MX1_HUMAN
ID MX1_HUMAN Reviewed; 662 AA.
AC P20591; B2RDA5; B3KU10; C9IYV7; C9J8D6; C9JN19; C9JN88; C9JUL1; C9JZS6;
AC D3DSI8; Q86YP5; Q96CI3;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 4.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Interferon-induced GTP-binding protein Mx1;
DE AltName: Full=Interferon-induced protein p78;
DE Short=IFI-78K;
DE AltName: Full=Interferon-regulated resistance GTP-binding protein MxA;
DE AltName: Full=Myxoma resistance protein 1;
DE AltName: Full=Myxovirus resistance protein 1;
DE Contains:
DE RecName: Full=Interferon-induced GTP-binding protein Mx1, N-terminally processed;
GN Name=MX1;
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), AND VARIANT ILE-379.
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 [MRNA] (ISOFORM 1), AND VARIANT ILE-379.
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-379, AND POSSIBLE
RP INVOLVEMENT IN ALLOPECIA AREATA.
RX PubMed=10942113; DOI=10.1007/s004390000318;
RA Tazi-Ahnini R., di Giovine F.S., McDonagh A.J., Messenger A.G., Amadou C.,
RA Cox A., Duff G.W., Cork M.J.;
RT "Structure and polymorphism of the human gene for the interferon-induced
RT p78 protein (MX1): evidence of association with alopecia areata in the Down
RT syndrome region.";
RL Hum. Genet. 106:639-645(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORMS 1 AND 2),
RP SUBCELLULAR LOCATION (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX PubMed=20603636; DOI=10.1038/icb.2010.83;
RA Ku C.C., Che X.B., Reichelt M., Rajamani J., Schaap-Nutt A., Huang K.J.,
RA Sommer M.H., Chen Y.S., Chen Y.Y., Arvin A.M.;
RT "Herpes simplex virus-1 induces expression of a novel MxA isoform that
RT enhances viral replication.";
RL Immunol. Cell Biol. 89:173-182(2011).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-379.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-379.
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-379.
RC TISSUE=B-cell, and Uterus;
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 [9]
RP PROTEIN SEQUENCE OF 1-10; 84-97 AND 442-481, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Prostatic carcinoma;
RA Bienvenut W.V., Gao M., Leug H.;
RL Submitted (JUL-2009) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 2-57, AND NUCLEOTIDE SEQUENCE OF 2-124.
RA Horisberger M.A., Hochkeppel H.K., Content J.;
RT "Interferon-induced human protein in pure form, monoclonal antibodies
RT thereto, and test kits containing these antibodies.";
RL Patent number EP0242329, 21-OCT-1987.
RN [11]
RP PROTEIN SEQUENCE OF 2-26.
RX PubMed=2607176; DOI=10.1089/jir.1989.9.679;
RA Weitz G., Bekisz J., Zoon K., Arnheiter H.;
RT "Purification and characterization of a human Mx protein.";
RL J. Interferon Res. 9:679-689(1989).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 486-569.
RA Narayan K., Pachner A.R.;
RT "Inf-induced gene expression analysis in MS patients: Loss of
RT bioavailability can be caused by either binding or neutralizing
RT antibodies.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP RESISTANCE TO INFLUENZA VIRUS AND VSV.
RX PubMed=2161946; DOI=10.1128/jvi.64.7.3370-3375.1990;
RA Pavlovic J., Zuercher T., Haller O., Staeheli P.;
RT "Resistance to influenza virus and vesicular stomatitis virus conferred by
RT expression of human MxA protein.";
RL J. Virol. 64:3370-3375(1990).
RN [14]
RP MUTAGENESIS OF SER-81 AND LYS-83.
RX PubMed=8411374; DOI=10.1128/jvi.67.11.6726-6732.1993;
RA Pitossi F., Blank A., Schroeder A., Schwarz A., Huessi P., Schwemmle M.,
RA Pavlovic J., Staeheli P.;
RT "A functional GTP-binding motif is necessary for antiviral activity of Mx
RT proteins.";
RL J. Virol. 67:6726-6732(1993).
RN [15]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-103.
