GM_PSHV1
ID GM_PSHV1 Reviewed; 413 AA.
AC Q6UDH4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 44.
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 Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS (Pacheco's disease virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX NCBI_TaxID=670426;
OH NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA Thureen D.R., Keeler C.L. Jr.;
RT "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL J. Virol. 80:7863-7872(2006).
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; AY372243; AAQ73736.1; -; Genomic_DNA.
DR RefSeq; NP_944430.1; NC_005264.1.
DR SMR; Q6UDH4; -.
DR GeneID; 2656970; -.
DR KEGG; vg:2656970; -.
DR Proteomes; UP000006840; 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..413
FT /note="Envelope glycoprotein M"
FT /id="PRO_0000406799"
FT TOPO_DOM 1..19
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 41..88
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 110..133
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 155..160
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 182..218
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 240..251
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 273..277
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 299..312
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 334..413
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT DISULFID 51
FT /note="Interchain (with gN)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
SQ SEQUENCE 413 AA; 45331 MW; 5A1CE87A739453BE CRC64;
MGNYYYGGQE SRLERISWRM WMVEAACYIV LVLLTLVSSF ASLSSTTGFP CFVGTVGESS
FGGDLMGHGM TPARRDGVKI FFMSSPSTLF VVFSAVFVWL VVAVYLLLGG VRVKMCNFDS
SYGASELSSA VATMTSLVTL SITAWAWQVF VLMLSYRQLT LAAVAFVGIF IAGLVFMLSF
ASGGKSPENY ATFNSQLKTV CKDVHAVITA FKAVVLNLFC VVFGVWHLML VMLGAVIMVL
NFGVSIPKAT TGALVVFIVL GLVYLMMIEL VVSRYVHVLL GPHLGMIIAL GIAGTSALSY
AETLDEIMYA SWKPVAAGIL GAFSVIVLAL AVLRAVRSYK FHKAAQSKFL QQVASVAQTV
KNRARRERNG PRVHKRYYDA VPVDAYEDDP YRQSPRRSRH GEAEDVIYEN MKY
