FABP4_MOUSE
ID FABP4_MOUSE Reviewed; 132 AA.
AC P04117;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Fatty acid-binding protein, adipocyte;
DE AltName: Full=3T3-L1 lipid-binding protein;
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;
DE AltName: Full=Myelin P2 protein homolog;
DE AltName: Full=P15;
DE AltName: Full=P2 adipocyte protein;
DE AltName: Full=Protein 422;
GN Name=Fabp4; Synonyms=Ap2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6206497; DOI=10.1073/pnas.81.17.5468;
RA Bernlohr D.A., Angus C.W., Lane M.D., Bolanowski M.A., Kelly T.J. Jr.;
RT "Expression of specific mRNAs during adipose differentiation:
RT identification of an mRNA encoding a homologue of myelin P2 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5468-5472(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3520554; DOI=10.1073/pnas.83.11.3786;
RA Hunt C.R., Ro J.H.-S., Dobson D.E., Min H.Y., Spiegelman B.M.;
RT "Adipocyte P2 gene: developmental expression and homology of 5'-flanking
RT sequences among fat cell-specific genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3786-3790(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3015943; DOI=10.1016/s0021-9258(18)67461-7;
RA Phillips M., Djian P., Green H.;
RT "The nucleotide sequence of three genes participating in the adipose
RT differentiation of 3T3 cells.";
RL J. Biol. Chem. 261:10821-10827(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 PROTEIN SEQUENCE OF 2-132.
RX PubMed=2844775; DOI=10.1016/s0021-9258(18)68254-7;
RA Matarese V., Bernlohr D.A.;
RT "Purification of murine adipocyte lipid-binding protein. Characterization
RT as a fatty acid- and retinoic acid-binding protein.";
RL J. Biol. Chem. 263:14544-14551(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RX PubMed=2452440; DOI=10.1073/pnas.85.9.2949;
RA Cook J.S., Lucas J.J., Sibley E., Bolanowski M.A., Christy R.J.,
RA Kelly T.J. Jr., Lane M.D.;
RT "Expression of the differentiation-induced gene for fatty acid-binding
RT protein is activated by glucocorticoid and cAMP.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:2949-2953(1988).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-132.
RX PubMed=3968175; DOI=10.1083/jcb.100.2.514;
RA Cook K.S., Hunt C.R., Spiegelman B.M.;
RT "Developmentally regulated mRNAs in 3T3-adipocytes: analysis of
RT transcriptional control.";
RL J. Cell Biol. 100:514-520(1985).
RN [9]
RP PROTEIN SEQUENCE OF 25-35; 37-51 AND 59-88.
RC TISSUE=Mammary gland;
RX PubMed=8447836; DOI=10.1006/bbrc.1993.1184;
RA Bansal M.P., Medina D.;
RT "Expression of fatty acid-binding proteins in the developing mouse mammary
RT gland.";
RL Biochem. Biophys. Res. Commun. 191:61-69(1993).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PPARG.
RX PubMed=12077340; DOI=10.1128/mcb.22.14.5114-5127.2002;
RA Tan N.-S., Shaw N.S., Vinckenbosch N., Liu P., Yasmin R., Desvergne B.,
RA Wahli W., Noy N.;
RT "Selective cooperation between fatty acid binding proteins and peroxisome
RT proliferator-activated receptors in regulating transcription.";
RL Mol. Cell. Biol. 22:5114-5127(2002).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PPARG.
RX PubMed=16574478; DOI=10.1016/j.bbalip.2006.02.006;
RA Adida A., Spener F.;
RT "Adipocyte-type fatty acid-binding protein as inter-compartmental shuttle
RT for peroxisome proliferator activated receptor gamma agonists in cultured
RT cell.";
RL Biochim. Biophys. Acta 1761:172-181(2006).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-22; ARG-31; LYS-32;
RP LEU-67; LEU-87 AND LEU-92.
