; A=1-132. DR PDB; 7FX2; X-ray; 1.47 A; A=1-132. DR PDB; 7FX3; X-ray; 1.12 A; A=1-132. DR PDB; 7FX4; X-ray; 1.02 A; A=1-132. DR PDB; 7FX5; X-ray; 1.12 A; A=1-132. DR PDB; 7FX6; X-ray; 1.05 A; A=1-132. DR PDB; 7FX7; X-ray; 1.12 A; A=1-132. DR PDB; 7FX8; X-ray; 1.12 A; A=1-132. DR PDB; 7FX9; X-ray; 1.10 A; A=1-132. DR PDB; 7FXA; X-ray; 1.12 A; A=1-132. DR PDB; 7FXB; X-ray; 1.12 A; A=1-132. DR PDB; 7FXC; X-ray; 1.12 A; A=1-132. DR PDB; 7FXE; X-ray; 1.04 A; A=1-132. DR PDB; 7FXF; X-ray; 0.95 A; A=1-132. DR PDB; 7FXG; X-ray; 1.12 A; A=1-132. DR PDB; 7FXH; X-ray; 1.02 A; A=1-132. DR PDB; 7FXI; X-ray; 1.51 A; A=1-132. DR PDB; 7FXJ; X-ray; 1.03 A; A=1-132. DR PDB; 7FXK; X-ray; 1.03 A; A=1-132. DR PDB; 7FXL; X-ray; 1.12 A; A=1-132. DR PDB; 7FXM; X-ray; 1.19 A; A=1-132. DR PDB; 7FXN; X-ray; 1.02 A; A=1-132. DR PDB; 7FXP; X-ray; 1.05 A; A=1-132. DR PDB; 7FXQ; X-ray; 1.12 A; A=1-132. DR PDB; 7FXR; X-ray; 0.99 A; A=1-132. DR PDB; 7FXS; X-ray; 1.25 A; A=1-132. DR PDB; 7FXT; X-ray; 1.07 A; A=1-132. DR PDB; 7FXU; X-ray; 1.96 A; A=1-132. DR PDB; 7FXV; X-ray; 0.88 A; A=1-132. DR PDB; 7FXW; X-ray; 1.18 A; A=1-132. DR PDB; 7FXX; X-ray; 1.29 A; A=1-132. DR PDB; 7FXY; X-ray; 1.13 A; A=1-132. DR PDB; 7FXZ; X-ray; 1.03 A; A=1-132. DR PDB; 7FY2; X-ray; 1.12 A; A=1-132. DR PDB; 7FY3; X-ray; 1.12 A; A=1-132. DR PDB; 7FY4; X-ray; 1.51 A; A=1-132. DR PDB; 7FY5; X-ray; 1.12 A; A=1-132. DR PDB; 7FY6; X-ray; 1.12 A; A=1-132. DR PDB; 7FY7; X-ray; 1.05 A; A=1-132. DR PDB; 7FY9; X-ray; 1.74 A; A=1-132. DR PDB; 7FYB; X-ray; 1.05 A; A=1-132. DR PDB; 7FYC; X-ray; 1.08 A; A=1-132. DR PDB; 7FYE; X-ray; 1.25 A; A=1-132. DR PDB; 7FYF; X-ray; 1.02 A; A=1-132. DR PDB; 7FYG; X-ray; 0.94 A; A=1-132. DR PDB; 7FYH; X-ray; 1.34 A; A=1-132. DR PDB; 7FYI; X-ray; 1.14 A; A=1-132. DR PDB; 7FYJ; X-ray; 2.60 A; A/B=1-132. DR PDB; 7FYK; X-ray; 1.12 A; A=1-132. DR PDB; 7FYL; X-ray; 1.07 A; A=1-132. DR PDB; 7FYM; X-ray; 1.21 A; A=1-132. DR PDB; 7FYO; X-ray; 1.12 A; A=1-132. DR PDB; 7FYP; X-ray; 1.12 A; A=1-132. DR PDB; 7FYQ; X-ray; 1.12 A; A=1-132. DR PDB; 7FYR; X-ray; 1.05 A; A=1-132. DR PDB; 7FYS; X-ray; 1.05 A; A=1-132. DR PDB; 7FYT; X-ray; 1.24 A; A=1-132. DR PDB; 7FYU; X-ray; 1.17 A; A=1-132. DR PDB; 7FYV; X-ray; 0.97 A; A=1-132. DR PDB; 7FYX; X-ray; 1.40 A; A=1-132. DR PDB; 7FYY; X-ray; 1.12 A; A=1-132. DR PDB; 7FYZ; X-ray; 1.13 A; A=1-132. DR PDB; 7FZ0; X-ray; 1.02 