RX PubMed=9060610; DOI=10.1128/jvi.71.4.2591-2599.1997;
RA Ponten A., Sick C., Weeber M., Haller O., Kochs G.;
RT "Dominant-negative mutants of human MxA protein: domains in the carboxy-
RT terminal moiety are important for oligomerization and antiviral activity.";
RL J. Virol. 71:2591-2599(1997).
RN [16]
RP INTERACTION WITH THOV NUCLEOPROTEIN.
RX PubMed=9933640; DOI=10.1074/jbc.274.7.4370;
RA Kochs G., Haller O.;
RT "GTP-bound human MxA protein interacts with the nucleocapsids of Thogoto
RT virus (Orthomyxoviridae).";
RL J. Biol. Chem. 274:4370-4376(1999).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LACV PROTEIN N, AND
RP MUTAGENESIS OF GLU-645.
RX PubMed=11880649; DOI=10.1073/pnas.052430399;
RA Kochs G., Janzen C., Hohenberg H., Haller O.;
RT "Antivirally active MxA protein sequesters La Crosse virus nucleocapsid
RT protein into perinuclear complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:3153-3158(2002).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCHFV PROTEIN N, AND
RP MUTAGENESIS OF GLU-645.
RX PubMed=15047845; DOI=10.1128/jvi.78.8.4323-4329.2004;
RA Andersson I., Bladh L., Mousavi-Jazi M., Magnusson K.E., Lundkvist A.,
RA Haller O., Mirazimi A.;
RT "Human MxA protein inhibits the replication of Crimean-Congo hemorrhagic
RT fever virus.";
RL J. Virol. 78:4323-4329(2004).
RN [19]
RP FUNCTION.
RX PubMed=14752052; DOI=10.1093/nar/gkh192;
RA Turan K., Mibayashi M., Sugiyama K., Saito S., Numajiri A., Nagata K.;
RT "Nuclear MxA proteins form a complex with influenza virus NP and inhibit
RT the transcription of the engineered influenza virus genome.";
RL Nucleic Acids Res. 32:643-652(2004).
RN [20]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15355513; DOI=10.1111/j.1600-0854.2004.00219.x;
RA Reichelt M., Stertz S., Krijnse-Locker J., Haller O., Kochs G.;
RT "Missorting of LaCrosse virus nucleocapsid protein by the interferon-
RT induced MxA GTPase involves smooth ER membranes.";
RL Traffic 5:772-784(2004).
RN [21]
RP FUNCTION.
RX PubMed=14687945; DOI=10.1016/j.virusres.2003.10.002;
RA Bridgen A., Dalrymple D.A., Weber F., Elliott R.M.;
RT "Inhibition of Dugbe nairovirus replication by human MxA protein.";
RL Virus Res. 99:47-50(2004).
RN [22]
RP FUNCTION, INTERACTION WITH TRPC1; TRPC3; TRPC4; TRPC5; TRPC6 AND TRPC7, AND
RP MUTAGENESIS OF LYS-83; THR-103 AND LEU-612.
RX PubMed=15757897; DOI=10.1074/jbc.m500391200;
RA Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N.,
RA St-Hilaire M., Pinard M., Boulay G.;
RT "MxA, a member of the dynamin superfamily, interacts with the ankyrin-like
RT repeat domain of TRPC.";
RL J. Biol. Chem. 280:19393-19400(2005).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, OLIGOMERIZATION, AND INTERACTION WITH LACV
RP PROTEIN N.
RX PubMed=16413306; DOI=10.1016/s0076-6879(05)04055-3;
RA Kochs G., Reichelt M., Danino D., Hinshaw J.E., Haller O.;
RT "Assay and functional analysis of dynamin-like Mx proteins.";
RL Methods Enzymol. 404:632-643(2005).
RN [24]
RP ISGYLATION.
RX PubMed=16009940; DOI=10.1073/pnas.0504754102;
RA Zhao C., Denison C., Huibregtse J.M., Gygi S.P., Krug R.M.;
RT "Human ISG15 conjugation targets both IFN-induced and constitutively
RT expressed proteins functioning in diverse cellular pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10200-10205(2005).
RN [25]
RP SUBCELLULAR LOCATION.
