ID GM_HHV11 Reviewed; 473 AA. AC P04288; B9VQD7; Q09IC3; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-1987, sequence version 1. DT 27-MAR-2024, entry version 107. DE RecName: Full=Envelope glycoprotein M {ECO:0000255|HAMAP-Rule:MF_04035}; DE Short=gM {ECO:0000255|HAMAP-Rule:MF_04035}; GN Name=gM {ECO:0000255|HAMAP-Rule:MF_04035}; ORFNames=UL10; OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus; OC Simplexvirus humanalpha1; Human herpesvirus 1. OX NCBI_TaxID=10299; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3010237; DOI=10.1093/nar/14.8.3435; RA McGeoch D.J., Dolan A., Frame M.C.; RT "DNA sequence of the region in the genome of herpes simplex virus type 1 RT containing the exonuclease gene and neighbouring genes."; RL Nucleic Acids Res. 14:3435-3448(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531; RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., RA Perry L.J., Scott J.E., Taylor P.; RT "The complete DNA sequence of the long unique region in the genome of RT herpes simplex virus type 1."; RL J. Gen. Virol. 69:1531-1574(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nonneuroinvasive mutant HF10; RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019; RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.; RT "Determination and analysis of the DNA sequence of highly attenuated herpes RT simplex virus type 1 mutant HF10, a potential oncolytic virus."; RL Microbes Infect. 9:142-149(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17 syn+; RA Cunningham C., Davison A.J.; RT "Herpes simplex virus type 1 bacterial artificial chromosome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98. RX PubMed=2826807; DOI=10.1128/jvi.62.2.444-453.1988; RA McGeoch D.J., Dalrymple M.A., Dolan A., McNab D., Perry L.J., Taylor P., RA Challberg M.D.; RT "Structures of herpes simplex virus type 1 genes required for replication RT of virus DNA."; RL J. Virol. 62:444-453(1988). RN [6] RP SUBCELLULAR LOCATION. RC STRAIN=F; RX PubMed=17079321; DOI=10.1128/jvi.01756-06; RA Baines J.D., Wills E., Jacob R.J., Pennington J., Roizman B.; RT "Glycoprotein M of herpes simplex virus 1 is incorporated into virions RT during budding at the inner nuclear membrane."; RL J. Virol. 81:800-812(2007). RN [7] RP SUBCELLULAR LOCATION. RC STRAIN=F; RX PubMed=18596102; DOI=10.1128/jvi.00904-08; RA Loret S., Guay G., Lippe R.; RT "Comprehensive characterization of extracellular herpes simplex virus type RT 1 virions."; RL J. Virol. 82:8605-8618(2008). RN [8] RP SUBCELLULAR LOCATION. RC STRAIN=F; RX PubMed=19279119; DOI=10.1128/jvi.02431-08; RA Wills E., Mou F., Baines J.D.; RT "The U(L)31 and U(L)34 gene products of herpes simplex virus 1 are required RT for optimal localization of viral glycoproteins D and M to the inner RT nuclear membranes of infected cells."; RL J. Virol. 83:4800-4809(2009). RN [9] RP INTERACTION WITH GN, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=26999189; DOI=10.3390/v8030083; RA Striebinger H., Funk C., Raschbichler V., Bailer S.M.; RT "Subcellular trafficking and functional relationship of the HSV-1 RT glycoproteins N and M."; RL Viruses 8:83-83(2016). CC -!- FUNCTION: Envelope glycoprotein important for virion assembly and CC egress. Plays a role in the correct incorporation of gH-gL into virion CC membrane. Directs the glycoprotein N (gN) to the host trans-Golgi CC network. {ECO:0000255|HAMAP-Rule:MF_04035, CC ECO:0000269|PubMed:26999189}. CC -!- SUBUNIT: Interacts (via N-terminus) with gN (via N-terminus). The gM-gN CC heterodimer forms the gCII complex. {ECO:0000255|HAMAP-Rule:MF_04035, CC ECO:0000269|PubMed:26999189}. CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP- CC Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network CC {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:26999189}. Host CC endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass CC membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner CC membrane {ECO:0000255|HAMAP-Rule:MF_04035, CC ECO:0000269|PubMed:17079321}; Multi-pass membrane protein CC {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, CC this protein accumulates in the trans-Golgi network where secondary CC envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035, CC ECO:0000269|PubMed:17079321}. CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein M family. CC {ECO:0000255|HAMAP-Rule:MF_04035}. 