UL130_HCMVM
ID UL130_HCMVM Reviewed; 214 AA.
AC F5HCP3;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 23-FEB-2022, entry version 26.
DE RecName: Full=Envelope glycoprotein UL130;
DE Flags: Precursor;
GN Name=UL130;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
RN [2]
RP FUNCTION, AND INTERACTION WITH GH; GL; UL128 AND UL131A.
RX PubMed=17942555; DOI=10.1128/jvi.01910-07;
RA Ryckman B.J., Rainish B.L., Chase M.C., Borton J.A., Nelson J.A.,
RA Jarvis M.A., Johnson D.C.;
RT "Characterization of the human cytomegalovirus gH/gL/UL128-131 complex that
RT mediates entry into epithelial and endothelial cells.";
RL J. Virol. 82:60-70(2008).
RN [3]
RP FUNCTION.
RX PubMed=23853586; DOI=10.1371/journal.ppat.1003463;
RA Nogalski M.T., Chan G.C., Stevenson E.V., Collins-McMillen D.K.,
RA Yurochko A.D.;
RT "The HCMV gH/gL/UL128-131 complex triggers the specific cellular activation
RT required for efficient viral internalization into target monocytes.";
RL PLoS Pathog. 9:E1003463-E1003463(2013).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=23804643; DOI=10.1128/jvi.01167-13;
RA Zhou M., Yu Q., Wechsler A., Ryckman B.J.;
RT "Comparative analysis of gO isoforms reveals that strains of human
RT cytomegalovirus differ in the ratio of gH/gL/gO and gH/gL/UL128-131 in the
RT virion envelope.";
RL J. Virol. 87:9680-9690(2013).
RN [5]
RP FUNCTION, AND INTERACTION WITH HOST NRP2.
RX PubMed=30057110; DOI=10.1016/j.cell.2018.06.028;
RA Martinez-Martin N., Marcandalli J., Huang C.S., Arthur C.P., Perotti M.,
RA Foglierini M., Ho H., Dosey A.M., Shriver S., Payandeh J., Leitner A.,
RA Lanzavecchia A., Perez L., Ciferri C.;
RT "An Unbiased Screen for Human Cytomegalovirus Identifies Neuropilin-2 as a
RT Central Viral Receptor.";
RL Cell 0:0-0(2018).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 1-214, FUNCTION, AND INTERACTION
RP WITH GH; GL; UL128 AND UL130.
RX PubMed=28783665; DOI=10.1126/sciimmunol.aan1457;
RA Chandramouli S., Malito E., Nguyen T., Luisi K., Donnarumma D., Xing Y.,
RA Norais N., Yu D., Carfi A.;
RT "Structural basis for potent antibody-mediated neutralization of human
RT cytomegalovirus.";
RL Sci. Immunol. 2:0-0(2017).
CC -!- FUNCTION: Plays a role in viral entry into host cells. Forms a
CC pentameric complex at the surface of the viral envelope together with
CC gH, gL, UL130 and UL131. This complex is required for entry in
CC epithelial, endothelial and myeloid host cells (PubMed:23853586,
CC PubMed:28783665, PubMed:17942555). Mechanistically, engages host
CC receptor(s) including neurophilin 2/NRP2 to mediate infection
CC (PubMed:30057110). {ECO:0000269|PubMed:17942555,
CC ECO:0000269|PubMed:23853586, ECO:0000269|PubMed:28783665,
CC ECO:0000269|PubMed:30057110}.
CC -!- SUBUNIT: Forms the envelope pentamer complex (PC) composed of gH, gL,
CC UL128, UL130, and UL131A. The pentamer interacts with host NRP2.
CC {ECO:0000269|PubMed:17942555, ECO:0000269|PubMed:28783665,
CC ECO:0000269|PubMed:30057110}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:23804643}.
CC Note=Found as a pentameric complex at the surface of virion envelope.
CC {ECO:0000269|PubMed:23804643}.
CC -!- SIMILARITY: Belongs to the HHV-5 UL130 protein family. {ECO:0000305}.
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DR EMBL; AY446894; AAR31669.1; -; Genomic_DNA.
DR RefSeq; YP_081565.1; NC_006273.2.
DR PDB; 5VOB; X-ray; 3.02 A; D=1-214.
DR PDB; 5VOC; X-ray; 3.99 A; D=1-214.
DR PDB; 5VOD; X-ray; 5.90 A; D=1-214.
DR PDBsum; 5VOB; -.
DR PDBsum; 5VOC; -.
DR PDBsum; 5VOD; -.
DR SMR; F5HCP3; -.
DR PRIDE; F5HCP3; -.
DR ABCD; F5HCP3; 1 sequenced antibody.
DR DNASU; 3077481; -.
DR GeneID; 3077481; -.
DR KEGG; vg:3077481; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Proteomes; UP000000938; Genome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; TAS:Reactome.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR021038; Herpes_UL130_cytomegalovirus.
DR Pfam; PF11668; Gp_UL130; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host-virus interaction; Membrane; Reference proteome; Signal;
KW Viral attachment to host cell; Viral attachment to host entry receptor;
KW Virion; Virus entry into host cell.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..214
FT /note="Envelope glycoprotein UL130"
FT /id="PRO_0000418314"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 153..165
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 168..182
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 188..198
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:5VOB"
SQ SEQUENCE 214 AA; 24709 MW; E76147BF59E30CF5 CRC64;
MLRLLLRHHF HCLLLCAVWA TPCLASPWST LTANQNPSPP WSKLTYSKPH DAATFYCPFL
YPSPPRSPLQ FSGFQRVSTG PECRNETLYL LYNREGQTLV ERSSTWVKKV IWYLSGRNQT
ILQRMPRTAS KPSDGNVQIS VEDAKIFGAH MVPKQTKLLR FVVNDGTRYQ MCVMKLESWA
HVFRDYSVSF QVRLTFTEAN NQTYTFCTHP NLIV
