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Database: UniProt
Entry: Q2VSK3_9GAMA
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Original site: Q2VSK3_9GAMA 
ID   Q2VSK3_9GAMA            Unreviewed;        61 AA.
AC   Q2VSK3;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   07-OCT-2020, entry version 36.
DE   RecName: Full=Cytoplasmic envelopment protein 3 {ECO:0000256|HAMAP-Rule:MF_04042};
GN   ORFNames=OvHV-2gp35 {ECO:0000313|EMBL:ABB22255.1};
OS   Ovine gammaherpesvirus 2.
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Macavirus.
OX   NCBI_TaxID=10398 {ECO:0000313|EMBL:AAX58073.1, ECO:0000313|Proteomes:UP000153759};
RN   [1] {ECO:0000313|Proteomes:UP000153759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8352654; DOI=10.1007/BF01309849;
RA   Baxter S.I., Pow I., Bridgen A., Reid H.W.;
RT   "PCR detection of the sheep-associated agent of malignant catarrhal
RT   fever.";
RL   Arch. Virol. 132:145-159(1993).
RN   [2] {ECO:0000313|Proteomes:UP000153759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9557713;
RA   Rovnak J., Quackenbush S.L., Reyes R.A., Baines J.D., Parrish C.R.,
RA   Casey J.W.;
RT   "Detection of a novel bovine lymphotropic herpesvirus.";
RL   J. Virol. 72:4237-4242(1998).
RN   [3] {ECO:0000313|Proteomes:UP000153759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11602790;
RA   Dunowska M., Letchworth G.J., Collins J.K., DeMartini J.C.;
RT   "Ovine herpesvirus-2 glycoprotein B sequences from tissues of ruminant
RT   malignant catarrhal fever cases and healthy sheep are highly conserved.";
RL   J. Gen. Virol. 82:2785-2790(2001).
RN   [4] {ECO:0000313|Proteomes:UP000153759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11311431; DOI=10.1016/S0168-1702(00)00252-5;
RA   Chmielewicz B., Goltz M., Ehlers B.;
RT   "Detection and multigenic characterization of a novel gammaherpesvirus in
RT   goats.";
RL   Virus Res. 75:87-94(2001).
RN   [5] {ECO:0000313|Proteomes:UP000153759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11842248;
RA   Coulter L.J., Reid H.W.;
RT   "Isolation and expression of three open reading frames from ovine
RT   herpesvirus-2.";
RL   J. Gen. Virol. 83:533-543(2002).
RN   [6] {ECO:0000313|Proteomes:UP000153759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12466476;
RA   Rosbottom J., Dalziel R.G., Reid H.W., Stewart J.P.;
RT   "Ovine herpesvirus 2 lytic cycle replication and capsid production.";
RL   J. Gen. Virol. 83:2999-3002(2002).
RN   [7] {ECO:0000313|EMBL:ABB22255.1, ECO:0000313|Proteomes:UP000152762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17170434; DOI=10.1099/vir.0.82285-0;
RA   Taus N.S., Herndon D.R., Traul D.L., Stewart J.P., Ackermann M., Li H.,
RA   Knowles D.P., Lewis G.S., Brayton K.A.;
RT   "Comparison of ovine herpesvirus 2 genomes isolated from domestic sheep
RT   (Ovis aries) and a clinically affected cow (Bos bovis).";
RL   J. Gen. Virol. 88:40-45(2007).
RN   [8] {ECO:0000313|EMBL:AAX58073.1, ECO:0000313|Proteomes:UP000153759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BJ1035 {ECO:0000313|EMBL:AAX58073.1};
RX   PubMed=19249164; DOI=10.1016/j.vetmic.2009.01.030;
RA   Meier-Trummer C.S., Tobler K., Hilbe M., Stewart J.P., Hart J.,
RA   Campbell I., Haig D.M., Glauser D.L., Ehrensperger F., Ackermann M.;
RT   "Ovine herpesvirus 2 structural proteins in epithelial cells and M-cells of
RT   the appendix in rabbits with malignant catarrhal fever.";
RL   Vet. Microbiol. 137:235-242(2009).
