ID NR4A1_HUMAN Reviewed; 598 AA. AC P22736; B4DML7; Q15627; Q53Y00; Q6IBU8; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 24-JAN-2024, entry version 235. DE RecName: Full=Nuclear receptor subfamily 4immunitygroup A member 1; DE AltName: Full=Early response protein NAK1; DE AltName: Full=Nuclear hormone receptor NUR/77; DE Short=Nur77; DE AltName: Full=Orphan nuclear receptor HMR; DE AltName: Full=Orphan nuclear receptor TR3; DE AltName: Full=ST-59; DE AltName: Full=Testicular receptor 3; GN Name=NR4A1; Synonyms=GFRP1, HMR, NAK1; 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] (ISOFORM 1). RC TISSUE=Fetal skeletal muscle; RX PubMed=2283997; DOI=10.1210/mend-4-10-1438; RA Nakai A., Kartha S., Sakurai A., Toback F.G., Degroot L.J.; RT "A human early response gene homologous to murine nur77 and rat NGFI-B, and RT related to the nuclear receptor superfamily."; RL Mol. Endocrinol. 4:1438-1443(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2626032; DOI=10.1016/0022-4731(89)90114-3; RA Chang C., Kokontis J., Liao S., Chang Y.; RT "Isolation and characterization of human TR3 receptor: a member of steroid RT receptor superfamily."; RL J. Steroid Biochem. 34:391-395(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Skeletal muscle; RA Ohkura N., Ito M., Tsukada T., Sasaki K., Yamaguchi K., Miki K.; RT "Identification of an isoform of human TR3 (NGFI-B, Nur77)."; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Kobayashi T., Kodani Y., Sawasaki T., Endo Y.; RT "Comprehensive DNA-binding analysis of human hormone nuclear receptors by RT fluorescence correlation spectroscopy based on cell-free system."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Heart; RA Kaighin V.A., Martin A.L., Aronstam R.S.; RT "Isolation of cDNA coding for multiple human nuclear receptor clones."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Brain, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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 [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-398 (ISOFORM 1), AND INDUCTION. RC TISSUE=Colon adenocarcinoma; RX PubMed=1651101; RA Bondy G.P.; RT "Phorbol ester, forskolin, and serum induction of a human colon nuclear RT hormone receptor gene related to the NUR 77/NGFI-B genes."; RL Cell Growth Differ. 2:203-208(1991). RN [13] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=8121493; DOI=10.1038/367277a0; RA Woronicz J.D., Calnan B., Ngo V., Winoto A.; RT "Requirement for the orphan steroid receptor Nur77 in apoptosis of T-cell RT hybridomas."; RL Nature 367:277-281(1994). RN [14] RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND INDUCTION. RX PubMed=9315652; DOI=10.1128/mcb.17.10.5946; RA Philips A., Lesage S., Gingras R., Maira M.H., Gauthier Y., Hugo P., RA Drouin J.; RT "Novel dimeric Nur77 signaling mechanism in endocrine and lymphoid cells."; RL Mol. Cell. Biol. 17:5946-5951(1997). RN [15] RP INTERACTION WITH RXRA, AND SUBCELLULAR LOCATION. RX PubMed=15509776; DOI=10.1128/mcb.24.22.9705-9725.2004; RA Cao X., Liu W., Lin F., Li H., Kolluri S.K., Lin B., Han Y.H., Dawson M.I., RA Zhang X.K.; RT "Retinoid X receptor regulates Nur77/TR3-dependent apoptosis [corrected] by RT modulating its nuclear export and mitochondrial targeting."; RL Mol. Cell. Biol. 24:9705-9725(2004). RN [16] RP FUNCTION. RX PubMed=15466594; DOI=10.1093/nar/gkh856; RA Harant H., Lindley I.J.; RT "Negative cross-talk between the human orphan nuclear receptor Nur77/NAK- RT 1/TR3 and nuclear factor-kappaB."; RL Nucleic Acids Res. 32:5280-5290(2004). RN [17] RP INTERACTION WITH GADD45GIP1. RX PubMed=15459248; DOI=10.1210/me.2004-0107; RA Park K.C., Song K.