RX PubMed=16978069; DOI=10.1089/jir.2006.26.650;
RA Stertz S., Reichelt M., Krijnse-Locker J., Mackenzie J., Simpson J.C.,
RA Haller O., Kochs G.;
RT "Interferon-induced, antiviral human MxA protein localizes to a distinct
RT subcompartment of the smooth endoplasmic reticulum.";
RL J. Interferon Cytokine Res. 26:650-660(2006).
RN [26]
RP FUNCTION.
RX PubMed=16202617; DOI=10.1016/j.nbd.2005.08.015;
RA Leroy M., Pire G., Baise E., Desmecht D.;
RT "Expression of the interferon-alpha/beta-inducible bovine Mx1 dynamin
RT interferes with replication of rabies virus.";
RL Neurobiol. Dis. 21:515-521(2006).
RN [27]
RP FUNCTION.
RX PubMed=17374778; DOI=10.1099/vir.0.82526-0;
RA Mundt E.;
RT "Human MxA protein confers resistance to double-stranded RNA viruses of two
RT virus families.";
RL J. Gen. Virol. 88:1319-1323(2007).
RN [28]
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 [29]
RP FUNCTION.
RX PubMed=18668195; DOI=10.1007/s00705-008-0168-9;
RA Yu Z., Wang Z., Chen J., Li H., Lin Z., Zhang F., Zhou Y., Hou J.;
RT "GTPase activity is not essential for the interferon-inducible MxA protein
RT to inhibit the replication of hepatitis B virus.";
RL Arch. Virol. 153:1677-1684(2008).
RN [30]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19109387; DOI=10.1128/jvi.00781-08;
RA Netherton C.L., Simpson J., Haller O., Wileman T.E., Takamatsu H.H.,
RA Monaghan P., Taylor G.;
RT "Inhibition of a large double-stranded DNA virus by MxA protein.";
RL J. Virol. 83:2310-2320(2009).
RN [31]
RP REVIEW ON STRUCTURE, DOMAIN GED, AND DOMAIN MIDDLE.
RX PubMed=20538602; DOI=10.1074/jbc.r110.145839;
RA Haller O., Gao S., von der Malsburg A., Daumke O., Kochs G.;
RT "Dynamin-like MxA GTPase: structural insights into oligomerization and
RT implications for antiviral activity.";
RL J. Biol. Chem. 285:28419-28424(2010).
RN [32]
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 [33]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH DDX39A AND DDX39B.
RX PubMed=21859714; DOI=10.1074/jbc.m111.251843;
RA Wisskirchen C., Ludersdorfer T.H., Mueller D.A., Moritz E., Pavlovic J.;
RT "Interferon-induced antiviral protein MxA interacts with the cellular RNA
RT helicases UAP56 and URH49.";
RL J. Biol. Chem. 286:34743-34751(2011).
RN [34]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-554;
RP LYS-555; LYS-556 AND LYS-557.
RX PubMed=21900240; DOI=10.1074/jbc.m111.249037;
RA von der Malsburg A., Abutbul-Ionita I., Haller O., Kochs G., Danino D.;
RT "Stalk domain of the dynamin-like MxA GTPase protein mediates membrane
RT binding and liposome tubulation via the unstructured L4 loop.";
RL J. Biol. Chem. 286:37858-37865(2011).
RN [35]
RP REVIEW.
RX PubMed=21166595; DOI=10.1089/jir.2010.0076;
RA Haller O., Kochs G.;
RT "Human MxA protein: an interferon-induced dynamin-like GTPase with broad
RT antiviral activity.";
RL J. Interferon Cytokine Res. 31:79-87(2011).
RN [36]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HSPA5.
RX PubMed=21992152; DOI=10.1089/jir.2010.0132;
RA Numajiri Haruki A., Naito T., Nishie T., Saito S., Nagata K.;
RT "Interferon-inducible antiviral protein MxA enhances cell death triggered
RT by endoplasmic reticulum stress.";
RL J. Interferon Cytokine Res. 31:847-856(2011).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 366-636, AND SUBUNIT.
RX PubMed=20428112; DOI=10.1038/nature08972;
RA Gao S., von der Malsburg A., Paeschke S., Behlke J., Haller O., Kochs G.,
RA Daumke O.;
RT "Structural basis of oligomerization in the stalk region of dynamin-like
RT MxA.";
RL Nature 465:502-506(2010).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 33-662, SUBUNIT, AND MUTAGENESIS
RP OF GLU-632 AND ARG-640.
