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Database: UniProt
Entry: O41955_MHV68
LinkDB: O41955_MHV68
Original site: O41955_MHV68 
ID   O41955_MHV68            Unreviewed;        75 AA.
AC   O41955;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   02-DEC-2020, entry version 73.
DE   RecName: Full=Cytoplasmic envelopment protein 3 {ECO:0000256|HAMAP-Rule:MF_04042};
GN   Name=GAMMAHV.ORF38 {ECO:0000313|EMBL:AAB66407.1};
GN   Synonyms=38 {ECO:0000313|EMBL:AAF19303.1};
OS   Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=33708 {ECO:0000313|EMBL:AAB66407.1, ECO:0000313|Proteomes:UP000175018};
OH   NCBI_TaxID=10129; Apodemus sylvaticus (European woodmouse).
RN   [1] {ECO:0000313|Proteomes:UP000099649}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8083987;
RA   Stewart J.P., Janjua N.J., Sunil-Chandra N.P., Nash A.A., Arrand J.R.;
RT   "Characterization of murine gammaherpesvirus 68 glycoprotein B (gB)
RT   homolog: similarity to Epstein-Barr virus gB (gp110).";
RL   J. Virol. 68:6496-6504(1994).
RN   [2] {ECO:0000313|Proteomes:UP000099649}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8648686;
RA   Stewart J.P., Janjua N.J., Pepper S.D., Bennion G., Mackett M., Allen T.,
RA   Nash A.A., Arrand J.R.;
RT   "Identification and characterization of murine gammaherpesvirus 68 gp150: a
RT   virion membrane glycoprotein.";
RL   J. Virol. 70:3528-3535(1996).
RN   [3] {ECO:0000313|Proteomes:UP000099649}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8638414; DOI=10.1006/viro.1996.0274;
RA   Pepper S.D., Stewart J.P., Arrand J.R., Mackett M.;
RT   "Murine gammaherpesvirus-68 encodes homologues of thymidine kinase and
RT   glycoprotein H: sequence, expression, and characterization of pyrimidine
RT   kinase activity.";
RL   Virology 219:475-479(1996).
RN   [4] {ECO:0000313|EMBL:AAF19303.1, ECO:0000313|Proteomes:UP000099649}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G2.4 {ECO:0000313|EMBL:AAF19303.1};
RX   PubMed=9191940;
RA   Mackett M., Stewart J.P., de V Pepper S., Chee M., Efstathiou S.,
RA   Nash A.A., Arrand J.R.;
RT   "Genetic content and preliminary transcriptional analysis of a
RT   representative region of murine gammaherpesvirus 68.";
RL   J. Gen. Virol. 78:1425-1433(1997).
RN   [5] {ECO:0000313|Proteomes:UP000099649}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9225045;
RA   Bowden R.J., Simas J.P., Davis A.J., Efstathiou S.;
RT   "Murine gammaherpesvirus 68 encodes tRNA-like sequences which are expressed
RT   during latency.";
RL   J. Gen. Virol. 78:1675-1687(1997).
RN   [6] {ECO:0000313|EMBL:AAB66407.1, ECO:0000313|Proteomes:UP000099649, ECO:0000313|Proteomes:UP000175018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G2.4 {ECO:0000313|EMBL:AAF19303.1}, and WUMS
RC   {ECO:0000313|EMBL:AAB66407.1};
RX   PubMed=9223479;
RA   Virgin H.W.IV., Latreille P., Wamsley P., Hallsworth K., Weck K.E.,
RA   Dal Canto A.J., Speck S.H.;
RT   "Complete sequence and genomic analysis of murine gammaherpesvirus 68.";
RL   J. Virol. 71:5894-5904(1997).
RN   [7] {ECO:0000313|EMBL:AAF19303.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=G2.4 {ECO:0000313|EMBL:AAF19303.1};
RA   Milligan S., Efstathiou S., Stewart J.P., Nash A.A., Davison A.J.;
RT   "Genetic content of murine gammaherpesviruses.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:AAB66407.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WUMS {ECO:0000313|EMBL:AAB66407.1};
RA   Lynn T., Virgin H.W.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:ACV65516.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4556 {ECO:0000313|EMBL:ACV65516.1};
RA   Halasova Z., Valovicova M., Belvoncikova P., Pancik P., Rezuchova I.,
RA   Kudelova M.;
RT   "Partial sequence and analysis of Murine herpesvirus strain 4556 (MHV4556)
RT   genome.";
RL   Submitted (JUL-2009) 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   -!- INTERACTION:
CC       O41955; O41949: GAMMAHV.ORF33; NbExp=3; IntAct=EBI-9640683, EBI-9640421;
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; U97553; AAB66407.1; -; Genomic_DNA.
DR   EMBL; AF105037; AAF19303.1; -; Genomic_DNA.
DR   EMBL; GQ421305; ACV65516.1; -; Genomic_DNA.
DR   RefSeq; NP_044876.1; NC_001826.2.
DR   DIP; DIP-47234N; -.
DR   IntAct; O41955; 3.
DR   GeneID; 1497164; -.
DR   KEGG; vg:1497164; -.
DR   Proteomes; UP000099649; Genome.
DR   Proteomes; UP000175018; 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   1: Evidence at protein level;
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:UP000099649};
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   REGION          42..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..75
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04042"
SQ   SEQUENCE   75 AA;  8232 MW;  D6811E0DBA9BB03C CRC64;
     MGAAFGCCKK THNPLKDVRG QLIDLTKDFE LISENTGLLV EDPSVGEGHL ELKPKPYGSD
     TDSDTDIEYE RGKHA
//
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