GM_BHV1C
ID GM_BHV1C Reviewed; 438 AA.
AC P52370; O39493;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 29-SEP-2021, entry version 75.
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 Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine
OS rhinotracheitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10323;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7793062; DOI=10.1006/viro.1995.1321;
RA Vlcek C., Benes V., Lu Z., Kutish G.F., Paces V., Rock D., Letchworth G.J.,
RA Schwyzer M.;
RT "Nucleotide sequence analysis of a 30-kb region of the bovine herpesvirus 1
RT genome which exhibits a colinear gene arrangement with the UL21 to UL4
RT genes of herpes simplex virus.";
RL Virology 210:100-108(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Schwyzer M., Paces V., Letchworth G.J., Misra V., Buhk H.J., Lowery D.E.,
RA Simard C., Bello L.J., Thiry E., Vlcek C.;
RT "Complete DNA sequence of bovine herpesvirus 1.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION OF PROBABLE FRAMESHIFT, GLYCOSYLATION, SUBUNIT, AND
RP DISULFIDE BOND.
RX PubMed=9525625; DOI=10.1128/jvi.72.4.3029-3036.1998;
RA Wu S.X., Zhu X.P., Letchworth G.J.;
RT "Bovine herpesvirus 1 glycoprotein M forms a disulfide-linked heterodimer
RT with the U(L)49.5 protein.";
RL J. Virol. 72:3029-3036(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 -!- 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 -!- PTM: N-glycosylated. It is not O-glycosylated.
CC {ECO:0000269|PubMed:9525625}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein M family.
CC {ECO:0000255|HAMAP-Rule:MF_04035}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA88123.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z48053; CAA88123.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AJ004801; CAA06124.1; -; Genomic_DNA.
DR PIR; S61245; S61245.
DR RefSeq; NP_045349.1; NC_001847.1.
DR PRIDE; P52370; -.
DR GeneID; 1487373; -.
DR KEGG; vg:1487373; -.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044177; C:host cell Golgi apparatus; IMP:AgBase.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0033644; C:host cell membrane; IDA:AgBase.
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:0044423; C:virion component; IDA:AgBase.
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; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Virion.
FT CHAIN 1..438
FT /note="Envelope glycoprotein M"
FT /id="PRO_0000115776"
FT TOPO_DOM 1..13
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 35..88
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 110..132
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 154..158
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 180..212
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 234..248
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 270..276
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 298..317
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT TOPO_DOM 339..438
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT REGION 395..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 45
FT /note="Interchain (with gN)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
SQ SEQUENCE 438 AA; 45517 MW; 4E7C7FA64FAAEFC7 CRC64;
MAGSAQPAAV HWRLWLAQVG VFAGLALLLL ITLIGAASPG AGLPCFYAAI VNYNARNLSA
DGGAWAQREL GARHPALFLE TPTTAAFSAY TAVVLLAVAA FDVAAAIIIR RENSGGFAAA
YHMNALATLA TPPGALLLGA LAAWTLQAAV LLLSHKIMVL AAATYLAHLA PPAAFVGLFC
TAGLPGAEYA QAVHALRERS PRAHRLLGPG RAVMINLAGG LLALIIGTAP LMLGQLLGAG
LGLSLAQTVV AGVTVFCLAA VLFLVLTELV LSRYTQVLPG PAFGTLVAAS CIAVASHDYF
HQLRGVVRTQ APRAAARVKL ALAGVALLAV AMLVLRLVRA CLHHRRKGSA FYGHVSAARQ
QAARYIARAR SSRGMAPLEG DAAALLDRGV ASDDEEAVYE AHAPPRPPTI PLRRPEVPHS
RASHPRPPPR SPPPAHVK