RX PubMed=21962493; DOI=10.1016/j.immuni.2011.07.012;
RA Gao S., von der Malsburg A., Dick A., Faelber K., Schroder G.F., Haller O.,
RA Kochs G., Daumke O.;
RT "Structure of myxovirus resistance protein a reveals intra- and
RT intermolecular domain interactions required for the antiviral function.";
RL Immunity 35:514-525(2011).
CC -!- FUNCTION: Interferon-induced dynamin-like GTPase with antiviral
CC activity against a wide range of RNA viruses and some DNA viruses. Its
CC target viruses include negative-stranded RNA viruses and HBV through
CC binding and inactivation of their ribonucleocapsid. May also antagonize
CC reoviridae and asfarviridae replication. Inhibits thogoto virus (THOV)
CC replication by preventing the nuclear import of viral nucleocapsids.
CC Inhibits La Crosse virus (LACV) replication by sequestering viral
CC nucleoprotein in perinuclear complexes, preventing genome
CC amplification, budding, and egress. Inhibits influenza A virus (IAV)
CC replication by decreasing or delaying NP synthesis and by blocking
CC endocytic traffic of incoming virus particles. Enhances ER stress-
CC mediated cell death after influenza virus infection. May regulate the
CC calcium channel activity of TRPCs. {ECO:0000269|PubMed:11880649,
CC ECO:0000269|PubMed:14687945, ECO:0000269|PubMed:14752052,
CC ECO:0000269|PubMed:15047845, ECO:0000269|PubMed:15355513,
CC ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:16202617,
CC ECO:0000269|PubMed:16413306, ECO:0000269|PubMed:17374778,
CC ECO:0000269|PubMed:18668195, ECO:0000269|PubMed:19109387,
CC ECO:0000269|PubMed:21900240, ECO:0000269|PubMed:21992152}.
CC -!- SUBUNIT: Homotetramer. Oligomerizes into multimeric filamentous or
CC ring-like structures by virtue of its stalk domain. Oligomerization is
CC critical for GTPase activity, protein stability, and recognition of
CC viral target structures. Interacts with TRPC1, TRPC3, TRPC4, TRPC5,
CC TRPC6 and TRPC7. Interacts with HSPA5. Interacts with DDX39A and
CC DDX39B. Interacts with TUBB/TUBB5 (By similarity). The GTP-bound form
CC interacts (via C-terminus) with THOV P5 protein. The GTP-bound form
CC interacts with LACV protein N. Interacts with CCHFV protein N.
CC {ECO:0000250, ECO:0000269|PubMed:11880649, ECO:0000269|PubMed:15047845,
CC ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:16413306,
CC ECO:0000269|PubMed:20428112, ECO:0000269|PubMed:21859714,
CC ECO:0000269|PubMed:21900240, ECO:0000269|PubMed:21962493,
CC ECO:0000269|PubMed:21992152, ECO:0000269|PubMed:9933640}.
CC -!- INTERACTION:
CC P20591; Q9H9S4: CAB39L; NbExp=3; IntAct=EBI-929476, EBI-1047244;
CC P20591; Q08380: LGALS3BP; NbExp=2; IntAct=EBI-929476, EBI-354956;
CC P20591; P59942: MCCD1; NbExp=6; IntAct=EBI-929476, EBI-11987923;
CC P20591; P20591: MX1; NbExp=13; IntAct=EBI-929476, EBI-929476;
CC P20591; O75928-2: PIAS2; NbExp=3; IntAct=EBI-929476, EBI-348567;
CC P20591; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-929476, EBI-747107;
CC P20591; Q13507: TRPC3; NbExp=2; IntAct=EBI-929476, EBI-520807;
CC P20591; Q9UBN4: TRPC4; NbExp=2; IntAct=EBI-929476, EBI-929504;
CC P20591; Q9Y210: TRPC6; NbExp=4; IntAct=EBI-929476, EBI-929362;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11880649,
CC ECO:0000269|PubMed:21859714, ECO:0000269|PubMed:21992152,
CC ECO:0000269|PubMed:9060610}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15355513, ECO:0000269|PubMed:16413306,
CC ECO:0000269|PubMed:21992152}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16413306}; Cytoplasmic side. Cytoplasm, perinuclear
CC region {ECO:0000269|PubMed:15047845}. Note=Binds preferentially to
CC negatively charged phospholipids (PubMed:21900240). Colocalizes with
CC CCHFV protein N in the perinuclear region (PubMed:15047845).
