ID MX2_HUMAN Reviewed; 715 AA. AC P20592; B7Z5D3; D3DSI7; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 27-MAR-2024, entry version 195. DE RecName: Full=Interferon-induced GTP-binding protein Mx2; DE AltName: Full=Interferon-regulated resistance GTP-binding protein MxB; DE AltName: Full=Myxovirus resistance protein 2; DE AltName: Full=p78-related protein; GN Name=MX2; 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). RX PubMed=2481229; DOI=10.1128/mcb.9.11.5062-5072.1989; RA Aebi M., Faeh J., Hurt N., Samuel C.E., Thomis D., Bazzigher L., RA Pavlovic J., Haller O., Staeheli P.; RT "cDNA structures and regulation of two interferon-induced human Mx RT proteins."; RL Mol. Cell. Biol. 9:5062-5072(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 29-715 (ISOFORM 1). RX PubMed=2154602; DOI=10.1128/jvi.64.3.1171-1181.1990; RA Horisberger M.A., McMaster G.K., Zeller H., Wathelet M.G., Dellis J., RA Content J.; RT "Cloning and sequence analyses of cDNAs for interferon- and virus-induced RT human Mx proteins reveal that they contain putative guanine nucleotide- RT binding sites: functional study of the corresponding gene promoter."; RL J. Virol. 64:1171-1181(1990). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-131 AND THR-151. RX PubMed=15184662; DOI=10.1073/pnas.0403167101; RA King M.C., Raposo G., Lemmon M.A.; RT "Inhibition of nuclear import and cell-cycle progression by mutated forms RT of the dynamin-like GTPase MxB."; RL Proc. Natl. Acad. Sci. U.S.A. 101:8957-8962(2004). RN [8] RP REVIEW, AND INDUCTION. RX PubMed=18062906; DOI=10.1016/j.micinf.2007.09.010; RA Haller O., Stertz S., Kochs G.; RT "The Mx GTPase family of interferon-induced antiviral proteins."; RL Microbes Infect. 9:1636-1643(2007). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP REVIEW. RX PubMed=24139395; DOI=10.1016/j.chom.2013.10.002; RA Haller O.; RT "Dynamins are forever: MxB inhibits HIV-1."; RL Cell Host Microbe 14:371-373(2013). RN [11] RP FUNCTION IN HIV-1 RESTRICTION. RX PubMed=24055605; DOI=10.1016/j.chom.2013.08.015; RA Liu Z., Pan Q., Ding S., Qian J., Xu F., Zhou J., Cen S., Guo F., Liang C.; RT "The interferon-inducible MxB protein inhibits HIV-1 infection."; RL Cell Host Microbe 14:398-410(2013). RN [12] RP FUNCTION IN HIV-1 RESTRICTION. RX PubMed=24048477; DOI=10.1038/nature12542; RA Goujon C., Moncorge O., Bauby H., Doyle T., Ward C.C., Schaller T., Hue S., RA Barclay W.S., Schulz R., Malim M.H.; RT "Human MX2 is an interferon-induced post-entry inhibitor of HIV-1 RT infection."; RL Nature 502:559-562(2013). RN [13] RP FUNCTION IN HIV-1 RESTRICTION. RX PubMed=24121441; DOI=10.1038/nature12653; RA Kane M., Yadav S.S., Bitzegeio J., Kutluay S.B., Zang T., Wilson S.J., RA Schoggins J.W., Rice C.M., Yamashita M., Hatziioannou T., Bieniasz P.D.; RT "MX2 is an interferon-induced inhibitor of HIV-1 infection."; RL Nature 502:563-566(2013). CC -!- FUNCTION: Interferon-induced dynamin-like GTPase with potent antiviral CC activity against human immunodeficiency virus type 1 (HIV-1). Acts by CC targeting the viral capsid and affects the nuclear uptake and/or CC stability of the HIV-1 replication complex and the subsequent CC chromosomal integration of the proviral DNA. Exhibits antiviral CC activity also against simian immunodeficiency virus (SIV-mnd). May play CC a role in regulating nucleocytoplasmic transport and cell-cycle CC progression. {ECO:0000269|PubMed:15184662, ECO:0000269|PubMed:24048477, CC ECO:0000269|PubMed:24055605, ECO:0000269|PubMed:24121441}. CC -!