A; A=1-132. DR PDB; 7FZ1; X-ray; 0.99 A; A=1-132. DR PDB; 7FZ2; X-ray; 1.12 A; A=1-132. DR PDB; 7FZ3; X-ray; 1.10 A; A=1-132. DR PDB; 7FZ4; X-ray; 1.01 A; A=3-132. DR PDB; 7FZ5; X-ray; 1.25 A; A=1-132. DR PDB; 7FZ6; X-ray; 1.09 A; A=1-132. DR PDB; 7FZ7; X-ray; 1.12 A; A=1-132. DR PDB; 7FZ8; X-ray; 1.22 A; A=1-132. DR PDB; 7FZ9; X-ray; 0.96 A; A=1-132. DR PDB; 7FZA; X-ray; 2.60 A; A/B=1-132. DR PDB; 7FZB; X-ray; 1.08 A; A=1-132. DR PDB; 7FZC; X-ray; 1.12 A; A=1-132. DR PDB; 7FZD; X-ray; 1.02 A; A=1-132. DR PDB; 7FZE; X-ray; 1.17 A; A=1-132. DR PDB; 7FZF; X-ray; 1.09 A; A=1-132. DR PDB; 7FZH; X-ray; 1.12 A; A=1-132. DR PDB; 7FZI; X-ray; 1.07 A; A=1-132. DR PDB; 7FZJ; X-ray; 1.25 A; A=1-132. DR PDB; 7FZK; X-ray; 1.12 A; A=1-132. DR PDB; 7FZL; X-ray; 1.12 A; A=1-132. DR PDB; 7FZM; X-ray; 1.05 A; A=1-132. DR PDB; 7FZN; X-ray; 1.12 A; A=1-132. DR PDB; 7FZO; X-ray; 0.99 A; A=1-132. DR PDB; 7FZP; X-ray; 1.12 A; A=1-132. DR PDB; 7FZR; X-ray; 1.12 A; A=1-132. DR PDB; 7FZS; X-ray; 1.04 A; A=1-132. DR PDB; 7FZT; X-ray; 1.40 A; A=1-132. DR PDB; 7FZU; X-ray; 1.25 A; A=1-132. DR PDB; 7FZV; X-ray; 2.55 A; A/B=1-132. DR PDB; 7FZW; X-ray; 1.24 A; A=3-132. DR PDB; 7FZX; X-ray; 1.07 A; A=1-132. DR PDB; 7FZY; X-ray; 1.17 A; A=1-132. DR PDB; 7FZZ; X-ray; 1.12 A; A=1-132. DR PDB; 7G02; X-ray; 1.03 A; A=1-132. DR PDB; 7G03; X-ray; 1.27 A; A=1-132. DR PDB; 7G05; X-ray; 0.95 A; A=1-132. DR PDB; 7G06; X-ray; 1.26 A; A=1-132. DR PDB; 7G07; X-ray; 1.61 A; A=1-132. DR PDB; 7G08; X-ray; 0.99 A; A=1-132. DR PDB; 7G09; X-ray; 1.05 A; A=1-132. DR PDB; 7G0A; X-ray; 1.12 A; A=1-132. DR PDB; 7G0C; X-ray; 1.14 A; A=1-132. DR PDB; 7G0F; X-ray; 1.12 A; A=1-132. DR PDB; 7G0G; X-ray; 1.12 A; A=1-132. DR PDB; 7G0H; X-ray; 1.46 A; A=1-132. DR PDB; 7G0I; X-ray; 1.07 A; A=1-132. DR PDB; 7G0J; X-ray; 1.08 A; A=1-132. DR PDB; 7G0K; X-ray; 1.13 A; A=1-132. DR PDB; 7G0L; X-ray; 1.18 A; A=1-132. DR PDB; 7G0M; X-ray; 1.05 A; A=1-132. DR PDB; 7G0N; X-ray; 1.12 A; A=1-132. DR PDB; 7G0O; X-ray; 1.32 A; A=1-132. DR PDB; 7G0P; X-ray; 1.02 A; A=1-132. DR PDB; 7G0Q; X-ray; 1.02 A; A=1-132. DR PDB; 7G0R; X-ray; 1.03 A; A=1-132. DR PDB; 7G0S; X-ray; 1.02 A; A=1-132. DR PDB; 7G0T; X-ray; 1.65 A; A=1-132. DR PDB; 7G0U; X-ray; 1.12 A; A=1-132. DR PDB; 7G0V; X-ray; 1.06 A; A=1-132. DR PDB; 7G0X; X-ray; 1.48 A; A=1-132. DR PDB; 7G0Y; X-ray; 0.99 A; A=1-132. DR PDB; 7G0Z; X-ray; 