-H., Chung H.K., Kim H., Kim D.W., Song J.H., Hwang E.S., RA Jung H.S., Park S.-H., Bae I., Lee I.K., Choi H.-S., Shong M.; RT "CR6-interacting factor 1 interacts with orphan nuclear receptor Nur77 and RT inhibits its transactivation."; RL Mol. Endocrinol. 19:12-24(2005). RN [18] RP PHOSPHORYLATION AT SER-351. RX PubMed=17360704; DOI=10.1074/jbc.m700906200; RA Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J., RA Sonenberg N., Blenis J.; RT "RAS/ERK signaling promotes site-specific ribosomal protein S6 RT phosphorylation via RSK and stimulates cap-dependent translation."; RL J. Biol. Chem. 282:14056-14064(2007). RN [19] RP INTERACTION WITH RXRA, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP 1-MET--LYS-50 AND 299-ALA--PRO-361. RX PubMed=17761950; DOI=10.1210/me.2007-0107; RA Zhao W.X., Tian M., Zhao B.X., Li G.D., Liu B., Zhan Y.Y., Chen H.Z., RA Wu Q.; RT "Orphan receptor TR3 attenuates the p300-induced acetylation of retinoid X RT receptor-alpha."; RL Mol. Endocrinol. 21:2877-2889(2007). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [21] RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, INTERACTION WITH NCOA1; NCOA1 AND RP NCOA3, SUBCELLULAR LOCATION, INDUCTION, AND MUTAGENESIS OF TYR-453. RX PubMed=18690216; DOI=10.1038/nchembio.106; RA Zhan Y., Du X., Chen H., Liu J., Zhao B., Huang D., Li G., Xu Q., Zhang M., RA Weimer B.C., Chen D., Cheng Z., Zhang L., Li Q., Li S., Zheng Z., Song S., RA Huang Y., Ye Z., Su W., Lin S.C., Shen Y., Wu Q.; RT "Cytosporone B is an agonist for nuclear orphan receptor Nur77."; RL Nat. Chem. Biol. 4:548-556(2008). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [23] RP ACETYLATION, AND SUBCELLULAR LOCATION. RX PubMed=20438716; DOI=10.1016/j.bcp.2010.04.026; RA Kang S.A., Na H., Kang H.J., Kim S.H., Lee M.H., Lee M.O.; RT "Regulation of Nur77 protein turnover through acetylation and deacetylation RT induced by p300 and HDAC1."; RL Biochem. Pharmacol. 80:867-873(2010). RN [24] RP INTERACTION WITH IFI27, AND SUBCELLULAR LOCATION. RX PubMed=22427340; DOI=10.1161/circresaha.111.258814; RA Papac-Milicevic N., Breuss J.M., Zaujec J., Ryban L., Plyushch T., RA Wagner G.A., Fenzl S., Dremsek P., Cabaravdic M., Steiner M., Glass C.K., RA Binder C.J., Uhrin P., Binder B.R.; RT "The interferon stimulated gene 12 inactivates vasculoprotective functions RT of NR4A nuclear receptors."; RL Circ. Res. 110:E50-E63(2012). RN [25] RP DOMAIN NR LBD, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=37001519; DOI=10.1016/j.immuni.2023.03.003; RA Zhu F., Ma J., Li W., Liu Q., Qin X., Qian Y., Wang C., Zhang Y., Li Y., RA Jiang D., Wang S., Xia P.; RT "The orphan receptor Nur77 binds cytoplasmic LPS to activate the non- RT canonical NLRP3 inflammasome."; RL Immunity 56:753-767(2023). RN [26] {ECO:0007744|PDB:3V3E, ECO:0007744|PDB:3V3Q} RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 351-598 ALONE