CC {ECO:0000269|PubMed:15047845, ECO:0000269|PubMed:21900240}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:20603636}. Nucleus {ECO:0000269|PubMed:20603636}.
CC Note=Translocates into the nuclei of HSV-1 infected cells
CC (PubMed:20603636). {ECO:0000269|PubMed:20603636}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P20591-1; Sequence=Displayed;
CC Name=2; Synonyms=56-kda, varMxA;
CC IsoId=P20591-2; Sequence=VSP_042904;
CC -!- INDUCTION: By type I and type III interferons. Isoform 2 is induced by
CC HSV-1. {ECO:0000269|PubMed:18062906}.
CC -!- DOMAIN: The C-terminal GTPase effector domain (GED) is involved in
CC oligomerization and viral target recognition.
CC {ECO:0000269|PubMed:20538602}.
CC -!- DOMAIN: The middle domain mediates self-assembly and oligomerization.
CC {ECO:0000269|PubMed:20538602}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16009940}.
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; M30817; AAA36337.1; -; mRNA.
DR EMBL; M33882; AAA36458.1; -; mRNA.
DR EMBL; AF135187; AAD43063.1; -; Genomic_DNA.
DR EMBL; AK096355; BAG53272.1; -; mRNA.
DR EMBL; AK315465; BAG37852.1; -; mRNA.
DR EMBL; AL163285; CAB90556.1; -; Genomic_DNA.
DR EMBL; AL773577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL773578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09600.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09601.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09602.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09603.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09604.1; -; Genomic_DNA.
DR EMBL; BC014222; AAH14222.2; -; mRNA.
DR EMBL; BC032602; AAH32602.1; -; mRNA.
DR EMBL; AY186254; AAO31807.1; -; mRNA.
DR CCDS; CCDS13673.1; -. [P20591-1]
DR CCDS; CCDS74796.1; -. [P20591-2]
DR PIR; A33481; A33481.
DR RefSeq; NP_001138397.1; NM_001144925.2. [P20591-1]
DR RefSeq; NP_001171517.1; NM_001178046.2. [P20591-1]
DR RefSeq; NP_001269849.1; NM_001282920.1. [P20591-2]
DR RefSeq; NP_002453.2; NM_002462.4. [P20591-1]
DR RefSeq; XP_005261035.1; XM_005260978.4. [P20591-1]
DR RefSeq; XP_005261036.1; XM_005260979.2. [P20591-1]
DR RefSeq; XP_005261037.1; XM_005260980.2. [P20591-1]
DR RefSeq; XP_005261038.1; XM_005260981.2. [P20591-1]
DR RefSeq; XP_005261039.1; XM_005260982.2. [P20591-1]
DR RefSeq; XP_011527870.1; XM_011529568.2. [P20591-1]
DR RefSeq; XP_016883838.1; XM_017028349.1. [P20591-1]
DR RefSeq; XP_016883839.1; XM_017028350.1. [P20591-1]
DR PDB; 3LJB; X-ray; 2.40 A; A/B=366-636.
DR PDB; 3SZR; X-ray; 3.50 A; A=33-662.
DR PDB; 3ZYS; EM; 12.20 A; B/E=1-662.
DR PDB; 4P4S; X-ray; 3.30 A; A=70-342, B=43-662.
DR PDB; 4P4T; X-ray; 2.30 A; A=37-366, A=637-662.
DR PDB; 4P4U; X-ray; 1.90 A; A=37-364, A=632-661.
DR PDB; 5GTM; X-ray; 2.90 A; A/B=33-662.
DR PDBsum; 3LJB; -.
DR PDBsum; 3SZR; -.
DR PDBsum; 3ZYS; -.
DR PDBsum; 4P4S; -.
DR PDBsum; 4P4T; -.
DR PDBsum; 4P4U; -.
DR PDBsum; 5GTM; -.