0.84 A; A=1-132. DR PDB; 7G10; X-ray; 1.26 A; A=1-132. DR PDB; 7G11; X-ray; 1.12 A; A=1-132. DR PDB; 7G12; X-ray; 1.64 A; A=1-132. DR PDB; 7G13; X-ray; 1.15 A; A=1-132. DR PDB; 7G14; X-ray; 1.20 A; A=1-132. DR PDB; 7G15; X-ray; 1.28 A; A=1-132. DR PDB; 7G16; X-ray; 1.10 A; A=1-132. DR PDB; 7G17; X-ray; 1.05 A; A=1-132. DR PDB; 7G18; X-ray; 1.12 A; A=1-132. DR PDB; 7G19; X-ray; 1.04 A; A=1-132. DR PDB; 7G1A; X-ray; 1.12 A; A=1-132. DR PDB; 7G1B; X-ray; 1.17 A; A=1-132. DR PDB; 7G1C; X-ray; 1.08 A; A=1-132. DR PDB; 7G1D; X-ray; 1.12 A; A=1-132. DR PDB; 7G1E; X-ray; 1.21 A; A=1-132. DR PDB; 7G1F; X-ray; 0.91 A; A=1-132. DR PDB; 7G1G; X-ray; 1.03 A; A=1-132. DR PDB; 7G1H; X-ray; 1.12 A; A=1-132. DR PDB; 7G1I; X-ray; 1.53 A; A=1-132. DR PDB; 7G1J; X-ray; 1.11 A; A=1-132. DR PDB; 7G1K; X-ray; 1.12 A; A=1-132. DR PDB; 7G1L; X-ray; 0.98 A; A=1-132. DR PDB; 7G1M; X-ray; 1.34 A; A=1-132. DR PDB; 7G1N; X-ray; 1.55 A; A=1-132. DR PDB; 7G1O; X-ray; 1.12 A; A=1-132. DR PDB; 7G1P; X-ray; 1.28 A; A=1-132. DR PDB; 7G1R; X-ray; 0.93 A; A=1-132. DR PDB; 7G1S; X-ray; 1.08 A; A=1-132. DR PDB; 7G1T; X-ray; 1.10 A; A=1-132. DR PDB; 7G1U; X-ray; 1.14 A; A=1-132. DR PDB; 7G1V; X-ray; 1.02 A; A=1-132. DR PDB; 7G1W; X-ray; 1.34 A; A=1-132. DR PDB; 7G1Y; X-ray; 0.95 A; A=1-132. DR PDB; 7G1Z; X-ray; 1.12 A; A=1-132. DR PDB; 7G20; X-ray; 1.12 A; A=1-132. DR PDB; 7G21; X-ray; 1.12 A; A=1-132. DR PDB; 7WC3; X-ray; 1.50 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 PDBsum; 7FVU; -. DR PDBsum; 7FVV; -. DR PDBsum; 7FVW; -. DR PDBsum; 7FVX; -. DR PDBsum; 7FVY; -. DR PDBsum; 7FVZ; -. DR PDBsum; 7FW0; -. DR PDBsum; 7FW1; -. DR PDBsum; 7FW2; -. DR PDBsum; 7FW3; -. DR PDBsum; 7FW4; -. DR PDBsum; 7FW5; -. DR PDBsum; 7FW6; -. DR PDBsum; 7FW7; -. DR PDBsum; 7FW8; -. DR PDBsum; 7FW9; -. DR PDBsum; 7FWA; -. DR PDBsum; 7FWB; -. DR PDBsum; 7FWC; -. DR PDBsum; 7FWD; -. DR PDBsum; 7FWE; -. DR PDBsum; 7FWF; -. DR PDBsum; 7FWG; -. DR PDBsum; 7FWH; -. DR PDBsum; 7FWJ; -. DR PDBsum; 7FWK; -. DR PDBsum; 7FWL; -. DR PDBsum; 7FWM; -. DR PDBsum; 7FWN; -. DR PDBsum; 7FWO; -. DR PDBsum; 7FWP; -. DR PDBsum; 7FWQ; -. DR PDBsum; 7FWR; -. DR PDBsum; 7FWS; -. DR PDBsum; 7FWU; -. DR PDBsum; 7FWV; -. DR PDBsum; 7FWW; -. DR PDBsum; 7FWX; -. DR PDBsum; 7FWY; -. DR PDBsum; 7FWZ; -. DR PDBsum; 7FX0; -. DR PDBsum; 7FX1; -. DR PDBsum; 7FX2; -. DR PDBsum; 7FX3; -. DR PDBsum; 