GB_PSHV1
ID GB_PSHV1 Reviewed; 911 AA.
AC Q6UDK4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 02-JUN-2021, entry version 59.
DE RecName: Full=Envelope glycoprotein B {ECO:0000255|HAMAP-Rule:MF_04032};
DE Short=gB {ECO:0000255|HAMAP-Rule:MF_04032};
DE Flags: Precursor;
GN Name=gB {ECO:0000255|HAMAP-Rule:MF_04032}; Synonyms=UL27;
OS Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS (Pacheco's disease virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX NCBI_TaxID=670426;
OH NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA Thureen D.R., Keeler C.L. Jr.;
RT "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL J. Virol. 80:7863-7872(2006).
CC -!- FUNCTION: Envelope glycoprotein that forms spikes at the surface of
CC virion envelope. Essential for the initial attachment to heparan
CC sulfate moieties of the host cell surface proteoglycans. Involved in
CC fusion of viral and cellular membranes leading to virus entry into the
CC host cell. Following initial binding to its host receptors, membrane
CC fusion is mediated by the fusion machinery composed at least of gB and
CC the heterodimer gH/gL. May be involved in the fusion between the virion
CC envelope and the outer nuclear membrane during virion egress.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Binds to heparan sulfate
CC proteoglycans. Interacts with gH/gL heterodimer. {ECO:0000255|HAMAP-
CC Rule:MF_04032}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032};
CC Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}.
CC Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi
CC apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type
CC I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During
CC virion morphogenesis, this protein probably accumulates in the
CC endosomes and trans-Golgi where secondary envelopment occurs. It is
CC probably transported to the cell surface from where it is endocytosed
CC and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-
CC Rule:MF_04032}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
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DR EMBL; AY372243; AAQ73706.1; -; Genomic_DNA.
DR RefSeq; NP_944400.1; NC_005264.1.
DR SMR; Q6UDK4; -.
DR PRIDE; Q6UDK4; -.
DR GeneID; 2656973; -.
DR KEGG; vg:2656973; -.
DR Proteomes; UP000006840; Genome.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma 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:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.29.100; -; 1.
DR HAMAP; MF_04032; HSV_GB; 1.
DR InterPro; IPR035377; Glycoprot_B_PH1.
DR InterPro; IPR035381; Glycoprot_B_PH2.
DR InterPro; IPR038631; Glycoprot_B_PH2_sf.
DR InterPro; IPR000234; Herpes_Glycoprot_B.
DR Pfam; PF17416; Glycoprot_B_PH1; 1.
DR Pfam; PF17417; Glycoprot_B_PH2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Host cell membrane; Host endosome;
KW Host Golgi apparatus; Host membrane; Host-virus interaction; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..30
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 31..911
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000406813"
FT TOPO_DOM 31..778
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 800..911
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 143..149
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 228..233
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 591..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..776
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 86..543
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 103..499
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 177..239
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 330..378
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 566..635
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 911 AA; 101121 MW; 372AF533CC3B676D CRC64;
MRVCSEASPR RRQVTMLVSL LLFSAQAGFC ARSAAGHSGI LSLGDPAASG SALGAAEDVG
DITFAEAVNS AAFDTSAIFE NKLYACSTPN GASVVRLAQP RKCHKYTDST NMTEGIAVTF
KQNIAPLIFN ATLYYKHITT VTTWKGFGLA QITNEYRTRV NIGFGEIKED IDGKGECVTR
AAYNRNKVVY EAYDNDVYGV YKPLVPTLLR SPSTRSFHTT NVTQRRTALG YRTSTTVDCV
VEYMQARSVY PYTYFGLATG NTLEISPFYK SSDKHSRYNL YAEDRVYEAL GYQARDLETR
VLAPPHNRNF VFEDEFTVAW DQMDETTTAC TMAKWLEIPE AVRVSYNKSF HFNFKDLTAT
LVASKTPFNI SRLHLGGCVP RIANETIEAI YGKKYKNTHV RSGGIEYYLA NGGFLIAFQR
LVSNDLAELY LDEAARQNHS AVSRSKRAAP SGGGSILSGP AGDLINTHTS ATFAMLQFTY
DKIQKHVNML IGNLLEAWCE MQNRQLVVWH EIKKLNPASL MTSMYGHAVA ARLLGDVLAV
SKCLEIPIEN VVMQDSMRVP GDPSMCYVRP VLVFKYPAAA DSEAMRGRVA RPANNSDVGG
SQQAGEAEAQ QHVGVHGQLG EHNEILHGRT LIEPCKASHR RYFLFGANYL LYEDYKFIRQ
VNASEIEEIS STFVNLDVTL LEDLDFVPLA VYTREELRDV GTLNYDEVVR YNNLYNKMFR
DLDTALKFDD GLATLRAIGE FLTNTLGGAG KVLGNVVMGA AAAIISTVSG ISSFLANPFA
ALGIGIAVIV CVIMGLLAFR YVMTLRANPV QTLFPGIIDV GEKARQHATV RKDEDASDKE
LAERVLRGLE ILSFESEVRK RREKAAASAK STLAKRIGQF LRHRKTSTKD DTRKLLKTFD
DEDYYYDDEH L