DR AlphaFoldDB; P20591; -.
DR SMR; P20591; -.
DR BioGRID; 110684; 54.
DR DIP; DIP-35694N; -.
DR IntAct; P20591; 23.
DR MINT; P20591; -.
DR STRING; 9606.ENSP00000381601; -.
DR iPTMnet; P20591; -.
DR PhosphoSitePlus; P20591; -.
DR SwissPalm; P20591; -.
DR BioMuta; MX1; -.
DR DMDM; 251757499; -.
DR EPD; P20591; -.
DR jPOST; P20591; -.
DR MassIVE; P20591; -.
DR MaxQB; P20591; -.
DR PaxDb; P20591; -.
DR PeptideAtlas; P20591; -.
DR PRIDE; P20591; -.
DR ProteomicsDB; 53763; -. [P20591-1]
DR ProteomicsDB; 53764; -. [P20591-2]
DR Antibodypedia; 23580; 529 antibodies from 33 providers.
DR DNASU; 4599; -.
DR Ensembl; ENST00000398598.8; ENSP00000381599.3; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000398600.6; ENSP00000381601.2; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000413778.6; ENSP00000408498.2; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000417963.6; ENSP00000402215.2; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000419044.6; ENSP00000392151.2; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000455164.6; ENSP00000410523.2; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000619682.1; ENSP00000478441.1; ENSG00000157601.15. [P20591-2]
DR Ensembl; ENST00000679445.1; ENSP00000505630.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000679464.1; ENSP00000505874.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000679543.1; ENSP00000505047.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000679626.1; ENSP00000506481.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000679705.1; ENSP00000506372.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000679911.1; ENSP00000505189.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000680176.1; ENSP00000506270.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000680182.1; ENSP00000506395.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000680347.1; ENSP00000506183.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000680364.1; ENSP00000505781.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000680536.1; ENSP00000505029.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000680629.1; ENSP00000506047.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000680760.1; ENSP00000506199.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000680776.1; ENSP00000506512.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000681039.1; ENSP00000506220.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000681191.1; ENSP00000505657.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000681266.1; ENSP00000506348.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000681415.1; ENSP00000506062.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000681607.1; ENSP00000505489.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000681671.1; ENSP00000506712.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000681849.1; ENSP00000505051.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000681857.1; ENSP00000505669.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000681867.1; ENSP00000506690.1; ENSG00000157601.15. [P20591-1]
DR Ensembl; ENST00000681896.1; ENSP00000505457.1; ENSG00000157601.15. [P20591-1]
DR GeneID; 4599; -.
DR KEGG; hsa:4599; -.
DR MANE-Select; ENST00000398598.8; ENSP00000381599.3; NM_002462.5; NP_002453.2.
DR UCSC; uc002yzh.5; human. [P20591-1]
DR CTD; 4599; -.
DR DisGeNET; 4599; -.
DR GeneCards; MX1; -.
DR HGNC; HGNC:7532; MX1.
DR HPA; ENSG00000157601; Tissue enhanced (brain, salivary gland).
DR MIM; 147150; gene.
DR neXtProt; NX_P20591; -.
DR OpenTargets; ENSG00000157601; -.
DR PharmGKB; PA31333; -.
DR VEuPathDB; HostDB:ENSG00000157601; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000155686; -.
DR HOGENOM; CLU_008964_8_0_1; -.
DR InParanoid; P20591; -.
DR OMA; FHKWSAV; -.
DR OrthoDB; 494748at2759; -.
DR PhylomeDB; P20591; -.
DR TreeFam; TF331484; -.
DR BRENDA; 3.6.5.5; 2681.
DR PathwayCommons; P20591; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR SignaLink; P20591; -.
DR SIGNOR; P20591; -.
DR BioGRID-ORCS; 4599; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; MX1; human.
DR EvolutionaryTrace; P20591; -.
DR GeneWiki; MX1; -.
DR GenomeRNAi; 4599; -.
DR Pharos; P20591; Tbio.
DR PRO; PR:P20591; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P20591; protein.
DR Bgee; ENSG00000157601; Expressed in trigeminal ganglion and 186 other tissues.
DR ExpressionAtlas; P20591; baseline and differential.