7FX4; -. DR PDBsum; 7FX5; -. DR PDBsum; 7FX6; -. DR PDBsum; 7FX7; -. DR PDBsum; 7FX8; -. DR PDBsum; 7FX9; -. DR PDBsum; 7FXA; -. DR PDBsum; 7FXB; -. DR PDBsum; 7FXC; -. DR PDBsum; 7FXE; -. DR PDBsum; 7FXF; -. DR PDBsum; 7FXG; -. DR PDBsum; 7FXH; -. DR PDBsum; 7FXI; -. DR PDBsum; 7FXJ; -. DR PDBsum; 7FXK; -. DR PDBsum; 7FXL; -. DR PDBsum; 7FXM; -. DR PDBsum; 7FXN; -. DR PDBsum; 7FXP; -. DR PDBsum; 7FXQ; -. DR PDBsum; 7FXR; -. DR PDBsum; 7FXS; -. DR PDBsum; 7FXT; -. DR PDBsum; 7FXU; -. DR PDBsum; 7FXV; -. DR PDBsum; 7FXW; -. DR PDBsum; 7FXX; -. DR PDBsum; 7FXY; -. DR PDBsum; 7FXZ; -. DR PDBsum; 7FY2; -. DR PDBsum; 7FY3; -. DR PDBsum; 7FY4; -. DR PDBsum; 7FY5; -. DR PDBsum; 7FY6; -. DR PDBsum; 7FY7; -. DR PDBsum; 7FY9; -. DR PDBsum; 7FYB; -. DR PDBsum; 7FYC; -. DR PDBsum; 7FYE; -. DR PDBsum; 7FYF; -. DR PDBsum; 7FYG; -. DR PDBsum; 7FYH; -. DR PDBsum; 7FYI; -. DR PDBsum; 7FYJ; -. DR PDBsum; 7FYK; -. DR PDBsum; 7FYL; -. DR PDBsum; 7FYM; -. DR PDBsum; 7FYO; -. DR PDBsum; 7FYP; -. DR PDBsum; 7FYQ; -. DR PDBsum; 7FYR; -. DR PDBsum; 7FYS; -. DR PDBsum; 7FYT; -. DR PDBsum; 7FYU; -. DR PDBsum; 7FYV; -. DR PDBsum; 7FYX; -. DR PDBsum; 7FYY; -. DR PDBsum; 7FYZ; -. DR PDBsum; 7FZ0; -. DR PDBsum; 7FZ1; -. DR PDBsum; 7FZ2; -. DR PDBsum; 7FZ3; -. DR PDBsum; 7FZ4; -. DR PDBsum; 7FZ5; -. DR PDBsum; 7FZ6; -. DR PDBsum; 7FZ7; -. DR PDBsum; 7FZ8; -. DR PDBsum; 7FZ9; -. DR PDBsum; 7FZA; -. DR PDBsum; 7FZB; -. DR PDBsum; 7FZC; -. DR PDBsum; 7FZD; -. DR PDBsum; 7FZE; -. DR PDBsum; 7FZF; -. DR PDBsum; 7FZH; -. DR PDBsum; 7FZI; -. DR PDBsum; 7FZJ; -. DR PDBsum; 7FZK; -. DR PDBsum; 7FZL; -. DR PDBsum; 7FZM; -. DR PDBsum; 7FZN; -. DR PDBsum; 7FZO; -. DR PDBsum; 7FZP; -. DR PDBsum; 7FZR; -. DR PDBsum; 7FZS; -. DR PDBsum; 7FZT; -. DR PDBsum; 7FZU; -. DR PDBsum; 7FZV; -. DR PDBsum; 7FZW; -. DR PDBsum; 7FZX; -. DR PDBsum; 7FZY; -. DR PDBsum; 7FZZ; -. DR PDBsum; 7G02; -. DR PDBsum; 7G03; -. DR PDBsum; 7G05; -. DR PDBsum; 7G06; -. DR PDBsum; 7G07; -. DR PDBsum; 7G08; -. DR PDBsum; 7G09; -. DR PDBsum; 7G0A; -. DR PDBsum; 7G0C; -. DR PDBsum; 7G0F; -. DR PDBsum; 7G0G; -. DR PDBsum; 7G0H; -. DR PDBsum; 7G0I; -. DR PDBsum; 7G0J; -. DR PDBsum; 7G0K; -. DR PDBsum; 7G0L; -. DR PDBsum; 7G0M; -. DR PDBsum; 7G0N; -. DR PDBsum; 7G0O; -. DR PDBsum; 7G0P; -. DR PDBsum; 7G0Q; -. DR PDBsum; 7G0R; -. DR PDBsum; 7G0S; -. DR PDBsum; 7G0T; -. DR PDBsum; 7G0U; -. DR PDBsum; 