- INTERACTION: CC P20592; Q8WXE1: ATRIP; NbExp=3; IntAct=EBI-10200618, EBI-747353; CC P20592; A2ABF9: EHMT2; NbExp=3; IntAct=EBI-10200618, EBI-10174566; CC P20592; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-10200618, EBI-744366; CC P20592; O75928: PIAS2; NbExp=3; IntAct=EBI-10200618, EBI-348555; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15184662}. Nucleus CC {ECO:0000269|PubMed:15184662}. Nucleus, nuclear pore complex CC {ECO:0000269|PubMed:15184662}. Note=Localization to nuclear pores CC requires GTP-binding. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P20592-1; Sequence=Displayed; CC Name=2; CC IsoId=P20592-2; Sequence=VSP_056443, VSP_056444, VSP_056445; CC -!- INDUCTION: By type I and type III interferons. CC {ECO:0000269|PubMed:18062906}. CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE- CC ProRule:PRU01055}. 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; M30818; AAA36338.1; -; mRNA. DR EMBL; M33883; AAA36459.1; -; mRNA. DR EMBL; AK298780; BAH12869.1; -; mRNA. DR EMBL; AL163285; CAB90555.1; -; Genomic_DNA. DR EMBL; AL773578; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471079; EAX09605.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09606.1; -; Genomic_DNA. DR EMBL; BC035293; AAH35293.1; -; mRNA. DR CCDS; CCDS13672.1; -. [P20592-1] DR PIR; B33481; B33481. DR RefSeq; NP_002454.1; NM_002463.1. [P20592-1] DR RefSeq; XP_005261040.1; XM_005260983.4. [P20592-1] DR RefSeq; XP_005261041.1; XM_005260984.1. [P20592-1] DR RefSeq; XP_011527873.1; XM_011529571.1. DR RefSeq; XP_011527874.1; XM_011529572.1. [P20592-1] DR PDB; 4WHJ; X-ray; 3.20 A; A/B=84-715. DR PDB; 4X0R; X-ray; 2.90 A; A/B=413-678. DR PDB; 5UOT; EM; 4.60 A; 0/1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=93-711. DR PDBsum; 4WHJ; -. DR PDBsum; 4X0R; -. DR PDBsum; 5UOT; -. DR AlphaFoldDB; P20592; -. DR EMDB; EMD-8577; -. DR SMR; P20592; -. DR BioGRID; 110685; 16. DR DIP; DIP-59212N; -. DR IntAct; P20592; 7. DR STRING; 9606.ENSP00000333657; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR iPTMnet; P20592; -. DR PhosphoSitePlus; P20592; -. DR SwissPalm; P20592; -. DR BioMuta; MX2; -. DR DMDM; 127571; -. DR EPD; P20592; -. DR jPOST; P20592; -. DR MassIVE; P20592; -. DR MaxQB; P20592; -. DR PaxDb; 9606-ENSP00000333657; -. DR PeptideAtlas; P20592; -. DR ProteomicsDB; 53765; -. [P20592-1] DR ProteomicsDB; 6679; -. DR Antibodypedia; 23558; 179 antibodies from 25 providers. DR DNASU; 4600; -. DR Ensembl; ENST00000330714.8; ENSP00000333657.3; ENSG00000183486.14. [P20592-1] DR Ensembl; ENST00000418103.2; ENSP00000410188.2; ENSG00000183486.14. [P20592-2] DR Ensembl; ENST00000435611.6; ENSP00000389256.2; ENSG00000183486.14. [P20592-1] DR Ensembl; ENST00000680862.1; ENSP00000506423.1; ENSG00000183486.14. [P20592-1] DR GeneID; 4600; -. DR KEGG; hsa:4600; -. DR MANE-Select; ENST00000330714.8; ENSP00000333657.3; NM_002463.2; NP_002454.1. DR UCSC; uc002yzf.2; human. [P20592-1] DR AGR; HGNC:7533; -. DR CTD; 4600; -. DR DisGeNET; 4600; -. DR GeneCards; MX2; -. DR HGNC; HGNC:7533; MX2. DR