ID Q9DPS4_MEHV1 Unreviewed; 423 AA.
AC Q9DPS4;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=UL10 virion membrane glycoprotein M {ECO:0000313|EMBL:AAG45747.1};
GN Name=HVT017 {ECO:0000313|EMBL:AAG45747.1};
OS Meleagrid herpesvirus 1 (MeHV-1) (Turkey herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Mardivirus;
OC Mardivirus meleagridalpha1.
OX NCBI_TaxID=37108 {ECO:0000313|EMBL:AAG45747.1, ECO:0000313|Proteomes:UP000175168};
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1] {ECO:0000313|EMBL:AAG45747.1, ECO:0000313|Proteomes:UP000175168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FC126 {ECO:0000313|EMBL:AAG45747.1};
RX PubMed=11134310; DOI=10.1128/JVI.75.2.971-978.2001;
RA Afonso C.L., Tulman E.R., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of turkey herpesvirus.";
RL J. Virol. 75:971-978(2001).
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:0000256|ARBA:ARBA00003017}.
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DR EMBL; AF291866; AAG45747.1; -; Genomic_DNA.
DR RefSeq; NP_073303.1; NC_002641.1.
DR GeneID; 918568; -.
DR KEGG; vg:918568; -.
DR OrthoDB; 7915at10239; -.
DR Proteomes; UP000175168; 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: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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000175168};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 423 AA; 47530 MW; 536A4C47BD5582BF CRC64;
MDGQTKLRKP RGGSKQMDYV YKKIWAIQAA CFTIAVLAFL GTLMSASIHL AEGFPCFFAA
VVDYAIVNTS TIHTGLTNPR LGGVVPVLFF QTKSTVFFFY AISIVFMVLM FYIIVGAVIA
NKSHVGVAYM ERGMFAYSLI ISPTTLLLGT VSMWLLQAIV IVLAHKLIVL AAAIYLVYFS
AITFFYGYFC GRGVDSKVYA EDVATTKYID RTLHRMVGSV RAVVINLLSI VYSLILIMAG
LMFGMLLANS FTLKFFHVIV VILVTTSIST LMYLLIVEFL IARYVHMIMG TYLGLIIGYG
MLWMTSCDYV NRFYYAMDNA SSLRAACHGV LAVFTILILL GMIVRLVRAG LYHRRRSTHA
YASAIKLQKS VKERLKRWNR GRTRYDSVAE DEHALTQTPY TETSDDETIY DRVYSGSDSE
WDD
//
