UL11P_HCMVM
ID UL11P_HCMVM Reviewed; 272 AA.
AC Q6SWB9; D2K3I1;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 58.
DE RecName: Full=Protein UL11;
DE Flags: Precursor;
GN Name=UL11;
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, INTERACTION WITH HOST PTPRC, AND SUBCELLULAR LOCATION.
RX PubMed=22174689; DOI=10.1371/journal.ppat.1002432;
RA Gabaev I., Steinbrueck L., Pokoyski C., Pich A., Stanton R.J.,
RA Schwinzer R., Schulz T.F., Jacobs R., Messerle M., Kay-Fedorov P.C.;
RT "The human cytomegalovirus UL11 protein interacts with the receptor
RT tyrosine phosphatase CD45, resulting in functional paralysis of T cells.";
RL PLoS Pathog. 7:E1002432-E1002432(2011).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=25275132; DOI=10.1128/jvi.01691-14;
RA Gabaev I., Elbasani E., Ameres S., Steinbrueck L., Stanton R., Doering M.,
RA Lenac Rovis T., Kalinke U., Jonjic S., Moosmann A., Messerle M.;
RT "Expression of the human cytomegalovirus UL11 glycoprotein in viral
RT infection and evaluation of its effect on virus-specific CD8 T cells.";
RL J. Virol. 88:14326-14339(2014).
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:0000269|PubMed:22174689, ECO:0000269|PubMed:25275132}.
CC -!- SUBUNIT: Interacts with host PTPRC; this interaction affects T-cell
CC signaling. {ECO:0000269|PubMed:22174689}.
CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000269|PubMed:22174689};
CC Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic
CC reticulum {ECO:0000269|PubMed:25275132}. Note=Localizes to the host
CC cell membrane when highly glycosylated while less glycosylated forms
CC are found on the endoplasmic reticulum.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:25275132}.
CC -!- SIMILARITY: Belongs to the RL11 family. {ECO:0000305}.
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DR EMBL; AY446894; AAR31577.1; -; Genomic_DNA.
DR RefSeq; YP_081471.1; NC_006273.2.
DR PRIDE; Q6SWB9; -.
DR DNASU; 3077560; -.
DR GeneID; 3077560; -.
DR KEGG; vg:3077560; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Proteomes; UP000000938; 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.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein 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..272
FT /note="Protein UL11"
FT /id="PRO_0000418313"
FT TOPO_DOM 32..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 142..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..180
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 93
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 272 AA; 30881 MW; 50B9D252EB1EC5DB CRC64;
MLFRYITFHR EKVLYLTAAC IFGVYISLHD ACIPVVGKIG TNVTLNAVDV LPPRDQVRWS
YGPGGQGYML CIFTGTSTTT FNNTRFNFSC LSNYSLLLIN VTTQYSTTYR TMTSLDHWLH
QRHNHGSRWT LDTCYNLTVN ENGTFPTTTT KKPTTTTRTT TTTTQRTTTT RTTTTAKKTT
ISTTHHKHPS PKKSTTPNSH VEHHVGFEAT AAETPLQPSP QHQHLATHAL WVLAVVIVII
IIIIFYFRIP QKLWLLWQHD KHGIVLIPQT DL