HPA; ENSG00000183486; Tissue enhanced (lymphoid). DR MIM; 147890; gene. DR neXtProt; NX_P20592; -. DR OpenTargets; ENSG00000183486; -. DR PharmGKB; PA31334; -. DR VEuPathDB; HostDB:ENSG00000183486; -. DR eggNOG; KOG0446; Eukaryota. DR GeneTree; ENSGT00940000163266; -. DR HOGENOM; CLU_008964_8_0_1; -. DR InParanoid; P20592; -. DR OMA; KSYFQIA; -. DR OrthoDB; 1052588at2759; -. DR PhylomeDB; P20592; -. DR TreeFam; TF331484; -. DR PathwayCommons; P20592; -. DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR SignaLink; P20592; -. DR BioGRID-ORCS; 4600; 9 hits in 1159 CRISPR screens. DR ChiTaRS; MX2; human. DR GeneWiki; MX2; -. DR GenomeRNAi; 4600; -. DR Pharos; P20592; Tbio. DR PRO; PR:P20592; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; P20592; Protein. DR Bgee; ENSG00000183486; Expressed in blood and 147 other cell types or tissues. DR ExpressionAtlas; P20592; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; IBA:GO_Central. DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IMP:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0006952; P:defense response; TAS:ProtInc. DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB. DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:UniProtKB. DR GO; GO:0035455; P:response to interferon-alpha; IDA:UniProtKB. DR GO; GO:0009615; P:response to virus; IDA:UniProtKB. DR CDD; cd08771; DLP_1; 1. DR Gene3D; 1.20.120.1240; Dynamin, middle domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR022812; Dynamin. DR InterPro; IPR001401; Dynamin_GTPase. DR InterPro; IPR019762; Dynamin_GTPase_CS. DR InterPro; IPR045063; Dynamin_N. DR InterPro; IPR000375; Dynamin_stalk. DR InterPro; IPR030381; G_DYNAMIN_dom. DR InterPro; IPR003130; GED. DR InterPro; IPR020850; GED_dom. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11566; DYNAMIN; 1. DR PANTHER; PTHR11566:SF46; INTERFERON-INDUCED GTP-BINDING PROTEIN MX2; 1. DR Pfam; PF01031; Dynamin_M; 1. DR Pfam; PF00350; Dynamin_N; 1. DR Pfam; PF02212; GED; 1. DR PRINTS; PR00195; DYNAMIN. DR SMART; SM00053; DYNc; 1. DR SMART; SM00302; GED; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00410; G_DYNAMIN_1; 1. DR PROSITE; PS51718; G_DYNAMIN_2; 1. DR PROSITE; PS51388; GED; 1. DR Genevisible; P20592; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Antiviral defense; Cytoplasm; KW GTP-binding; Immunity; Innate immunity; mRNA transport; KW Nuclear pore complex; Nucleotide-binding; Nucleus; Protein transport; KW Reference proteome; Translocation; Transport. FT CHAIN 1..715 FT /note="Interferon-induced GTP-binding protein Mx2" FT /id="PRO_0000206598" FT DOMAIN 115..387 FT /note="Dynamin-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT DOMAIN 623..714 FT /note="GED" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720" FT REGION 125..132 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 150..152 FT /note="G2 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 225..228 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 294..297 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 326..329 FT /note="G5 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT BINDING 125..132 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT BINDING 225..229 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT BINDING 294..297 