DR Genevisible; P20591; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0140374; P:antiviral innate immune response; IEP:ARUK-UCL.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; IEP:ARUK-UCL.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
DR GO; GO:0034340; P:response to type I interferon; TAS:UniProtKB.
DR GO; GO:0009615; P:response to virus; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd08771; DLP_1; 1.
DR DisProt; DP01239; -.
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; Acetylation; Alternative splicing; Antiviral defense;
KW Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; GTP-binding;
KW Immunity; Innate immunity; Membrane; Nucleotide-binding; Nucleus;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..662
FT /note="Interferon-induced GTP-binding protein Mx1"
FT /id="PRO_0000382943"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:2607176, ECO:0000269|Ref.10"
FT CHAIN 2..662
FT /note="Interferon-induced GTP-binding protein Mx1, N-
FT terminally processed"
FT /id="PRO_0000206592"
FT DOMAIN 67..340
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 574..662
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 77..84
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 102..104
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 178..181
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 247..250
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 279..282
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 341..366
FT /note="Bundle signaling element (BSE)"
FT REGION 366..533
FT /note="Middle domain"
FT REGION 367..632
FT /note="Stalk"
FT REGION 554..557
FT /note="Critical for lipid-binding"
FT BINDING 77..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 178..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 247..250
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine; in Interferon-induced GTP-
FT binding protein Mx1; alternate"
FT /evidence="ECO:0000269|Ref.9"
FT VAR_SEQ 425..662
FT /note="GHKILSRKIQKFENQYRGRELPGFVNYRTFETIVKQQIKALEEPAVDMLHTV
FT TDMVRLAFTDVSIKNFEEFFNLHRTAKSKIEDIRAEQEREGEKLIRLHFQMEQIVYCQD
FT QVYRGALQKVREKELEEEKKKKSWDFGAFQSSSATDSSMEEIFQHLMAYHQEASKRISS
FT HIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARLTQA
FT RRRLAQFPG -> GGQQAHLQPHPFDHPVLHAPDVRPAASEGHAAAPAGQGHLQLAPEG
FT AERHQRQAEVPEGAACTADAGSAPACPVPRLTTLCPAP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20603636"
FT /id="VSP_042904"
FT VARIANT 379
FT /note="V -> I (in dbSNP:rs469390)"
FT /evidence="ECO:0000269|PubMed:10830953,
FT ECO:0000269|PubMed:10942113, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2154602,
FT ECO:0000269|PubMed:2481229"
FT /id="VAR_058010"
FT VARIANT 381
FT /note="A -> V (in dbSNP:rs34717738)"
FT /id="VAR_034116"
FT VARIANT 611
FT /note="Q -> H (in dbSNP:rs2230454)"
FT /id="VAR_034117"
FT MUTAGEN 81
FT /note="S->C: No effect on GTP-binding, nor on viral
FT infection."
FT /evidence="ECO:0000269|PubMed:8411374"
FT MUTAGEN 83
FT /note="K->A: Loss of GTP-binding. Loss of potentiation of
FT TRPC6 activity. Loss of protection against viral
FT infection."
FT /evidence="ECO:0000269|PubMed:15757897,
FT ECO:0000269|PubMed:8411374"
FT MUTAGEN 83
FT /note="K->M: Loss of GTP-binding. Loss of protection
FT against viral infection."
FT /evidence="ECO:0000269|PubMed:15757897,
FT ECO:0000269|PubMed:8411374"
FT MUTAGEN 103
FT /note="T->A: Loss of GTP-binding. Loss of potentiation of
FT TRPC6 activity. Loss of protection against viral
FT infection."
FT /evidence="ECO:0000269|PubMed:15757897,
FT ECO:0000269|PubMed:9060610"
FT MUTAGEN 554
FT /note="K->E: Strong liposome-binding reduction."
FT /evidence="ECO:0000269|PubMed:21900240"
FT MUTAGEN 555
FT /note="K->E: Strong liposome-binding reduction."
FT /evidence="ECO:0000269|PubMed:21900240"
FT MUTAGEN 556
FT /note="K->E: Strong liposome-binding reduction."
FT /evidence="ECO:0000269|PubMed:21900240"
FT MUTAGEN 557
FT /note="K->E: Strong liposome-binding reduction."
