ID   UL11P_HCMVA             Reviewed;         275 AA.
AC   P16721; Q7M6T3;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   02-JUN-2021, entry version 66.
DE   RecName: Full=Protein UL11;
DE   Flags: Precursor;
GN   Name=UL11;
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   NUCLEOTIDE SEQUENCE, AND SUBCELLULAR LOCATION.
RX   PubMed=9267452; DOI=10.1007/s007050050169;
RA   Hitomi S., Kozuka-Hata Z., Chen S., Sugano S., Yamaguchi N., Watanabe S.;
RT   "Human cytomegalovirus open reading frame UL11 encodes a highly polymorphic
RT   protein expressed on the infected cell surface.";
RL   Arch. Virol. 142:1407-1427(1997).
RN   [3]
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   [4]
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).
CC   -!- FUNCTION: Plays a role in the modulation of host immune response by
CC       modulating T-cell function. Interacts with host PTPRC/CD45 and thereby
CC       reduces host TCR signaling and T-cell proliferation.
CC       {ECO:0000250|UniProtKB:Q6SWB9}.
CC   -!- SUBUNIT: Interacts with host PTPRC; this interaction affects T-cell
CC       signaling. {ECO:0000250|UniProtKB:Q6SWB9}.
CC   -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000269|PubMed:9267452};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6SWB9}.
CC       Host endoplasmic reticulum {ECO:0000250|UniProtKB:Q6SWB9}.
CC       Note=Localizes to the host cell membrane when highly glycosylated while
CC       less glycosylated forms are found on the endoplasmic reticulum.
CC       {ECO:0000250|UniProtKB:Q6SWB9}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q6SWB9}.
CC   -!- SIMILARITY: Belongs to the RL11 family. {ECO:0000305}.
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DR   EMBL; X17403; CAA35444.1; -; Genomic_DNA.
DR   EMBL; D66905; BAA24102.1; -; mRNA.
DR   EMBL; BK000394; DAA00101.1; -; Genomic_DNA.
DR   PIR; S09774; S09774.
DR   SMR; P16721; -.
DR   Proteomes; UP000008991; Genome.
DR   Proteomes; UP000008992; Genome.
DR   GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Host cell membrane; Host endoplasmic reticulum;
KW   Host membrane; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..275
FT                   /note="Protein UL11"
FT                   /id="PRO_0000037449"
FT   TOPO_DOM        32..227
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        249..275
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          145..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   275 AA;  31381 MW;  D7230EECCC7827D3 CRC64;
     MLLRYITFHR EKVLYLAIAC FFGIYISFHD ACILVPAKVG TNVTLNAVHV HDGDYVYWSF
     GGGGANRLMC RYTPRLDEIH KNTNRSFSCL TNHSLLLINV TEEYTDYYRT MTTFVHQSHN
     WHNHGNKWTL DTCYYVYVTQ NGTLPTTTTK KPTTTTRTTT TTTTKKTTTT STTTTTTTTK
     KTTTSTTHHR HSNPKESTTP KTHVELHVGL GATAAETPLQ PSPQYQHVAT HALWVLAVVI
     VIIIIIIFYF RIPQKLWLLW QHDKHGIVLI PQTDL