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT VAR_SEQ 148..192 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056443" FT VAR_SEQ 245..246 FT /note="IK -> VS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056444" FT VAR_SEQ 247..715 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056445" FT MUTAGEN 131 FT /note="K->A: Loss of GTP-binding and localization to FT nuclear pore. Disruption of nuclear import." FT /evidence="ECO:0000269|PubMed:15184662" FT MUTAGEN 151 FT /note="T->A: Defective GTP-hydrolysis. Disruption of FT nuclear import and cell-cycle progression." FT /evidence="ECO:0000269|PubMed:15184662" FT HELIX 94..109 FT /evidence="ECO:0007829|PDB:4WHJ" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:4WHJ" FT HELIX 131..139 FT /evidence="ECO:0007829|PDB:4WHJ" FT STRAND 155..160 FT /evidence="ECO:0007829|PDB:4WHJ" FT STRAND 167..172 FT /evidence="ECO:0007829|PDB:4WHJ" FT TURN 173..175 FT /evidence="ECO:0007829|PDB:4WHJ" FT STRAND 176..179 FT /evidence="ECO:0007829|PDB:4WHJ" FT HELIX 183..198 FT /evidence="ECO:0007829|PDB:4WHJ" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:4WHJ" FT STRAND 209..214 FT /evidence="ECO:0007829|PDB:4WHJ" FT STRAND 220..225 FT /evidence="ECO:0007829|PDB:4WHJ" FT HELIX 242..253 FT /evidence="ECO:0007829|PDB:4WHJ" FT STRAND 258..265 FT /evidence="ECO:0007829|PDB:4WHJ" FT HELIX 270..272 FT /evidence="ECO:0007829|PDB:4WHJ" FT HELIX 274..282 FT /evidence="ECO:0007829|PDB:4WHJ" FT STRAND 287..294 FT /evidence="ECO:0007829|PDB:4WHJ" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:4WHJ" FT HELIX 302..312 FT /evidence="ECO:0007829|PDB:4WHJ" FT STRAND 322..324 FT /evidence="ECO:0007829|PDB:4WHJ" FT HELIX 339..352 FT /evidence="ECO:0007829|PDB:4WHJ" FT HELIX 356..361 FT /evidence="ECO:0007829|PDB:4WHJ" FT STRAND 362..364 FT /evidence="ECO:0007829|PDB:4WHJ" FT HELIX 370..406 FT /evidence="ECO:0007829|PDB:4WHJ" FT TURN 413..415 FT /evidence="ECO:0007829|PDB:4WHJ" FT HELIX 418..421 FT /evidence="ECO:0007829|PDB:4X0R" FT HELIX 422..438 FT /evidence="ECO:0007829|PDB:4X0R" FT HELIX 450..487 FT /evidence="ECO:0007829|PDB:4X0R" FT HELIX 500..539 FT /evidence="ECO:0007829|PDB:4X0R" FT HELIX 543..579 FT /evidence="ECO:0007829|PDB:4X0R" FT HELIX 623..653 FT /evidence="ECO:0007829|PDB:4X0R" FT HELIX 655..668 FT /evidence="ECO:0007829|PDB:4X0R" FT HELIX 672..677 FT /evidence="ECO:0007829|PDB:4X0R" FT HELIX 685..710 FT /evidence="ECO:0007829|PDB:4WHJ" SQ SEQUENCE 715 AA; 82089 MW; 1AE4B80157545344 CRC64; MSKAHKPWPY RRRSQFSSRK YLKKEMNSFQ QQPPPFGTVP PQMMFPPNWQ GAEKDAAFLA KDFNFLTLNN QPPPGNRSQP RAMGPENNLY SQYEQKVRPC IDLIDSLRAL GVEQDLALPA IAVIGDQSSG KSSVLEALSG VALPRGSGIV TRCPLVLKLK KQPCEAWAGR ISYRNTELEL QDPGQVEKEI HKAQNVMAGN GRGISHELIS LEITSPEVPD LTIIDLPGIT RVAVDNQPRD IGLQIKALIK KYIQRQQTIN LVVVPCNVDI ATTEALSMAH EVDPEGDRTI GILTKPDLMD RGTEKSVMNV VRNLTYPLKK GYMIVKCRGQ QEITNRLSLA EATKKEITFF QTHPYFRVLL EEGSATVPRL AERLTTELIM HIQKSLPLLE GQIRESHQKA TEELRRCGAD IPSQEADKMF FLIEKIKMFN QDIEKLVEGE EVVRENETRL YNKIREDFKN WVGILATNTQ KVKNIIHEEV EKYEKQYRGK ELLGFVNYKT FEIIVHQYIQ QLVEPALSML QKAMEIIQQA FINVAKKHFG EFFNLNQTVQ STIEDIKVKH TAKAENMIQL QFRMEQMVFC QDQIYSVVLK KVREEIFNPL GTPSQNMKLN SHFPSNESSV SSFTEIGIHL NAYFLETSKR LANQIPFIIQ YFMLRENGDS LQKAMMQILQ EKNRYSWLLQ EQSETATKRR ILKERIYRLT QARHALCQFS SKEIH //