FT /evidence="ECO:0000269|PubMed:21900240"
FT MUTAGEN 612
FT /note="L->K: Loss of GTP-hydrolysis. No effect on GTP-
FT binding, nor on potentiation of TRPC6 activity."
FT /evidence="ECO:0000269|PubMed:15757897"
FT MUTAGEN 632
FT /note="E->A: Reduced antiviral activity."
FT /evidence="ECO:0000269|PubMed:21962493"
FT MUTAGEN 640
FT /note="R->A: Fails to sequester viral nucleoproteins, no
FT antiviral activity."
FT /evidence="ECO:0000269|PubMed:21962493"
FT MUTAGEN 645
FT /note="E->R: Loss of antiviral activity towards CCHFV and
FT LACV."
FT /evidence="ECO:0000269|PubMed:11880649,
FT ECO:0000269|PubMed:15047845"
FT CONFLICT 164
FT /note="L -> R (in Ref. 1; AAA36337)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="D -> G (in Ref. 4; BAG53272)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="Q -> H (in Ref. 4; BAG37852)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="E -> G (in Ref. 4; BAG53272)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="M -> I (in Ref. 4; BAG37852)"
FT /evidence="ECO:0000305"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 50..61
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4P4U"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:4P4U"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4P4S"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:4P4U"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:4P4S"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:4P4U"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:4P4U"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4P4S"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:4P4U"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:4P4U"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3SZR"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:4P4U"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:4P4U"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:3SZR"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:4P4U"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:4P4U"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 292..304
FT /evidence="ECO:0007829|PDB:4P4U"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 320..338
FT /evidence="ECO:0007829|PDB:4P4U"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 342..358
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 367..390
FT /evidence="ECO:0007829|PDB:4P4U"
FT HELIX 403..437
FT /evidence="ECO:0007829|PDB:3LJB"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:3SZR"
FT HELIX 451..463
FT /evidence="ECO:0007829|PDB:3LJB"
FT HELIX 466..492
FT /evidence="ECO:0007829|PDB:3LJB"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:5GTM"
FT HELIX 496..528
FT /evidence="ECO:0007829|PDB:3LJB"
FT HELIX 574..604
FT /evidence="ECO:0007829|PDB:3LJB"
FT HELIX 606..618
FT /evidence="ECO:0007829|PDB:3LJB"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:3LJB"
FT HELIX 626..629
FT /evidence="ECO:0007829|PDB:3LJB"
FT HELIX 634..659
FT /evidence="ECO:0007829|PDB:5GTM"
SQ SEQUENCE 662 AA; 75520 MW; 626A7DD946F89384 CRC64;
MVVSEVDIAK ADPAAASHPL LLNGDATVAQ KNPGSVAENN LCSQYEEKVR PCIDLIDSLR
ALGVEQDLAL PAIAVIGDQS SGKSSVLEAL SGVALPRGSG IVTRCPLVLK LKKLVNEDKW
RGKVSYQDYE IEISDASEVE KEINKAQNAI AGEGMGISHE LITLEISSRD VPDLTLIDLP
GITRVAVGNQ PADIGYKIKT LIKKYIQRQE TISLVVVPSN VDIATTEALS MAQEVDPEGD
RTIGILTKPD LVDKGTEDKV VDVVRNLVFH LKKGYMIVKC RGQQEIQDQL SLSEALQREK
IFFENHPYFR DLLEEGKATV PCLAEKLTSE LITHICKSLP LLENQIKETH QRITEELQKY
GVDIPEDENE KMFFLIDKVN AFNQDITALM QGEETVGEED IRLFTRLRHE FHKWSTIIEN
NFQEGHKILS RKIQKFENQY RGRELPGFVN YRTFETIVKQ QIKALEEPAV DMLHTVTDMV
RLAFTDVSIK NFEEFFNLHR TAKSKIEDIR AEQEREGEKL IRLHFQMEQI VYCQDQVYRG
ALQKVREKEL EEEKKKKSWD FGAFQSSSAT DSSMEEIFQH LMAYHQEASK RISSHIPLII
QFFMLQTYGQ QLQKAMLQLL QDKDTYSWLL KERSDTSDKR KFLKERLARL TQARRRLAQF
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