GM_GAHVM
ID GM_GAHVM Reviewed; 424 AA.
AC Q9E6Q6;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 23-FEB-2022, entry version 59.
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=MDV022;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
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}.
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; AF243438; AAG14202.1; -; Genomic_DNA.
DR RefSeq; YP_001033938.1; NC_002229.3.
DR SMR; Q9E6Q6; -.
DR GeneID; 4811483; -.
DR KEGG; vg:4811483; -.
DR Proteomes; UP000008072; 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..424
FT /note="Envelope glycoprotein M"
FT /id="PRO_0000406501"
FT TOPO_DOM 1..23
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 45..94
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 116..143
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 165..166
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 188..226
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 248..261
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 283
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 305..327
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 349..424
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT REGION 382..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 56
FT /note="Interchain (with gN)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
SQ SEQUENCE 424 AA; 47527 MW; F6AAFFE9A805D5BC CRC64;
MASRARMERN YRGLSHIDYV HKKMWVVQAV CFGIAVLVFF GTLVAASINL TEGFPCFFAA
VVDYRTVNTT LVHTGLTYPR LGGVVPVLFF QTKAVVFFFY ATSIVFVFLV CYITVGAIIS
SKKHVGAAYM GSGAFVFSLM ASPLTILLGT VSIWLLQAVV IVLAHKLIVL AAAVYLVHFS
TITFFYGYFC GRGVDSKVYA EDISSAKDID GSLHKLIGNV RAMMVNLLSI VYSIILIMSS
LMFGMLLANS FTLKFWHVIV TVLITTSVLT LIYLLVIEFL IARYVHIILG AYIGLLIGYG
MLWTTTCDYV NRFYYAMGAN ASNLRIACHS VLAVFTVLIL LAMVVRLIRA SLYHRRRSTR
AYAKAMKLQQ NVKHRLRQLR RSYKQRGSQS EDERALTQSR SAEASDEDTI YDRVYSGSES
EWDD