7G0V; -. DR PDBsum; 7G0X; -. DR PDBsum; 7G0Y; -. DR PDBsum; 7G0Z; -. DR PDBsum; 7G10; -. DR PDBsum; 7G11; -. DR PDBsum; 7G12; -. DR PDBsum; 7G13; -. DR PDBsum; 7G14; -. DR PDBsum; 7G15; -. DR PDBsum; 7G16; -. DR PDBsum; 7G17; -. DR PDBsum; 7G18; -. DR PDBsum; 7G19; -. DR PDBsum; 7G1A; -. DR PDBsum; 7G1B; -. DR PDBsum; 7G1C; -. DR PDBsum; 7G1D; -. DR PDBsum; 7G1E; -. DR PDBsum; 7G1F; -. DR PDBsum; 7G1G; -. DR PDBsum; 7G1H; -. DR PDBsum; 7G1I; -. DR PDBsum; 7G1J; -. DR PDBsum; 7G1K; -. DR PDBsum; 7G1L; -. DR PDBsum; 7G1M; -. DR PDBsum; 7G1N; -. DR PDBsum; 7G1O; -. DR PDBsum; 7G1P; -. DR PDBsum; 7G1R; -. DR PDBsum; 7G1S; -. DR PDBsum; 7G1T; -. DR PDBsum; 7G1U; -. DR PDBsum; 7G1V; -. DR PDBsum; 7G1W; -. DR PDBsum; 7G1Y; -. DR PDBsum; 7G1Z; -. DR PDBsum; 7G20; -. DR PDBsum; 7G21; -. DR PDBsum; 7WC3; -. DR AlphaFoldDB; P15090; -. DR SMR; P15090; -. DR BioGRID; 108465; 41. 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 CPTAC; CPTAC-5845; -. DR CPTAC; CPTAC-5870; -. DR jPOST; P15090; -. DR MassIVE; P15090; -. DR MaxQB; P15090; -. DR PaxDb; 9606-ENSP00000256104; -. DR PeptideAtlas; P15090; -. DR ProteomicsDB; 53106; -. DR Pumba; P15090; -. DR ABCD; P15090; 2 sequenced antibodies. DR Antibodypedia; 994; 939 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 AGR; HGNC:3559; -. 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; CIMGDVI; -. DR OrthoDB; 46617at2759; -. 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; 17 hits in 1136 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 163 other cell types or tissues. DR ExpressionAtlas; P15090; baseline and differential. 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:0045892; P:negative regulation of DNA-templated transcription; 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 CDD; cd19467; FABP4; 1. DR Gene3D; 2.40.128.20; -; 1. DR InterPro; IPR012674; Calycin. DR InterPro; IPR000463; Fatty_acid-bd. DR InterPro; IPR031259; ILBP. DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom. DR PANTHER; PTHR11955; FATTY ACID BINDING PROTEIN; 1. DR PANTHER; PTHR11955:SF83; FATTY ACID-BINDING PROTEIN, ADIPOCYTE; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR00178; FATTYACIDBP. DR SUPFAM; SSF50814; Lipocalins; 1. DR PROSITE; PS00214; FABP; 1. DR UCD-2DPAGE; P15090; -. DR Genevisible; P15090; HS. 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 //