GM_EBVB9
ID GM_EBVB9 Reviewed; 405 AA.
AC P03215; Q777D4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 93.
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=BBRF3;
OS Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [2]
RP INTERACTION WITH GN.
RX PubMed=9621013; DOI=10.1128/jvi.72.7.5559-5564.1998;
RA Lake C.M., Molesworth S.J., Hutt-Fletcher L.M.;
RT "The Epstein-Barr virus (EBV) gN homolog BLRF1 encodes a 15-kilodalton
RT glycoprotein that cannot be authentically processed unless it is
RT coexpressed with the EBV gM homolog BBRF3.";
RL J. Virol. 72:5559-5564(1998).
RN [3]
RP FUNCTION.
RX PubMed=11070013; DOI=10.1128/jvi.74.23.11162-11172.2000;
RA Lake C.M., Hutt-Fletcher L.M.;
RT "Epstein-Barr virus that lacks glycoprotein gN is impaired in assembly and
RT infection.";
RL J. Virol. 74:11162-11172(2000).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15534216; DOI=10.1073/pnas.0407320101;
RA Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E.,
RA Illanes D., Sarracino D., Kieff E.;
RT "Proteins of purified Epstein-Barr virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004).
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:11070013}.
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:9621013}.
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 -!- DOMAIN: The highly charged and proline-rich cytoplasmic tail might
CC interact with the virion tegument.
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; V01555; CAA24825.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53435.1; -; Genomic_DNA.
DR PIR; G43043; QQBE35.
DR RefSeq; YP_401685.1; NC_007605.1.
DR SMR; P03215; -.
DR PRIDE; P03215; -.
DR DNASU; 3783687; -.
DR GeneID; 3783687; -.
DR KEGG; vg:3783687; -.
DR Proteomes; UP000153037; 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 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..405
FT /note="Envelope glycoprotein M"
FT /id="PRO_0000115783"
FT TOPO_DOM 1..17
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 39..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..121
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 143..149
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 171..192
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 193..215
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 216..245
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 267
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 289..299
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 321..405
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT REGION 346..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..397
FT /note="Polar residues"
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 405 AA; 45792 MW; 25A8A46B6CDC0AE1 CRC64;
MKSSKNDTFV YRTWVKTLVV YFVMFVMSAV VPITAMFPNL GYPCYFNALV DYGALNLTNY
NLAHHLTPTL YLEPPEMFVY ITLVFIADCV AFIYYACGEV ALIKARKKVS GLTDLSAWVS
AVGSPTVLFL AILKLWSIQV FIQVLSYKHV FLSAFVYFLH FLASVLHACA CVTRFSPVWV
VKAQDNSIPQ DTFLWWVVFY LKPVVTNLYL GCLALETLVF SLSVFLALGN SFYFMVGDMV
LGAVNLFLIL PIFWYILTEV WLASFLRHNF GFYCGMFIAS IILILPLVRY EAVFVSAKLH
TTVAINVAII PILCSVAMLI RICRIFKSMR QGTDYVPVSE TVELELESEP RPRPSRTPSP
GRNRRRSSTS SSSSRSTRRQ RPVSTQALVS SVLPMTTDSE EEIFP
