GD_GAHVM
ID GD_GAHVM Reviewed; 403 AA.
AC Q9E6L6;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 02-DEC-2020, entry version 66.
DE RecName: Full=Envelope glycoprotein D;
DE Short=gD;
DE Flags: Precursor;
GN Name=MDV094;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
CC -!- FUNCTION: Envelope glycoprotein that binds to host cell entry
CC receptors. May trigger fusion with host membrane, by recruiting the
CC fusion machinery composed of gB and gH/gL (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Note=During virion morphogenesis, this
CC protein probably accumulates in the endosomes and trans-Golgi where
CC secondary envelopment occurs. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein D family.
CC {ECO:0000305}.
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DR EMBL; AF243438; AAG14268.1; -; Genomic_DNA.
DR SMR; Q9E6L6; -.
DR Proteomes; UP000008072; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR002896; Herpes_glycop_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR Pfam; PF01537; Herpes_glycop_D; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Host-virus interaction; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral attachment to host entry receptor;
KW Viral envelope protein; Virion; Virus entry into host cell.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..403
FT /note="Envelope glycoprotein D"
FT /id="PRO_0000406596"
FT TOPO_DOM 35..357
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..403
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 88..209
FT /evidence="ECO:0000250|UniProtKB:P57083"
FT DISULFID 127..222
FT /evidence="ECO:0000250|UniProtKB:P57083"
FT DISULFID 139..148
FT /evidence="ECO:0000250|UniProtKB:P57083"
SQ SEQUENCE 403 AA; 46199 MW; A2BC7235EAA5E938 CRC64;
MNRYRYESIF FRYISSTRMI LIICLLLGIG DMSAMGLKKD NSPIIPTLHP KGNENLRATL
NEYKIPSPLF DTLDNSYETK HVIYTDNCSF AVLNPFGDPK YTLLSLLLMG RRKYDALVAW
FVLGRACGRP IYLREYANCS TNEPFGTCKL KSLGWWDRRY AMTSYIDRDE LKLIIAAPSR
ELSGLYTRLI IINGEPISSD ILLTVKETCS FSRRGIKDNK LCKPFSFFVN GTTRLLDMVG
TGTPRAHEEN VKQWLERIGG KHLPIVVETS MQQVSNLPRS FRDSYFKSPD DDKYDDVKMT
SATTNNITTS VDGYTGLTNR PEDFEKAPYI TKRPIISVEE ASSQSPKIST EKKSRTQIII
SLVVLCVMFC FIVIGSGIWI LRKHRKTVMY DRRRPSRRAY SRL