RX PubMed=17516629; DOI=10.1021/bi700047a;
RA Ayers S.D., Nedrow K.L., Gillilan R.E., Noy N.;
RT "Continuous nucleocytoplasmic shuttling underlies transcriptional
RT activation of PPARgamma by FABP4.";
RL Biochemistry 46:6744-6752(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1554730; DOI=10.1021/bi00128a024;
RA Xu Z., Bernlohr D.A., Banaszak L.J.;
RT "Crystal structure of recombinant murine adipocyte lipid-binding protein.";
RL Biochemistry 31:3484-3492(1992).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=8463311; DOI=10.1016/s0021-9258(18)53039-8;
RA Xu Z., Bernlohr D.A., Banaszak L.J.;
RT "The adipocyte lipid-binding protein at 1.6-A resolution. Crystal
RT structures of the apoprotein and with bound saturated and unsaturated fatty
RT acids.";
RL J. Biol. Chem. 268:7874-7884(1993).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=10423455; DOI=10.1016/s0006-3495(99)76961-4;
RA Ory J.J., Banaszak L.J.;
RT "Studies of the ligand binding reaction of adipocyte lipid binding protein
RT using the fluorescent probe 1, 8-anilinonaphthalene-8-sulfonate.";
RL Biophys. J. 77:1107-1116(1999).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
RX PubMed=8161548; DOI=10.1021/bi00182a017;
RA LaLonde J.M., Bernlohr D.A., Banaszak L.J.;
RT "X-ray crystallographic structures of adipocyte lipid-binding protein
RT complexed with palmitate and hexadecanesulfonic acid. Properties of cavity
RT binding sites.";
RL Biochemistry 33:4885-4895(1994).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
RX PubMed=7929228; DOI=10.2210/pdb1adl/pdb;
RA LaLonde J.M., Levenson M.A., Roe J.J., Bernlohr D.A., Banaszak L.J.;
RT "Adipocyte lipid-binding protein complexed with arachidonic acid. Titration
RT calorimetry and X-ray crystallographic studies.";
RL J. Biol. Chem. 269:25339-25347(1994).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
RX PubMed=14594993; DOI=10.1194/jlr.m300113-jlr200;
RA Reese A.J., Banaszak L.J.;
RT "Specificity determinants for lipids bound to beta-barrel proteins.";
RL J. Lipid Res. 45:232-243(2004).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH TROGLITAZONE AND
RP LINOLEIC ACID, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-58;
RP LEU-67; LEU-87 AND LEU-92.
RX PubMed=17761196; DOI=10.1016/j.jmb.2007.07.040;
RA Gillilan R.E., Ayers S.D., Noy N.;
RT "Structural basis for activation of fatty acid-binding protein 4.";
RL J. Mol. Biol. 372:1246-1260(2007).
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:0000269|PubMed:12077340, ECO:0000269|PubMed:16574478,
CC ECO:0000269|PubMed:17516629}.
CC -!- SUBUNIT: Monomer (By similarity). Homodimer. Interacts with PPARG.
CC {ECO:0000250, ECO:0000269|PubMed:12077340, ECO:0000269|PubMed:14594993,
CC ECO:0000269|PubMed:16574478, ECO:0000269|PubMed:17761196,
CC ECO:0000269|PubMed:7929228, ECO:0000269|PubMed:8161548}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17516629,
CC ECO:0000269|PubMed:17761196}. Nucleus {ECO:0000269|PubMed:17516629,
CC ECO:0000269|PubMed:17761196}. 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 (PubMed:17516629). Subject
CC to constitutive nuclear export (PubMed:17516629, PubMed:17761196).
CC {ECO:0000269|PubMed:17516629, ECO:0000269|PubMed:17761196}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC ligand 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; K02109; AAA39416.1; -; mRNA.
DR EMBL; M13264; AAA39870.1; -; Genomic_DNA.
DR EMBL; M13261; AAA39870.1; JOINED; Genomic_DNA.
DR EMBL; M13262; AAA39870.1; JOINED; Genomic_DNA.
DR EMBL; M13263; AAA39870.1; JOINED; Genomic_DNA.