AND IN COMPLEX WITH RP ANTAGONIST, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STK11, AND RP MUTAGENESIS OF THR-595. RX PubMed=22983157; DOI=10.1038/nchembio.1069; RA Zhan Y.Y., Chen Y., Zhang Q., Zhuang J.J., Tian M., Chen H.Z., Zhang L.R., RA Zhang H.K., He J.P., Wang W.J., Wu R., Wang Y., Shi C., Yang K., Li A.Z., RA Xin Y.Z., Li T.Y., Yang J.Y., Zheng Z.H., Yu C.D., Lin S.C., Chang C., RA Huang P.Q., Lin T., Wu Q.; RT "The orphan nuclear receptor Nur77 regulates LKB1 localization and RT activates AMPK."; RL Nat. Chem. Biol. 8:897-904(2012). CC -!- FUNCTION: Orphan nuclear receptor. Binds the NGFI-B response element CC (NBRE) 5'-AAAGGTCA-3' (PubMed:18690216, PubMed:9315652, CC PubMed:8121493). Binds 9-cis-retinoic acid outside of its ligand- CC binding (NR LBD) domain (PubMed:18690216). Participates in energy CC homeostasis by sequestrating the kinase STK11 in the nucleus, thereby CC attenuating cytoplasmic AMPK activation (PubMed:22983157). Regulates CC the inflammatory response in macrophages by regulating metabolic CC adaptations during inflammation, including repressing the transcription CC of genes involved in the citric acid cycle (TCA) (By similarity). CC Inhibits NF-kappa-B signaling by binding to low-affinity NF-kappa-B CC binding sites, such as at the IL2 promoter (PubMed:15466594). May act CC concomitantly with NR4A2 in regulating the expression of delayed-early CC genes during liver regeneration (By similarity). Plays a role in the CC vascular response to injury (By similarity). CC {ECO:0000250|UniProtKB:P12813, ECO:0000250|UniProtKB:P22829, CC ECO:0000269|PubMed:15466594, ECO:0000269|PubMed:18690216, CC ECO:0000269|PubMed:22983157, ECO:0000269|PubMed:8121493, CC ECO:0000269|PubMed:9315652}. CC -!- FUNCTION: In the cytosol, upon its detection of both bacterial CC lipopolysaccharide (LPS) and NBRE-containing mitochondrial DNA released CC by GSDMD pores during pyroptosis, it promotes non-canonical NLRP3 CC inflammasome activation by stimulating association of NLRP3 and NEK7. CC {ECO:0000250|UniProtKB:P12813}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P22829}; CC Note=Binds 2 zinc ions. {ECO:0000250|UniProtKB:P22829}; CC -!- ACTIVITY REGULATION: Its transcription factor activity is activated by CC binding cytosporone B (Csn-B) via its ligand-binding (NR LBD) domain CC and stimulates recruitment of coactivators NCOA1 and NCOA2, but not CC NCOA3, to promoters (PubMed:18690216). Csn-B-binding is also CC accompanied by its translocation to the mitochondrion CC (PubMed:18690216). Its transcription factor activity is activated by CC corticotropin-releasing hormone (CRH) and forskolin (PubMed:9315652). CC Not activated by binding cytosporone C (Csn-C) (PubMed:18690216). CC {ECO:0000269|PubMed:18690216, ECO:0000269|PubMed:9315652}. CC -!