UL128_HCMVA
ID UL128_HCMVA Reviewed; 171 AA.
AC P16837; Q7M6S2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Uncharacterized protein UL128;
GN Name=UL128;
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 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 [3]
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 [4]
RP X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS), AND INTERACTION WITH GL; GH; UL130
RP AND UL131A.
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. Mechanistically,
CC engages host receptor(s) including neurophilin 2/NRP2 to mediate
CC infection. Additionally, monomeric UL128 may interfere with certain
CC inflammatory cytokines to increase infection and dissemination by
CC blocking monocytes migration. {ECO:0000250|UniProtKB:V9LLX6}.
CC -!- SUBUNIT: Forms the envelope pentamer complex (PC) composed of gH, gL,
CC UL128, UL130, and UL131A (PubMed:28783665). The pentamer interacts with
CC host NRP2 (By similarity). {ECO:0000250|UniProtKB:V9LLX6,
CC ECO:0000269|PubMed:28783665}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:V9LLX6}.
CC Note=Found as a pentameric complex at the surface of virion envelope.
CC {ECO:0000250|UniProtKB:V9LLX6}.
CC -!- SIMILARITY: Belongs to the HHV-5 UL128 protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35330.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; X17403; CAA35330.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK000394; DAA00114.1; -; Genomic_DNA.
DR PIR; S09894; S09894.
DR PDB; 5VOB; X-ray; 3.02 A; C=1-171.
DR PDB; 5VOC; X-ray; 3.99 A; C=1-171.
DR PDB; 5VOD; X-ray; 5.90 A; C=1-171.
DR PDB; 7KBB; EM; 4.02 A; C=28-171.
DR PDB; 7M22; EM; 3.65 A; C=28-171.
DR PDB; 7M30; EM; 3.81 A; C=28-171.
DR PDBsum; 5VOB; -.
DR PDBsum; 5VOC; -.
DR PDBsum; 5VOD; -.
DR PDBsum; 7KBB; -.
DR PDBsum; 7M22; -.
DR PDBsum; 7M30; -.
DR SMR; P16837; -.
DR PRIDE; P16837; -.
DR ABCD; P16837; 1 sequenced antibody.
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 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;
KW Viral attachment to host cell; Viral attachment to host entry receptor;
KW Virion; Virus entry into host cell.
FT CHAIN 1..171
FT /note="Uncharacterized protein UL128"
FT /id="PRO_0000115363"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:5VOB"
SQ SEQUENCE 171 AA; 19747 MW; 1E2A70A913F49098 CRC64;
MSPKDLTPFL TTLWLLLGHS RVPRVRAEEC CEFINVNHPP ERCYDFKMCN RFTVALRCPD
GEVCYSPEKT AEIRGIVTTM THSLTRQVVH NKLTSCNYNP LYLEADGRIR CGKVNDKAQY
LLGAAGSVPY RWINLEYDKI TRIVGLDQYL ESVKKHKRLD VCRAKMGYML Q
