位置:首页 > 蛋白库 > GM_HCMVA
GM_HCMVA
ID   GM_HCMVA                Reviewed;         372 AA.
AC   P16733; Q7M6T7;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   23-FEB-2022, entry version 89.
DE   RecName: Full=Envelope glycoprotein M {ECO:0000255|HAMAP-Rule:MF_04035};
DE            Short=gM {ECO:0000255|HAMAP-Rule:MF_04035};
GN   Name=gM {ECO:0000255|HAMAP-Rule:MF_04035}; ORFNames=UL100;
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 [GENOMIC DNA].
RX   PubMed=2547996; DOI=10.1128/jvi.63.9.3792-3800.1989;
RA   Lehner R., Meyer H., Mach M.;
RT   "Identification and characterization of a human cytomegalovirus gene coding
RT   for a membrane protein that is conserved among human herpesviruses.";
RL   J. Virol. 63:3792-3800(1989).
RN   [2]
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   [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).
RN   [7]
RP   SUBUNIT, SUBCELLULAR LOCATION, AND DISULFIDE BOND.
RX   PubMed=11090188; DOI=10.1128/jvi.74.24.11881-11892.2000;
RA   Mach M., Kropff B., Dal Monte P., Britt W.;
RT   "Complex formation by human cytomegalovirus glycoproteins M (gpUL100) and N
RT   (gpUL73).";
RL   J. Virol. 74:11881-11892(2000).
RN   [8]
RP   SUBUNIT, AND DISULFIDE BOND.
RX   PubMed=15681419; DOI=10.1128/jvi.79.4.2160-2170.2005;
RA   Mach M., Kropff B., Kryzaniak M., Britt W.;
RT   "Complex formation by glycoproteins M and N of human cytomegalovirus:
RT   structural and functional aspects.";
RL   J. Virol. 79:2160-2170(2005).
RN   [9]
RP   INTERACTION WITH HOST RAB11FIP4.
RX   PubMed=19761540; DOI=10.1111/j.1600-0854.2009.00967.x;
RA   Krzyzaniak M.A., Mach M., Britt W.J.;
RT   "HCMV-encoded glycoprotein M (UL100) interacts with Rab11 effector protein
RT   FIP4.";
RL   Traffic 10:1439-1457(2009).
CC   -!- FUNCTION: Envelope glycoprotein important for virion assembly and
CC       egress. Plays a role in the correct incorporation of gH-gL into virion
CC       membrane. Directs the glycoprotein N (gN) to the host trans-Golgi
CC       network. {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:11090188,
CC       ECO:0000269|PubMed:15681419, ECO:0000269|PubMed:19761540}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with gN (via N-terminus). The gM-gN
CC       heterodimer forms the gCII complex. Interacts with host RAB11FIP4.
CC       {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:11090188,
CC       ECO:0000269|PubMed:15681419, ECO:0000269|PubMed:19761540}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04035,
CC       ECO:0000305|PubMed:11090188}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000305|PubMed:11090188}. Host
CC       Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-
CC       Rule:MF_04035, ECO:0000305|PubMed:11090188}. Host endosome membrane
CC       {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000305|PubMed:11090188}. Host
CC       nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_04035,
CC       ECO:0000305|PubMed:11090188}. Note=During virion morphogenesis, this
CC       protein accumulates in the trans-Golgi network where secondary
CC       envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
CC   -!- SIMILARITY: Belongs to the herpesviridae glycoprotein M family.
CC       {ECO:0000255|HAMAP-Rule:MF_04035}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M28350; AAA45984.1; -; Genomic_DNA.
DR   EMBL; X17403; CAA35336.1; -; Genomic_DNA.
DR   EMBL; BK000394; DAA00097.1; -; Genomic_DNA.
DR   PIR; S09865; QQBEJ7.
DR   SMR; P16733; -.
DR   Proteomes; UP000008991; Genome.
DR   Proteomes; UP000008992; Genome.
DR   GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0044201; C:host cell nuclear inner 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   HAMAP; MF_04035; HSV_GM; 1.
DR   InterPro; IPR000785; Herpes_glycop_M.
DR   Pfam; PF01528; Herpes_glycop; 1.
DR   PRINTS; PR00333; HSVINTEGRLMP.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Host endosome; Host Golgi apparatus;
KW   Host membrane; Host nucleus; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Viral envelope protein; Virion.
FT   CHAIN           1..372
FT                   /note="Envelope glycoprotein M"
FT                   /id="PRO_0000115785"
FT   TOPO_DOM        1..13
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TOPO_DOM        35..79
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TOPO_DOM        101..126
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TOPO_DOM        148..151
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TOPO_DOM        173..200
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TOPO_DOM        222..239
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TOPO_DOM        261..264
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TOPO_DOM        286..298
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   TOPO_DOM        320..372
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04035"
FT   REGION          348..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        44
FT                   /note="Interchain (with C-90 in gN)"
FT                   /evidence="ECO:0000269|PubMed:11090188,
FT                   ECO:0000269|PubMed:15681419"
SQ   SEQUENCE   372 AA;  42861 MW;  F2F99BEC69BF8E32 CRC64;
     MAPSHVDKVN TRTWSASIVF MVLTFVNVSV HLVLSNFPHL GYPCVYYHVV DFERLNMSAY
     NVMHLHTPML FLDSVQLVCY AVFMQLVFLA VTIYYLVCWI KISMRKDKGM SLNQSTRDIS
     YMGDSLTAFL FILSMDTFQL FTLTMSFRLP SMIAFMAAVH FFCLTIFNVS MVTQYRSYKR
     SLFFFSRLHP KLKGTVQFRT LIVNLVEVAL GFNTTVVAMA LCYGFGNNFF VRTGHMVLAV
     FVVYAIISII YFLLIEAVFF QYVKVQFGYH LGAFFGLCGL IYPIVQYDTF LSNEYRTGIS
     WSFGMLFFIW AMFTTCRAVR YFRGRGSGSV KYQALATASG EEVAVLSHHD SLESRRLREE
     EDDDDDEDFE DA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024