GM_HHV8P
ID GM_HHV8P Reviewed; 400 AA.
AC F5HDD0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 29-SEP-2021, entry version 30.
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}; Synonyms=ORF39;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [3]
RP FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH GN.
RX PubMed=12771417; DOI=10.1099/vir.0.18941-0;
RA Koyano S., Mar E.C., Stamey F.R., Inoue N.;
RT "Glycoproteins M and N of human herpesvirus 8 form a complex and inhibit
RT cell fusion.";
RL J. Gen. Virol. 84:1485-1491(2003).
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 ECO:0000269|PubMed:12771417}.
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 ECO:0000269|PubMed:12771417}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04035,
CC ECO:0000269|PubMed:12771417}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}. Host
CC Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-
CC Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-
CC Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04035, ECO:0000269|PubMed:12771417}. Host nucleus inner
CC membrane {ECO:0000255|HAMAP-Rule:MF_04035,
CC ECO:0000269|PubMed:12771417}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}.
CC Note=During virion morphogenesis, this protein accumulates in the
CC trans-Golgi network where secondary envelopment occurs.
CC {ECO:0000255|HAMAP-Rule:MF_04035}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12771417}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein M family.
CC {ECO:0000255|HAMAP-Rule:MF_04035}.
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DR EMBL; AF148805; ABD28890.1; -; Genomic_DNA.
DR RefSeq; YP_001129392.1; NC_009333.1.
DR BioGRID; 1776940; 2.
DR PRIDE; F5HDD0; -.
DR DNASU; 4961437; -.
DR GeneID; 4961437; -.
DR KEGG; vg:4961437; -.
DR Proteomes; UP000000942; 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; IDA:CACAO.
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 1: Evidence at protein level;
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..400
FT /note="Envelope glycoprotein M"
FT /id="PRO_0000423792"
FT TOPO_DOM 1..16
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 38..76
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 98..113
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 135..152
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 174..208
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 230..234
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 256..270
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 292..300
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 322..400
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT REGION 348..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 44
FT /note="Interchain (with gN)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
SQ SEQUENCE 400 AA; 45364 MW; F7D162F0199EE670 CRC64;
MRASKSDRFL MSSWVKLLFV AVIMYICSAV VPMAATYEGL GFPCYFNNLV NYSALNLTVR
NSAKHLTPTL FLEKPEMLVY IFWTFIVDGI AIVYYCLAAV AVYRAKHVHA TTMMSMQSWI
ALLGSHSVLY VAILRMWSMQ LFIHVLSYKH VLMAAFVYCI HFCISFAHIQ SLITCNSAQW
EIPLLEQHVP DNTMMESLLT RWKPVCVNLY LSTTALEMLL FSLSTMMAVG NSFYVLVSDA
IFGAVNMFLA LTVVWYINTE FFLVKFMRRQ VGFYVGVFVG YLILLLPVIR YENAFVQANL
HYIVAINISC IPILCILAIV IRVIRSDWGL CTPSAAYMPL ATSAPTVDRT PTVHQKPPPL
PAKTRARAKV KDISTPAPRT QYQSDHESDS EIDETQMIFI
