GM_SUHVK
ID GM_SUHVK Reviewed; 393 AA.
AC Q85041; Q5PP86; Q85042;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 71.
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 Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain
OS Kaplan)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=33703;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8764089; DOI=10.1128/jvi.70.8.5684-5688.1996;
RA Dijkstra J.M., Visser N., Mettenleiter T.C., Klupp B.G.;
RT "Identification and characterization of pseudorabies virus glycoprotein gM
RT as a nonessential virion component.";
RL J. Virol. 70:5684-5688(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14671123; DOI=10.1128/jvi.78.1.424-440.2004;
RA Klupp B.G., Hengartner C.J., Mettenleiter T.C., Enquist L.W.;
RT "Complete, annotated sequence of the pseudorabies virus genome.";
RL J. Virol. 78:424-440(2004).
RN [3]
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=9420258; DOI=10.1128/jvi.72.1.550-557.1998;
RA Joens A., Dijkstra J.M., Mettenleiter T.C.;
RT "Glycoproteins M and N of pseudorabies virus form a disulfide-linked
RT complex.";
RL J. Virol. 72:550-557(1998).
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 ECO:0000269|PubMed:9420258}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA65905.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X97257; CAA65904.1; -; Genomic_DNA.
DR EMBL; X97257; CAA65905.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK001744; DAA02185.1; -; Genomic_DNA.
DR RefSeq; YP_068365.1; NC_006151.1.
DR IntAct; Q85041; 2.
DR PRIDE; Q85041; -.
DR GeneID; 2952500; -.
DR KEGG; vg:2952500; -.
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 GO; GO:0019068; P:virion assembly; IMP:AgBase.
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; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Virion.
FT CHAIN 1..393
FT /note="Envelope glycoprotein M"
FT /id="PRO_5000095951"
FT TOPO_DOM 1..14
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 36..83
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 105..130
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 152..154
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 176..207
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 229..241
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 263..264
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 286..303
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 325..393
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT DISULFID 45
FT /note="Interchain (with gN)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
SQ SEQUENCE 393 AA; 41546 MW; 527613E8DE169D8A CRC64;
MCGPRNAEAV SWRSWLIEVC GFALAALTLV LTLIFASLPE MGFPCFYATV ADYDTLNDTS
GGVWTRQPLV APALFLETPT VTSFFGFTAT VLLAHALYAV AGAVVLRREA GRLAFQPSVV
LYAASTVAAP GTLMLGALCA WTLQAVVLLM AHKQAGLAAA AYITHFVFLA LFGACHACKG
TGDVRAALAA SPPLRRVAVH ARAVVTNVVL GAVGLGAAVV GLMLGVLLAN SFHISLWKTA
EAALAVFTLL ALALMVFVEV VVSGYVQVLP TPAFCVLVAS AAFGVSAHRY FAKFSEALGE
THGVVIGTRA VLAVLSLIAL AMIVVRLVRA CIAHRARGSR FYANVDKART TARRYLQKRL
HGRGNDEYLL APGSGDDEFD DGDEVVYENL GFE
