U131A_HCMVM
ID U131A_HCMVM Reviewed; 129 AA.
AC F5HET4;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Protein UL131A;
DE Flags: Precursor;
GN Name=UL131A;
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, SUBCELLULAR LOCATION, AND INTERACTION WITH GH.
RC STRAIN=AD169 with UL131A ORF from isolate VR1814;
RX PubMed=16894182; DOI=10.1099/vir.0.81921-0;
RA Adler B., Scrivano L., Ruzcics Z., Rupp B., Sinzger C., Koszinowski U.;
RT "Role of human cytomegalovirus UL131A in cell type-specific virus entry and
RT release.";
RL J. Gen. Virol. 87:2451-2460(2006).
RN [3]
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 [4]
RP FUNCTION.
RC STRAIN=TB40-BAC4;
RX PubMed=22031943; DOI=10.1128/jvi.05354-11;
RA Schuessler A., Sampaio K.L., Straschewski S., Sinzger C.;
RT "Mutational mapping of pUL131A of human cytomegalovirus emphasizes its
RT central role for endothelial cell tropism.";
RL J. Virol. 86:504-512(2012).
RN [5]
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 [6]
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 [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 1-129, 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:17942555). Mechanistically, engages host receptor(s) including
CC neurophilin 2/NRP2 to mediate infection (PubMed:30057110). Contributes
CC to the formation of the complex between UL128, UL130 and gH-gL.
CC {ECO:0000269|PubMed:16894182, ECO:0000269|PubMed:17942555,
CC ECO:0000269|PubMed:22031943, ECO:0000269|PubMed:23853586,
CC ECO:0000269|PubMed:28783665, 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 (PubMed:17942555, PubMed:28783665, PubMed:30057110). The interaction
CC with gH is important for the formation of UL128, UL130, gH-gL complex
CC (PubMed:16894182). {ECO:0000269|PubMed:16894182,
CC ECO:0000269|PubMed:17942555, ECO:0000269|PubMed:28783665,
CC ECO:0000269|PubMed:30057110}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:16894182,
CC ECO:0000269|PubMed:23804643}. Note=Found as a pentameric complex at the
CC surface of virion envelope. {ECO:0000269|PubMed:23804643}.
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DR EMBL; AY446894; AAR31670.1; -; Genomic_DNA.
DR RefSeq; YP_081566.1; NC_006273.2.
DR PDB; 5VOB; X-ray; 3.02 A; E=1-129.
DR PDB; 5VOC; X-ray; 3.99 A; E=1-129.
DR PDB; 5VOD; X-ray; 5.90 A; E=1-129.
DR PDB; 7KBB; EM; 4.02 A; E=19-129.
DR PDB; 7M22; EM; 3.65 A; E=19-129.
DR PDB; 7M30; EM; 3.81 A; E=19-129.
DR PDBsum; 5VOB; -.
DR PDBsum; 5VOC; -.
DR PDBsum; 5VOD; -.
DR PDBsum; 7KBB; -.
DR PDBsum; 7M22; -.
DR PDBsum; 7M30; -.
DR SMR; F5HET4; -.
DR PRIDE; F5HET4; -.
DR ABCD; F5HET4; 1 sequenced antibody.
DR GeneID; 3077493; -.
DR KEGG; vg:3077493; -.
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.
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 Viral envelope protein; Virion; Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..129
FT /note="Protein UL131A"
FT /id="PRO_0000418315"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 46..68
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 115..126
FT /evidence="ECO:0007829|PDB:5VOB"
SQ SEQUENCE 129 AA; 14989 MW; 3488C28116DF2D56 CRC64;
MRLCRVWLSV CLCAVVLGQC QRETAEKNDY YRVPHYWDAC SRALPDQTRY KYVEQLVDLT
LNYHYDASHG LDNFDVLKRI NVTEVSLLIS DFRRQNRRGG TNKRTTFNAA GSLAPHARSL
EFSVRLFAN
