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GO_HCMVA
ID   GO_HCMVA                Reviewed;         466 AA.
AC   P16750; Q7M6L8;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   29-SEP-2021, entry version 60.
DE   RecName: Full=Glycoprotein O;
DE            Short=gO;
DE   Flags: Precursor;
GN   Name=GO; Synonyms=UL74;
OS   Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=10360;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA   Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA   Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA   Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT   "Analysis of the protein-coding content of the sequence of human
RT   cytomegalovirus strain AD169.";
RL   Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 189-195, SUBCELLULAR LOCATION, CHARACTERIZATION,
RP   GLYCOSYLATION, AND IDENTIFICATION IN A COMPLEX WITH GL AND GH.
RX   PubMed=9733861; DOI=10.1128/jvi.72.10.8191-8197.1998;
RA   Huber M.T., Compton T.;
RT   "The human cytomegalovirus UL74 gene encodes the third component of the
RT   glycoprotein H-glycoprotein L-containing envelope complex.";
RL   J. Virol. 72:8191-8197(1998).
RN   [3]
RP   GENOME REANNOTATION.
RX   PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA   Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA   McGeoch D.J., Hayward G.S.;
RT   "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT   cytomegalovirus genome.";
RL   J. Gen. Virol. 84:17-28(2003).
RN   [4]
RP   ERRATUM OF PUBMED:12533697.
RA   Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA   McGeoch D.J., Hayward G.S.;
RL   J. Gen. Virol. 84:1053-1053(2003).
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004;
RA   Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA   Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA   Shenk T., Smith R.D., Nelson J.A.;
RT   "Identification of proteins in human cytomegalovirus (HCMV) particles: the
RT   HCMV proteome.";
RL   J. Virol. 78:10960-10966(2004).
RN   [6]
RP   ERRATUM OF PUBMED:15452216.
RA   Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA   Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA   Shenk T., Smith R.D., Nelson J.A.;
RL   J. Virol. 78:13395-13395(2004).
CC   -!- FUNCTION: Plays a role in viral entry into host cells. Forms a trimeric
CC       complex at the surface of the viral envelope together with gH and gL.
CC       This complex is required for entry in host fibroblasts.
CC       Mechanistically, engages host receptor(s) including PDGFRA to mediate
CC       infection. {ECO:0000250|UniProtKB:F5HGP1}.
CC   -!- SUBUNIT: Forms the envelope trimer complex composed of gH, gL, and gO.
CC       The trimer interacts with host PDGFRA. {ECO:0000250|UniProtKB:F5HGP1}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305|PubMed:9733861}.
CC       Note=Host membrane associated, either via its interaction with gH, or
CC       as a type II transmembrane protein. {ECO:0000305}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9733861}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the herpesviridae U47 family. {ECO:0000305}.
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DR   EMBL; X17403; CAA35389.1; -; Genomic_DNA.
DR   EMBL; BK000394; DAA00170.1; -; Genomic_DNA.
DR   PIR; S09837; S09837.
DR   SMR; P16750; -.
DR   Proteomes; UP000008991; Genome.
DR   Proteomes; UP000008992; Genome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR012564; Herpes_UL74.
DR   Pfam; PF07982; Herpes_UL74; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Membrane; Reference proteome;
KW   Signal; Virion.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..466
FT                   /note="Glycoprotein O"
FT                   /id="PRO_0000038318"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        399
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   466 AA;  54235 MW;  20B931D97AB5D41D CRC64;
     MGRKEMMVRD VPKMVFLISI SFLLVSFINC KVMSKALYNR PWRGLVLSKI GKYKLDQLKL
     EILRQLETTI STKYNVSKQP VKNLTMNMTE FPQYYILAGP IQNYSITYLW FDFYSTQLRK
     PAKYVYSQYN HTAKTITFRP PPCGTVPSMT CLSEMLNVSK RNDTGEQGCG NFTTFNPMFF
     NVPRWNTKLY VGPTKVNVDS QTIYFLGLTA LLLRYAQRNC THSFYLVNAM SRNLFRVPKY
     INGTKLKNTM RKLKRKQAPV KEQFEKKAKK TQSTTTPYFS YTTSAALNVT TNVTYSITTA
     ARRVSTSTIA YRPDSSFMKS IMATQLRDLA TWVYTTLRYR QNPFCEPSRN RTAVSEFMKN
     THVLIRNETP YTIYGTLDMS SLYYNETMFV ENKTASDSNK TTPTSPSMGF QRTFIDPLWD
     YLDSLLFLDE IRNFSLRSPT YVNLTPPEHR RAVNLSTLNS LWWWLQ
 
 
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