MX2_HUMAN
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 03-AUG-2022, entry version 186.
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}.
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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. [P20592-1]
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 SMR; P20592; -.
DR BioGRID; 110685; 13.
DR DIP; DIP-59212N; -.
DR IntAct; P20592; 6.
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; P20592; -.
DR PeptideAtlas; P20592; -.
DR PRIDE; P20592; -.
DR ProteomicsDB; 53765; -. [P20592-1]
DR ProteomicsDB; 6679; -.
DR Antibodypedia; 23558; 145 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 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; EYISEWH; -.
DR OrthoDB; 494748at2759; -.
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; 8 hits in 1080 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 146 other tissues.
DR ExpressionAtlas; P20592; baseline and differential.
DR Genevisible; P20592; HS.
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; 3.40.50.300; -; 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; PTHR11566; 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; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
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