- SUBUNIT: Binds the NGFI-B response element (NBRE) as a monomer CC (PubMed:18690216). Binds the Nur response element (NurRE), consisting CC of two inverse NBRE-related octanucleotide repeats separated by 6 base- CC pairs, as a dimer (PubMed:18690216, PubMed:9315652). Interacts (via N- CC terminus) with NLRP3 (via LRR repeat domain); the interaction is CC direct, requires binding of NR4A1/Nur77 to NBRE-containing dsDNA and CC lipopolysaccharide, and leads to non-canonical NLRP3 inflammasome CC activation (By similarity). Interacts with GADD45GIP1 CC (PubMed:15459248). Interacts with STK11 (PubMed:22983157). Interacts CC with IFI27 (PubMed:22427340). Heterodimer (via DNA-binding domain) with CC RXRA (via C-terminus); DNA-binding of the heterodimer is enhanced by 9- CC cis retinoic acid (PubMed:17761950, PubMed:15509776). Competes for the CC RXRA interaction with EP300 and thereby attenuates EP300 mediated CC acetylation of RXRA (PubMed:17761950). Interacts with NCOA1 CC (PubMed:18690216). Interacts with NCOA2 (PubMed:18690216). Interacts CC with NCOA3 (PubMed:18690216). {ECO:0000250|UniProtKB:P12813, CC ECO:0000250|UniProtKB:P22829, ECO:0000269|PubMed:15459248, CC ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:17761950, CC ECO:0000269|PubMed:22427340, ECO:0000269|PubMed:22983157}. CC -!- INTERACTION: CC P22736; Q9P2G1: ANKIB1; NbExp=2; IntAct=EBI-721550, EBI-2687890; CC P22736; P10415: BCL2; NbExp=7; IntAct=EBI-721550, EBI-77694; CC P22736; P55273: CDKN2D; NbExp=4; IntAct=EBI-721550, EBI-745859; CC P22736; O60888: CUTA; NbExp=2; IntAct=EBI-721550, EBI-1051556; CC P22736; P32189: GK; NbExp=3; IntAct=EBI-721550, EBI-3926629; CC P22736; P40305-2: IFI27; NbExp=8; IntAct=EBI-721550, EBI-27124263; CC P22736; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-721550, EBI-10172150; CC P22736; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-721550, EBI-2341787; CC P22736; P43243: MATR3; NbExp=2; IntAct=EBI-721550, EBI-352602; CC P22736; Q96JS3: PGBD1; NbExp=3; IntAct=EBI-721550, EBI-10290053; CC P22736; Q9Y4D7: PLXND1; NbExp=2; IntAct=EBI-721550, EBI-310731; CC P22736; Q99873: PRMT1; NbExp=6; IntAct=EBI-721550, EBI-78738; CC P22736; P40763: STAT3; NbExp=3; IntAct=EBI-721550, EBI-518675; CC P22736; P04637: TP53; NbExp=6; IntAct=EBI-721550, EBI-366083; CC P22736; P04350: TUBB4A; NbExp=2; IntAct=EBI-721550, EBI-355007; CC P22736; P50552: VASP; NbExp=2; IntAct=EBI-721550, EBI-748201; CC P22736; O14980: XPO1; NbExp=2; IntAct=EBI-721550, EBI-355867; CC P22736; P03120: E2; Xeno; NbExp=3; IntAct=EBI-721550, EBI-1779322; CC P22736; PRO_0000037545 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-721550, EBI-9028517; CC P22736-1; O60238: BNIP3L; NbExp=4; IntAct=EBI-16085263, EBI-849893; CC P22736-1; Q16539-1: MAPK14; NbExp=5; IntAct=EBI-16085263, EBI-15834191; CC P22736-1; Q04206: RELA; NbExp=3; IntAct=EBI-16085263, EBI-73886; CC P22736-1; P12235: SLC25A4; NbExp=2; IntAct=EBI-16085263, EBI-359074; CC P22736-2; Q96JS3: PGBD1; NbExp=3; IntAct=EBI-12697871, EBI-10290053; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15509776, CC ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:18690216, CC ECO:0000269|PubMed:20438716, ECO:0000269|PubMed:22427340, CC ECO:0000269|PubMed:22983157, ECO:0000269|PubMed:8121493}. Cytoplasm, CC cytosol {ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:20438716, CC ECO:0000269|PubMed:22427340}. Mitochondrion CC {ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:18690216}. CC Note=Nuclear export to the cytosol is XPO1-mediated and positively CC regulated by IFI27 (PubMed:22427340). Translocation to the CC mitochondrion upon interaction with RXRA and upon the presence of 9-cis CC retinoic acid (PubMed:17761950). {ECO:0000269|PubMed:17761950, CC ECO:0000269|PubMed:22427340}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P22736-1; Sequence=Displayed; CC Name=2; CC IsoId=P22736-2; Sequence=VSP_043086; CC Name=3; CC IsoId=P22736-3; Sequence=VSP_047769, VSP_047770; CC -!