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; X14112; CAA32346.1; -; Genomic_DNA. DR EMBL; X03839; CAA27451.1; -; Genomic_DNA. DR EMBL; DQ889502; ABI63472.1; -; Genomic_DNA. DR EMBL; FJ593289; ACM62232.1; -; Genomic_DNA. DR EMBL; AH002360; AAA45821.2; -; Genomic_DNA. DR PIR; A03736; WMBE51. DR RefSeq; YP_009137084.1; NC_001806.2. DR SMR; P04288; -. DR BioGRID; 971418; 1. DR ChEMBL; CHEMBL2364696; -. DR DrugCentral; P04288; -. DR TCDB; 9.B.212.1.1; the human simplex virus-1 gm protein (hsv-gm) family. DR DNASU; 2703379; -. DR GeneID; 2703379; -. DR KEGG; vg:2703379; -. DR PRO; PR:P04288; -. DR Proteomes; UP000009294; Genome. DR Proteomes; UP000180652; Genome. DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-UniRule. DR GO; GO:0044201; C:host cell nuclear inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IDA:CAFA. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR HAMAP; MF_04035; HSV_GM; 1. DR InterPro; IPR000785; Herpes_glycop_M. DR Pfam; PF01528; Herpes_glycop; 1. DR PRINTS; PR00333; HSVINTEGRLMP. PE 1: Evidence at protein level; KW Disulfide bond; Glycoprotein; Host endosome; Host Golgi apparatus; KW Host membrane; Host nucleus; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Viral envelope protein; Virion. FT CHAIN 1..473 FT /note="Envelope glycoprotein M" FT /id="PRO_0000115775" FT TOPO_DOM 1..32 FT /note="Intravirion" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TRANSMEM 33..53 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TOPO_DOM 54..90 FT /note="Virion surface" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TRANSMEM 91..111 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TOPO_DOM 112..137 FT /note="Intravirion" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TRANSMEM 138..158 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TOPO_DOM 159..163 FT /note="Virion surface" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TRANSMEM 164..184 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TOPO_DOM 185..216 FT /note="Intravirion" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TRANSMEM 217..237 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TOPO_DOM 238..250 FT /note="Virion surface" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TRANSMEM 251..271 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TOPO_DOM 272..280 FT /note="Intravirion" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TRANSMEM 281..301 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TOPO_DOM 302..318 FT /note="Virion surface" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TRANSMEM 319..339 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT TOPO_DOM 340..473 FT /note="Intravirion" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT REGION 371..399 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 440..473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 59 FT /note="Interchain (with gN)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035" FT VARIANT 77 FT /note="R -> C (in strain: Nonneuroinvasive mutant HF10)" FT VARIANT 105 FT /note="V -> A (in strain: Nonneuroinvasive mutant HF10)" FT VARIANT 279 FT /note="V -> M (in STRAIN: 17 syn+)" FT VARIANT 448 FT /note="D -> E (in strain: Nonneuroinvasive mutant HF10)" FT VARIANT 462 FT /note="A -> T (in strain: Nonneuroinvasive mutant HF10)" SQ SEQUENCE 473 AA; 51393 MW; E08FD792409A81E6 CRC64; MGRPAPRGSP DSAPPTKGMT GARTAWWVWC VQVATFVVSA VCVTGLLVLA SVFRARFPCF YATASSYAGV NSTAEVRGGV AVPLRLDTQS LVGTYVITAV LLLAVAVYAV VGAVTSRYDR ALDAGRRLAA ARMAMPHATL IAGNVCSWLL QITVLLLAHR ISQLAHLVYV LHFACLVYFA AHFCTRGVLS GTYLRQVHGL MELAPTHHRV VGPARAVLTN ALLLGVFLCT ADAAVSLNTI AAFNFNFSAP GMLICLTVLF AILVVSLLLV VEGVLCHYVR VLVGPHLGAV AATGIVGLAC EHYYTNGYYV VETQWPGAQT GVRVALALVA AFALGMAVLR CTRAYLYHRR HHTKFFMRMR DTRHRAHSAL KRVRSSMRGS RDGRHRPAPG SPPGIPEYAE DPYAISYGGQ LDRYGDSDGE PIYDEVADDQ TDVLYAKIQH PRHLPDDDPI YDTVGGYDPE PAEDPVYSTV RRW //