DR EMBL; M13385; AAA39417.1; -; Genomic_DNA.
DR EMBL; AK003143; BAB22601.1; -; mRNA.
DR EMBL; BC054426; AAH54426.1; -; mRNA.
DR EMBL; M20497; AAA37188.1; -; Genomic_DNA.
DR EMBL; M28726; AAA37112.1; -; mRNA.
DR CCDS; CCDS17238.1; -.
DR PIR; B25952; B25952.
DR RefSeq; NP_077717.1; NM_024406.2.
DR PDB; 1A18; X-ray; 2.40 A; A=2-132.
DR PDB; 1A2D; X-ray; 2.40 A; A/B=2-132.
DR PDB; 1AB0; X-ray; 1.90 A; A=3-132.
DR PDB; 1ACD; X-ray; 2.70 A; A=3-132.
DR PDB; 1ADL; X-ray; 1.60 A; A=2-132.
DR PDB; 1ALB; X-ray; 2.50 A; A=2-132.
DR PDB; 1G74; X-ray; 1.70 A; A=2-132.
DR PDB; 1G7N; X-ray; 1.50 A; A=2-132.
DR PDB; 1LIB; X-ray; 1.70 A; A=2-132.
DR PDB; 1LIC; X-ray; 1.60 A; A=2-132.
DR PDB; 1LID; X-ray; 1.60 A; A=2-132.
DR PDB; 1LIE; X-ray; 1.60 A; A=2-132.
DR PDB; 1LIF; X-ray; 1.60 A; A=2-132.
DR PDB; 2ANS; X-ray; 2.50 A; A/B=2-132.
DR PDB; 2Q9S; X-ray; 2.30 A; A=1-132.
DR PDB; 2QM9; X-ray; 2.31 A; A/B=1-132.
DR PDB; 3HK1; X-ray; 1.70 A; A=2-132.
DR PDB; 3JS1; X-ray; 1.81 A; A/B=2-132.
DR PDB; 3JSQ; X-ray; 2.30 A; A=2-132.
DR PDB; 5C0N; X-ray; 3.00 A; A/B=1-132.
DR PDB; 5D8J; X-ray; 3.00 A; A=1-132.
DR PDBsum; 1A18; -.
DR PDBsum; 1A2D; -.
DR PDBsum; 1AB0; -.
DR PDBsum; 1ACD; -.
DR PDBsum; 1ADL; -.
DR PDBsum; 1ALB; -.
DR PDBsum; 1G74; -.
DR PDBsum; 1G7N; -.
DR PDBsum; 1LIB; -.
DR PDBsum; 1LIC; -.
DR PDBsum; 1LID; -.
DR PDBsum; 1LIE; -.
DR PDBsum; 1LIF; -.
DR PDBsum; 2ANS; -.
DR PDBsum; 2Q9S; -.
DR PDBsum; 2QM9; -.
DR PDBsum; 3HK1; -.
DR PDBsum; 3JS1; -.
DR PDBsum; 3JSQ; -.
DR PDBsum; 5C0N; -.
DR PDBsum; 5D8J; -.
DR AlphaFoldDB; P04117; -.
DR SMR; P04117; -.
DR BioGRID; 198128; 2.
DR STRING; 10090.ENSMUSP00000029041; -.
DR ChEMBL; CHEMBL1075118; -.
DR GuidetoPHARMACOLOGY; 2534; -.
DR CarbonylDB; P04117; -.
DR iPTMnet; P04117; -.
DR MetOSite; P04117; -.
DR PhosphoSitePlus; P04117; -.
DR SWISS-2DPAGE; P04117; -.
DR jPOST; P04117; -.
DR PaxDb; P04117; -.
DR PeptideAtlas; P04117; -.
DR PRIDE; P04117; -.
DR ProteomicsDB; 271547; -.
DR ABCD; P04117; 2 sequenced antibodies.
DR Antibodypedia; 994; 839 antibodies from 46 providers.
DR DNASU; 11770; -.