RN   [9] {ECO:0000313|EMBL:AAX58073.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BJ1035 {ECO:0000313|EMBL:AAX58073.1};
RA   Stewart J.P., Rosbottom J., Haig D.M., Ackermann M.;
RT   "Ovine herpesvirus 2 contains a functional spliced IL-10.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [10] {ECO:0000313|EMBL:AAX58073.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BJ1035 {ECO:0000313|EMBL:AAX58073.1};
RA   Stewart J.P., Rosbottom J.;
RT   "Ovine Herpesvirus 2 Lytic Cycle Replication and Particle Production.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [11] {ECO:0000313|EMBL:AAX58073.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BJ1035 {ECO:0000313|EMBL:AAX58073.1};
RA   Stewart J.P., Rosbottom J., Jayawardane G., Reid H., Ackermann M.;
RT   "Primary structure of the Ovine herpesvirus 2 genome.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in the cytoplasmic envelopment of
CC       tegument proteins and capsids during the assembly and egress processes.
CC       Participates also in viral entry at the fusion step probably by
CC       regulating the core fusion machinery. {ECO:0000256|HAMAP-
CC       Rule:MF_04042}.
CC   -!- SUBUNIT: Interacts with cytoplasmic envelopment protein 2; this
CC       interaction is essential for the proper localization of each protein to
CC       the assembly complex and thus for the production of infectious virus.
CC       {ECO:0000256|HAMAP-Rule:MF_04042}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000256|HAMAP-
CC       Rule:MF_04042}. Virion membrane {ECO:0000256|HAMAP-Rule:MF_04042};
CC       Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04042}. Host cell membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04042}; Lipid-anchor {ECO:0000256|HAMAP-
CC       Rule:MF_04042}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_04042}.
CC       Host Golgi apparatus membrane {ECO:0000256|HAMAP-Rule:MF_04042}; Lipid-
CC       anchor {ECO:0000256|HAMAP-Rule:MF_04042}; Cytoplasmic side
CC       {ECO:0000256|HAMAP-Rule:MF_04042}. Note=Virion membrane-associated
CC       tegument protein. Associates with host membrane lipids rafts. 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:0000256|HAMAP-
CC       Rule:MF_04042}.
CC   -!- PTM: Myristoylation and palmitoylation (probably on one or more of the
CC       nearby cysteines at the N-terminus) enable membrane-binding and Golgi
CC       apparatus-specific targeting and are essential for efficient packaging.
CC       {ECO:0000256|HAMAP-Rule:MF_04042}.
CC   -!- PTM: Phosphorylated. Phosphorylation does not seem to be required for
CC       recycling to the host Golgi apparatus. Packaging is selective for
CC       underphosphorylated forms. {ECO:0000256|HAMAP-Rule:MF_04042}.
CC   -!- SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment
CC       protein 3 family. {ECO:0000256|HAMAP-Rule:MF_04042}.
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DR   EMBL; AY839756; AAX58073.1; -; Genomic_DNA.
DR   EMBL; DQ198083; ABB22255.1; -; Genomic_DNA.
DR   RefSeq; YP_438161.1; NC_007646.1.
DR   GeneID; 26684014; -.
DR   KEGG; vg:26684014; -.
DR   Proteomes; UP000152762; Genome.
DR   Proteomes; UP000153759; Genome.
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:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046760; P:viral budding from Golgi membrane; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04042; HSV_CEP3_gammahv; 1.
DR   InterPro; IPR024360; Herpesvirus_UL11_homo.
DR   Pfam; PF10813; DUF2733; 1.
PE   3: Inferred from homology;
KW   Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04042};
KW   Host Golgi apparatus {ECO:0000256|ARBA:ARBA00022812, ECO:0000256|HAMAP-
KW   Rule:MF_04042}; Host membrane {ECO:0000256|HAMAP-Rule:MF_04042};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW   Rule:MF_04042};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04042};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707, ECO:0000256|HAMAP-Rule:MF_04042};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_04042};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_04042}; Reference proteome {ECO:0000313|Proteomes:UP000152762};
KW   Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04042};
KW   Virion tegument {ECO:0000256|ARBA:ARBA00022580, ECO:0000256|HAMAP-
KW   Rule:MF_04042}.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04042"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04042"
SQ   SEQUENCE   61 AA;  6838 MW;  AA014C924E5349BE CRC64;
     MGAYLSVCCR RHHPVIDMHG NQIDVAKDFE EFTESDELLS EINAAGSQKP LPDYSDNLSQ
     D
//
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