- TISSUE SPECIFICITY: Fetal muscle and adult liver, brain and thyroid. CC -!- INDUCTION: Induced by cytosporone B (Csn-B); directly stimulates its CC own expression (PubMed:18690216). Induced by corticotropin-releasing CC hormone (CRH) (PubMed:9315652). Induced by growth-stimulating agents CC (PubMed:1651101). {ECO:0000269|PubMed:1651101, CC ECO:0000269|PubMed:18690216, ECO:0000269|PubMed:9315652}. CC -!- DOMAIN: The NR LBD domain binds the lipid A moiety of CC lipopolysaccharide (LPS) in the cytosol. {ECO:0000269|PubMed:37001519}. CC -!- PTM: Phosphorylated at Ser-351 by RPS6KA1 and RPS6KA3 in response to CC mitogenic or stress stimuli. {ECO:0000269|PubMed:17360704}. CC -!- PTM: Acetylated by p300/CBP, acetylation increases stability. CC Deacetylated by HDAC1. {ECO:0000269|PubMed:20438716}. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR4 CC subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41573/NR4A1"; 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; D49728; BAA08565.1; -; mRNA. DR EMBL; L13740; AAA36763.1; -; mRNA. DR EMBL; D85245; BAA12746.1; -; mRNA. DR EMBL; AK297526; BAG59929.1; -; mRNA. DR EMBL; HQ692855; ADZ17366.1; -; mRNA. DR EMBL; AB307717; BAH02308.1; -; mRNA. DR EMBL; BT007144; AAP35808.1; -; mRNA. DR EMBL; AK314437; BAG37048.1; -; mRNA. DR EMBL; CR456704; CAG32985.1; -; mRNA. DR EMBL; AC025259; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471111; EAW58222.1; -; Genomic_DNA. DR EMBL; CH471111; EAW58224.1; -; Genomic_DNA. DR EMBL; CH471111; EAW58225.1; -; Genomic_DNA. DR EMBL; BC016147; AAH16147.1; -; mRNA. DR CCDS; CCDS55828.1; -. [P22736-2] DR CCDS; CCDS8818.1; -. [P22736-1] DR PIR; A37251; A37251. DR RefSeq; NP_001189162.1; NM_001202233.1. [P22736-2] DR RefSeq; NP_002126.2; NM_002135.4. [P22736-1] DR RefSeq; NP_775180.1; NM_173157.2. [P22736-1] DR RefSeq; XP_005268881.1; XM_005268824.3. [P22736-1] DR RefSeq; XP_006719426.1; XM_006719363.1. DR RefSeq; XP_006719427.1; XM_006719364.3. DR PDB; 2QW4; X-ray; 2.80 A; A/B/C/D=347-598. DR PDB; 3V3E; X-ray; 2.06 A; A/B=351-598. DR PDB; 3V3Q; X-ray; 2.22 A; A/B=351-598. DR PDB; 4JGV; X-ray; 3.01 A; A/B=351-598. DR PDB; 4KZI; X-ray; 2.41 A; A/B=351-598. DR PDB; 4KZJ; X-ray; 2.12 A; A/B=351-598. DR PDB; 4KZM; X-ray; 2.30 A; A/B=351-598. DR PDB; 4RE8; X-ray; 2.16 A; A/B=351-598. DR PDB; 4REE; X-ray; 2.37 A; A/B=351-598. DR PDB; 4REF; X-ray; 2.10 A; A/B=351-598. DR PDB; 4RZE; X-ray; 2.49 A; A/B=351-598. DR PDB; 4RZF; X-ray; 1.99 A; A/B=351-598. DR PDB; 4RZG; X-ray; 2.70 A; A/B=351-598. DR PDB; 4WHF; X-ray; 2.27 A; A/B=351-598. DR PDB; 4WHG; X-ray; 2.18 A; A/B=351-598. DR PDB; 6KZ5; X-ray; 4.45 A; A/B=351-598. DR PDB; 6LC1; X-ray; 3.12 A; A/D/G/J=265-351. DR PDBsum; 2QW4; -. DR PDBsum; 3V3E; -. DR PDBsum; 3V3Q; -. DR PDBsum; 4JGV; -. DR PDBsum; 4KZI; -. DR PDBsum; 4KZJ; -. DR PDBsum; 4KZM; -. DR PDBsum; 4RE8; -. DR PDBsum; 4REE; -. DR PDBsum; 4REF; -. DR PDBsum; 4RZE; -. DR PDBsum; 4RZF; -. DR PDBsum; 4RZG; -. DR PDBsum; 4WHF; -. DR PDBsum; 4WHG; -. DR PDBsum; 6KZ5; -. DR PDBsum; 6LC1; -. DR AlphaFoldDB; P22736; -. DR