DR Ensembl; ENSMUST00000029041; ENSMUSP00000029041; ENSMUSG00000062515.
DR GeneID; 11770; -.
DR KEGG; mmu:11770; -.
DR UCSC; uc008opl.2; mouse.
DR CTD; 2167; -.
DR MGI; MGI:88038; Fabp4.
DR VEuPathDB; HostDB:ENSMUSG00000062515; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000160340; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; P04117; -.
DR OMA; LTAKCIM; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; P04117; -.
DR TreeFam; TF316894; -.
DR Reactome; R-MMU-163560; Triglyceride catabolism.
DR BioGRID-ORCS; 11770; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Fabp4; mouse.
DR EvolutionaryTrace; P04117; -.
DR PRO; PR:P04117; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P04117; protein.
DR Bgee; ENSMUSG00000062515; Expressed in intercostal muscle and 183 other tissues.
DR ExpressionAtlas; P04117; baseline and differential.
DR Genevisible; P04117; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0051427; F:hormone receptor binding; IPI:UniProtKB.
DR GO; GO:0036041; F:long-chain fatty acid binding; IDA:UniProtKB.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IDA:UniProtKB.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0071285; P:cellular response to lithium ion; IDA:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:MGI.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0015909; P:long-chain fatty acid transport; IDA:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IGI:YuBioLab.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0050872; P:white fat cell differentiation; IDA:MGI.
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:0000269|PubMed:2844775"
FT CHAIN 2..132
FT /note="Fatty acid-binding protein, adipocyte"
FT /evidence="ECO:0000269|PubMed:2844775"
FT /id="PRO_0000067367"
FT MOTIF 22..32
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:17516629"
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:0000250|UniProtKB:P15090"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 20
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250"
FT MUTAGEN 22
FT /note="K->A: Abolishes ligand-induced translocation to the
FT nucleus; when associated with A-31 and A-32."
FT /evidence="ECO:0000269|PubMed:17516629"
FT MUTAGEN 31
FT /note="R->A: Abolishes ligand-induced translocation to the
FT nucleus; when associated with A-22 and A-32."
FT /evidence="ECO:0000269|PubMed:17516629"
FT MUTAGEN 32
FT /note="K->A: Abolishes ligand-induced translocation to the
FT nucleus; when associated with A-22 and A-31."
FT /evidence="ECO:0000269|PubMed:17516629"
FT MUTAGEN 58
FT /note="F->A: Abolishes ligand-induced translocation to the
FT nucleus."
FT /evidence="ECO:0000269|PubMed:17761196"
FT MUTAGEN 67
FT /note="L->A: Abolishes export from nucleus; when associated
FT with A-87 and A-92."
FT /evidence="ECO:0000269|PubMed:17516629,
FT ECO:0000269|PubMed:17761196"
FT MUTAGEN 87
FT /note="L->A: Abolishes export from nucleus; when associated
FT with A-67 and A-92."
FT /evidence="ECO:0000269|PubMed:17516629,
FT ECO:0000269|PubMed:17761196"
FT MUTAGEN 92
FT /note="L->A: Abolishes export from nucleus; when associated
FT with A-67 and A-87."
FT /evidence="ECO:0000269|PubMed:17516629,
FT ECO:0000269|PubMed:17761196"
FT CONFLICT 40
FT /note="N -> T (in Ref. 1; AAA39870)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="G -> V (in Ref. 2; AAA39417)"
FT /evidence="ECO:0000305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1G7N"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:1G7N"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:1G7N"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:1G7N"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1G7N"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1G7N"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1G7N"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5D8J"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1G7N"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1G7N"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:1G7N"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:1G7N"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1G7N"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:1G7N"
SQ SEQUENCE 132 AA; 14650 MW; ED08EDDBBE2D7E32 CRC64;
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDLV TIRSESTFKN
TEISFKLGVE FDEITADDRK VKSIITLDGG ALVQVQKWDG KSTTIKRKRD GDKLVVECVM
KGVTSTRVYE RA
