ID E9M5M3_9GAMA Unreviewed; 383 AA.
AC E9M5M3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glycoprotein M {ECO:0000313|EMBL:ADW24381.1};
GN ORFNames=RHVP-L.39 {ECO:0000313|EMBL:ADW24463.1}, RHVP.39
GN {ECO:0000313|EMBL:ADW24381.1};
OS Cricetid gammaherpesvirus 2.
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Rhadinovirus;
OC Rhadinovirus cricetidgamma2.
OX NCBI_TaxID=1605972 {ECO:0000313|EMBL:ADW24381.1, ECO:0000313|Proteomes:UP000134313};
RN [1] {ECO:0000313|Proteomes:UP000134313, ECO:0000313|Proteomes:UP000164320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21209105; DOI=10.1128/JVI.01661-10;
RA Loh J., Zhao G., Nelson C.A., Coder P., Droit L., Handley S.A.,
RA Johnson L.S., Vachharajani P., Guzman H., Tesh R.B., Wang D., Fremont D.H.,
RA Virgin H.W.;
RT "Identification and sequencing of a novel rodent gammaherpesvirus that
RT establishes acute and latent infection in laboratory mice.";
RL J. Virol. 85:2642-2656(2011).
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; HQ221963; ADW24381.1; -; Genomic_DNA.
DR EMBL; HQ698924; ADW24463.1; -; Genomic_DNA.
DR RefSeq; YP_004207876.1; NC_015049.1.
DR GeneID; 10192231; -.
DR KEGG; vg:10192231; -.
DR OrthoDB; 7915at10239; -.
DR Proteomes; UP000134313; Genome.
DR Proteomes; UP000164320; 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:UP000134313};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 383 AA; 43556 MW; 18045147F6FAECB7 CRC64;
MAVFKSAVIS RSDSFLLRTW TNLLALLALM YASTLLVPIA ASINNVGFPC YFINLVDYSN
FNLTVRNSAK HLTPTLFLEP VEMYVYLTWS FIVDGLNLAY FIYAAVILYR LKATAVTNMR
AIETWITLLG NHAVIFLIVA KLWTLQLFIH VLSYKHVFLA AFVYVFHFGL SYLHIHLFIS
RNVAQWKADD MERSLPEGTS LEKLVFIFRP IIANIQMSLL AMEMMVFSLS VMMAICNSFY
MLVSDAVFGA INLLLILTIA WHISAEVFLA RYLKHHVGFY VGLFVSYVIM LLPVIRYDAV
FVAARLHKPI TVNITIIPLI CIIVIVIRII RLRKSKPSMA SVSYSKVSDS VKLRNVSHVI
PSNPTPLMLD SETDDEEDFL FAK
//