SMR; P22736; -. DR BioGRID; 109407; 206. DR DIP; DIP-40392N; -. DR IntAct; P22736; 113. DR MINT; P22736; -. DR STRING; 9606.ENSP00000440864; -. DR BindingDB; P22736; -. DR ChEMBL; CHEMBL1293229; -. DR MoonDB; P22736; Predicted. DR GlyGen; P22736; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P22736; -. DR PhosphoSitePlus; P22736; -. DR BioMuta; NR4A1; -. DR DMDM; 127819; -. DR EPD; P22736; -. DR jPOST; P22736; -. DR MassIVE; P22736; -. DR MaxQB; P22736; -. DR PaxDb; 9606-ENSP00000440864; -. DR PeptideAtlas; P22736; -. DR ProteomicsDB; 54032; -. [P22736-1] DR ProteomicsDB; 54033; -. [P22736-2] DR ProteomicsDB; 60662; -. DR Pumba; P22736; -. DR Antibodypedia; 14466; 815 antibodies from 45 providers. DR DNASU; 3164; -. DR Ensembl; ENST00000243050.5; ENSP00000243050.1; ENSG00000123358.20. [P22736-1] DR Ensembl; ENST00000360284.7; ENSP00000353427.3; ENSG00000123358.20. [P22736-2] DR Ensembl; ENST00000394824.2; ENSP00000378301.2; ENSG00000123358.20. [P22736-1] DR Ensembl; ENST00000394825.6; ENSP00000378302.1; ENSG00000123358.20. [P22736-1] DR Ensembl; ENST00000548232.1; ENSP00000449587.1; ENSG00000123358.20. [P22736-3] DR Ensembl; ENST00000550082.5; ENSP00000449539.1; ENSG00000123358.20. [P22736-2] DR GeneID; 3164; -. DR KEGG; hsa:3164; -. DR MANE-Select; ENST00000394825.6; ENSP00000378302.1; NM_173157.3; NP_775180.1. DR UCSC; uc001rzs.4; human. [P22736-1] DR AGR; HGNC:7980; -. DR CTD; 3164; -. DR DisGeNET; 3164; -. DR GeneCards; NR4A1; -. DR HGNC; HGNC:7980; NR4A1. DR HPA; ENSG00000123358; Low tissue specificity. DR MIM; 139139; gene. DR neXtProt; NX_P22736; -. DR OpenTargets; ENSG00000123358; -. DR PharmGKB; PA31761; -. DR VEuPathDB; HostDB:ENSG00000123358; -. DR eggNOG; KOG4217; Eukaryota. DR GeneTree; ENSGT00950000183038; -. DR HOGENOM; CLU_007368_14_2_1; -. DR InParanoid; P22736; -. DR OMA; MEVIRKW; -. DR OrthoDB; 5395768at2759; -. DR PhylomeDB; P22736; -. DR TreeFam; TF315430; -. DR PathwayCommons; P22736; -. DR Reactome; R-HSA-198693; AKT phosphorylates targets in the nucleus. DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway. DR Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer. DR SignaLink; P22736; -. DR SIGNOR; P22736; -. DR BioGRID-ORCS; 3164; 21 hits in 1181 CRISPR screens. DR ChiTaRS; NR4A1; human. DR EvolutionaryTrace; P22736; -. DR GeneWiki; Nerve_Growth_factor_IB; -. DR GenomeRNAi; 3164; -. DR Pharos; P22736; Tchem. DR PRO; PR:P22736; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P22736; Protein. DR Bgee; ENSG00000123358; Expressed in mucosa of stomach and 207 other cell types or tissues. DR ExpressionAtlas; P22736; baseline and differential. DR GO; GO:0000785; C:chromatin; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0098793; C:presynapse; IEA:GOC. DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; ISS:BHF-UCL. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0001530; F:lipopolysaccharide binding; ISS:UniProtKB. DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IBA:GO_Central. DR GO; GO:0004879; F:nuclear receptor activity; TAS:ProtInc. DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl. DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IDA:BHF-UCL. DR GO; GO:0071376; P:cellular response to corticotropin-releasing hormone stimulus; ISS:UniProtKB. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IMP:BHF-UCL. DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:BHF-UCL. DR GO; GO:0032497; P:detection of lipopolysaccharide; ISS:UniProtKB. DR GO; GO:0035767; P:endothelial cell chemotaxis; IMP:BHF-UCL. DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB. DR GO; GO:0014860; P:neurotransmitter secretion involved in regulation of skeletal muscle contraction; IEA:Ensembl. DR GO; GO:0160075; P:non-canonical inflammasome complex assembly; ISS:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; ISS:UniProtKB. DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl. DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl. DR CDD; cd06969; NR_DBD_NGFI-B; 1. DR CDD; cd07348; NR_LBD_NGFI-B; 1. DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1. DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1. DR InterPro; IPR035500; NHR-like_dom_sf. DR InterPro; IPR003071; NR4A1. DR InterPro; IPR003070; NR4A1-3. DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd. DR InterPro; IPR001723; Nuclear_hrmn_rcpt. DR InterPro; IPR001628; Znf_hrmn_rcpt. DR InterPro; IPR013088; Znf_NHR/GATA. DR PANTHER; PTHR24085; NUCLEAR HORMONE RECEPTOR; 1. DR PANTHER; PTHR24085:SF1; NUCLEAR RECEPTOR SUBFAMILY 4 GROUP A MEMBER 1; 1. DR Pfam; PF00104; Hormone_recep; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR01285; HMRNUCRECPTR. DR PRINTS; PR01284; NUCLEARECPTR. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1. DR PROSITE; PS51843; NR_LBD; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. DR Genevisible; P22736; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; DNA-binding; KW Inflammatory response; Metal-binding; Mitochondrion; Nucleus; KW Phosphoprotein; Receptor; Reference proteome; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..598 FT /note="Nuclear receptor subfamily 4immunitygroup A member FT 1" FT /id="PRO_0000053715" FT DOMAIN 360..595 FT /note="NR LBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189" FT DNA_BIND 264..339 FT /note="Nuclear receptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 267..287 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 303..327 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT REGION 1..44 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 131..158 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 171..466 FT /note="Required for nuclear import" FT /evidence="ECO:0000269|PubMed:15509776" FT REGION 177..206 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 221..265 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 268..354 FT /note="Required for binding NBRE-containing DNA" FT /evidence="ECO:0000250|UniProtKB:P12813" FT REGION 299..361 FT /note="Required for the interaction with RXRA" FT /evidence="ECO:0000269|PubMed:17761950" FT REGION 341..361 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 521..544 FT /note="Binds lipopolysaccharide" FT /evidence="ECO:0000250|UniProtKB:P12813" FT REGION 584..595 FT /note="AF-2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189" FT COMPBIAS 180..194 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 341 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000250|UniProtKB:P22829" FT MOD_RES 351 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17360704, FT