ID   UL20_HCMVA              Reviewed;         340 AA.
AC   P16758; Q7M6R2;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   23-FEB-2022, entry version 67.
DE   RecName: Full=Uncharacterized protein UL20;
DE   Flags: Precursor;
GN   Name=UL20;
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   SUBCELLULAR LOCATION.
RX   PubMed=21689255; DOI=10.1111/j.1600-0854.2011.01236.x;
RA   Jelcic I., Reichel J., Schlude C., Treutler E., Sinzger C., Steinle A.;
RT   "The polymorphic HCMV glycoprotein UL20 is targeted for lysosomal
RT   degradation by multiple cytoplasmic dileucine motifs.";
RL   Traffic 12:1444-1456(2011).
CC   -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC       {ECO:0000305|PubMed:21689255}; Single-pass type I membrane protein
CC       {ECO:0000305|PubMed:21689255}. Note=Does not reach the host cell
CC       surface but is rapidely targeted to endosomes and lysosomes.
CC   -!- SIMILARITY: Belongs to the HHV-5 UL20 protein family. {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; CAA35419.1; -; Genomic_DNA.
DR   EMBL; BK000394; DAA00124.1; -; Genomic_DNA.
DR   PIR; S09783; QQBES6.
DR   Proteomes; UP000008991; Genome.
DR   Proteomes; UP000008992; Genome.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR035142; UL20.
DR   Pfam; PF17582; UL20; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Host endoplasmic reticulum; Host membrane; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..340
FT                   /note="Uncharacterized protein UL20"
FT                   /id="PRO_0000037453"
FT   TOPO_DOM        26..225
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..340
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        54
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        68
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   340 AA;  38702 MW;  C29697EE0BCFA433 CRC64;
     MLGIRAMLVM LDYYWIQLIT NNDTRSNNTD TIFVSLLTGA NGVTRTAIGG LHSNYTNLTE
     AFRFTPANTT TNSSTEGNWS VTNLTESCIN RGESYLTTIW LLNCADNNTY WYSGNAYNHT
     IDTCKNTVSG YLFFGMCQLW KDWVTNASHD TVRIQSLGNE IRCMLLPRQY TLNATVEWYN
     KSEGDVPEEF MDYVILTPLA VLTCGLQEAY ILDKGRRYMY LFSVSCAGIT GTVSIILVSL
     SLLILICYYR CGRLLICPRG FELLPEFTEE EEEKEKLLTY KDIEVQVPIR TRRLLVPWIR
     ESKMWVLPPP LPPRPPHLIE FPPSPPPSPG PMHMVVCMPA