ID   UL116_HCMVA             Reviewed;         314 AA.
AC   P16833; Q9PY28;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Uncharacterized protein UL116;
DE   Flags: Precursor;
GN   Name=UL116;
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   FUNCTION, INTERACTION WITH GH, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC   STRAIN=TR;
RX   PubMed=26937030; DOI=10.1128/jvi.02517-15;
RA   Calo S., Cortese M., Ciferri C., Bruno L., Gerrein R., Benucci B.,
RA   Monda G., Gentile M., Kessler T., Uematsu Y., Maione D., Lilja A.E.,
RA   Carfi A., Merola M.;
RT   "The Human Cytomegalovirus UL116 Gene Encodes an Envelope Glycoprotein
RT   Forming a Complex with gH Independently from gL.";
RL   J. Virol. 90:4926-4938(2016).
RN   [5]
RP   FUNCTION, INTERACTION WITH UL148, AND DISRUPTION PHENOTYPE.
RX   PubMed=33889136; DOI=10.3389/fmicb.2021.630121;
RA   Vezzani G., Amendola D., Yu D., Chandramouli S., Frigimelica E., Maione D.,
RA   Merola M.;
RT   "The Human Cytomegalovirus UL116 Glycoprotein Is a Chaperone to Control gH-
RT   Based Complexes Levels on Virions.";
RL   Front. Microbiol. 12:630121-630121(2021).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH UL148.
RX   PubMed=34011552; DOI=10.1128/jvi.02207-20;
RA   Siddiquey M.N.A., Schultz E.P., Yu Q., Amendola D., Vezzani G., Yu D.,
RA   Maione D., Lanchy J.M., Ryckman B.J., Merola M., Kamil J.P.;
RT   "The Human Cytomegalovirus Protein UL116 Interacts with the Viral
RT   Endoplasmic-Reticulum-Resident Glycoprotein UL148 and Promotes the
RT   Incorporation of gH/gL Complexes into Virions.";
RL   J. Virol. 95:e0220720-e0220720(2021).
CC   -!- FUNCTION: Chaperone protein that cooperates with UL148 to regulate the
CC       abundance of gH complexes in virion (PubMed:33889136, PubMed:26937030).
CC       First interactor of gH in the host endoplasmic reticulum, regulates the
CC       early folding steps of virion assembly. Then, UL148 is recruited and
CC       favors the binding of gL (PubMed:34011552).
CC       {ECO:0000269|PubMed:26937030, ECO:0000269|PubMed:33889136,
CC       ECO:0000269|PubMed:34011552}.
CC   -!- SUBUNIT: Interacts with gH (PubMed:26937030). Interacts with UL148
CC       (PubMed:33889136, PubMed:34011552). {ECO:0000269|PubMed:26937030,
CC       ECO:0000269|PubMed:33889136, ECO:0000269|PubMed:34011552}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:26937030}. Host
CC       endoplasmic reticulum {ECO:0000269|PubMed:26937030}. Note=First
CC       localizes to the cellular site of virus assembly and then inserts into
CC       the virion envelope. {ECO:0000269|PubMed:26937030}.
CC   -!- PTM: Highly glycosylated. {ECO:0000269|PubMed:26937030}.
CC   -!- DISRUPTION PHENOTYPE: Deletion causes infectivity defects of about 10-
CC       fold compared to wild-type virus and leads to reduced expression of
CC       both gH/gL complexes in virions. {ECO:0000269|PubMed:33889136}.
CC   -!- SIMILARITY: Belongs to the HHV-5 UL116 protein family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA35318.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X17403; CAA35318.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK000394; DAA00106.1; -; Genomic_DNA.
DR   PIR; S09883; S09883.
DR   Proteomes; UP000008991; Genome.
DR   Proteomes; UP000008992; Genome.
DR   GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Glycoprotein; Host endoplasmic reticulum; Reference proteome; Signal;
KW   Virion.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..314
FT                   /note="Uncharacterized protein UL116"
FT                   /id="PRO_0000037456"
FT   REGION          47..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   314 AA;  34140 MW;  4935CC9D35CA5994 CRC64;
     MKRRRRWRGW LLFPALCFCL LCEAVETNAT TVTSTTAAAA TTNTTVATTG TTTTSPNVTS
     TTSNTVTTPT TVSSVSNLTS STTSIPISTS TVSGTRNTGN NNTTTIGTNA TSPSPSVSIL
     TTVTPAATST ISVDGVVTAS DYTPTFDDLE NITTTRAPTR PPAQDLCSHN LSIILYEEES
     QSSVDIAVDE EEPELEDDDE YDELWFPLYF EAECNRNYTL HVNHSCDYSV RQSSVSFPPW
     RDIDSVTFVP RNLSNCSAHG LAVIVAGNQT WYVNPFSLAH LLDAIYNVLG IEDLSANFRR
     QLAPYRHTLI VPQT