ECO:0007744|PubMed:18669648" FT VAR_SEQ 1 FT /note="M -> MWLAKACWSIQSEM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043086" FT VAR_SEQ 293..325 FT /note="RTVQKNAKYICLANKDCPVDKRRRNRCQFCRFQ -> VPRSPRWGLLLEMER FT GWPHPIGTCGLPLGSPPS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3" FT /id="VSP_047769" FT VAR_SEQ 326..598 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3" FT /id="VSP_047770" FT VARIANT 26 FT /note="L -> V (in dbSNP:rs1882118)" FT /id="VAR_061534" FT MUTAGEN 1..50 FT /note="Missing: No impact on the interaction with RXRA." FT /evidence="ECO:0000269|PubMed:17761950" FT MUTAGEN 299..361 FT /note="Missing: Loss of interaction with RXRA." FT /evidence="ECO:0000269|PubMed:17761950" FT MUTAGEN 453 FT /note="Y->A: Abolishes binding to activity regulator FT Cytosporone B." FT /evidence="ECO:0000269|PubMed:18690216" FT MUTAGEN 595 FT /note="T->E: Strongly weakens interaction with STK11." FT /evidence="ECO:0000269|PubMed:22983157" FT CONFLICT 253 FT /note="T -> I (in Ref. 12)" FT /evidence="ECO:0000305" FT CONFLICT 262 FT /note="G -> P (in Ref. 2; AAA36763)" FT /evidence="ECO:0000305" FT CONFLICT 360 FT /note="S -> F (in Ref. 8; CAG32985)" FT /evidence="ECO:0000305" FT CONFLICT 370 FT /note="R -> L (in Ref. 2; AAA36763)" FT /evidence="ECO:0000305" FT TURN 268..270 FT /evidence="ECO:0007829|PDB:6LC1" FT STRAND 276..278 FT /evidence="ECO:0007829|PDB:6LC1" FT STRAND 281..283 FT /evidence="ECO:0007829|PDB:6LC1" FT HELIX 286..297 FT /evidence="ECO:0007829|PDB:6LC1" FT TURN 314..317 FT /evidence="ECO:0007829|PDB:6LC1" FT HELIX 320..329 FT /evidence="ECO:0007829|PDB:6LC1" FT HELIX 364..373 FT /evidence="ECO:0007829|PDB:4RZF" FT HELIX 379..381 FT /evidence="ECO:0007829|PDB:4RZF" FT STRAND 395..397 FT /evidence="ECO:0007829|PDB:4REF" FT HELIX 400..422 FT /evidence="ECO:0007829|PDB:4RZF" FT HELIX 427..429 FT /evidence="ECO:0007829|PDB:4RZF" FT HELIX 432..454 FT /evidence="ECO:0007829|PDB:4RZF" FT HELIX 457..459 FT /evidence="ECO:0007829|PDB:4RZF" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:4RZF" FT STRAND 467..471 FT /evidence="ECO:0007829|PDB:4RZF" FT HELIX 472..479 FT /evidence="ECO:0007829|PDB:4RZF" FT HELIX 482..495 FT /evidence="ECO:0007829|PDB:4RZF" FT HELIX 500..511 FT /evidence="ECO:0007829|PDB:4RZF" FT HELIX 521..541 FT /evidence="ECO:0007829|PDB:4RZF" FT TURN 544..546 FT /evidence="ECO:0007829|PDB:3V3Q" FT HELIX 550..556 FT /evidence="ECO:0007829|PDB:4RZF" FT HELIX 558..579 FT /evidence="ECO:0007829|PDB:4RZF" FT HELIX 586..594 FT /evidence="ECO:0007829|PDB:4RZF" SQ SEQUENCE 598 AA; 64463 MW; 41DAAEA7C25FDA22 CRC64; MPCIQAQYGT PAPSPGPRDH LASDPLTPEF IKPTMDLASP EAAPAAPTAL PSFSTFMDGY TGEFDTFLYQ LPGTVQPCSS ASSSASSTSS SSATSPASAS FKFEDFQVYG CYPGPLSGPV DEALSSSGSD YYGSPCSAPS PSTPSFQPPQ LSPWDGSFGH FSPSQTYEGL RAWTEQLPKA SGPPQPPAFF SFSPPTGPSP SLAQSPLKLF PSQATHQLGE GESYSMPTAF PGLAPTSPHL EGSGILDTPV TSTKARSGAP GGSEGRCAVC GDNASCQHYG VRTCEGCKGF FKRTVQKNAK YICLANKDCP VDKRRRNRCQ FCRFQKCLAV GMVKEVVRTD SLKGRRGRLP SKPKQPPDAS PANLLTSLVR AHLDSGPSTA KLDYSKFQEL VLPHFGKEDA GDVQQFYDLL SGSLEVIRKW AEKIPGFAEL SPADQDLLLE SAFLELFILR LAYRSKPGEG KLIFCSGLVL HRLQCARGFG DWIDSILAFS RSLHSLLVDV PAFACLSALV LITDRHGLQE PRRVEELQNR IASCLKEHVA AVAGEPQPAS CLSRLLGKLP ELRTLCTQGL QRIFYLKLED LVPPPPIIDK IFMDTLPF //