GM_VZVD
ID GM_VZVD Reviewed; 435 AA.
AC P09298;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 23-FEB-2022, entry version 81.
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=ORF50;
OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
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 -!- 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 -!- 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}. Host endosome membrane
CC {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane
CC {ECO:0000255|HAMAP-Rule:MF_04035}; 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 -!- SIMILARITY: Belongs to the herpesviridae glycoprotein M family.
CC {ECO:0000255|HAMAP-Rule:MF_04035}.
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DR EMBL; X04370; CAA27934.1; -; Genomic_DNA.
DR PIR; F27344; WZBE50.
DR SMR; P09298; -.
DR PRIDE; P09298; -.
DR Proteomes; UP000002602; 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:0016021; C:integral component of 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 3: Inferred from homology;
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..435
FT /note="Envelope glycoprotein M"
FT /id="PRO_0000115782"
FT TOPO_DOM 1..36
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 58..111
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 133..155
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 177..178
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 200..233
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 255..265
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 266..288
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 289..294
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 295..317
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 318..334
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 356..435
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT DISULFID 68
FT /note="Interchain (with gN)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
SQ SEQUENCE 435 AA; 48672 MW; F74EC830584DA2C2 CRC64;
MGTQKKGPRS EKVSPYDTTT PEVEALDHQM DTLNWRIWII QVMMFTLGAV MLLATLIAAS
SEYTGIPCFY AAVVDYELFN ATLDGGVWSG NRGGYSAPVL FLEPHSVVAF TYYTALTAMA
MAVYTLITAA IIHRETKNQR VRQSSGVAWL VVDPTTLFWG LLSLWLLNAV VLLLAYKQIG
VAATLYLGHF ATSVIFTTYF CGRGKLDETN IKAVANLRQQ SVFLYRLAGP TRAVFVNLMA
ALMAICILFV SLMLELVVAN HLHTGLWSSV SVAMSTFSTL SVVYLIVSEL ILAHYIHVLI
GPSLGTLVAC ATLGTAAHSY MDRLYDPISV QSPRLIPTTR GTLACLAVFS VVMLLLRLMR
AYVYHRQKRS RFYGAVRRVP ERVRGYIRKV KPAHRNSRRT NYPSQGYGYV YENDSTYETD
REDELLYERS NSGWE
