U21_HHV6Z
ID U21_HHV6Z Reviewed; 433 AA.
AC Q9QJ45;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=U21 glycoprotein;
GN Name=U21;
OS Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=36351;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA Pellett P.E.;
RT "Human herpesvirus 6B genome sequence: coding content and comparison with
RT human herpesvirus 6A.";
RL J. Virol. 73:8040-8052(1999).
CC -!- FUNCTION: Binds to MHC class I molecules in the endoplasmic reticulum
CC and targets them from the Golgi directly to the lysosomes. Once in the
CC lysosomes both proteins are degraded. In consequence, surface class I
CC molecules are down-regulated and infected cells are masked for immune
CC recognition by cytotoxic T lymphocytes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- DOMAIN: The ER-lumenal domain associates with class I MHC molecules and
CC is responsible for lysosomal sorting. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae U21 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD49633.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF157706; AAD49633.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_050201.1; NC_000898.1.
DR PRIDE; Q9QJ45; -.
DR DNASU; 1497017; -.
DR GeneID; 1497017; -.
DR KEGG; vg:1497017; -.
DR Proteomes; UP000006930; 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.
PE 3: Inferred from homology;
KW Glycoprotein; Host endoplasmic reticulum; Host membrane;
KW Host-virus interaction; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Viral immunoevasion.
FT CHAIN 1..433
FT /note="U21 glycoprotein"
FT /id="PRO_0000116356"
FT TOPO_DOM 1..370
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 433 AA; 49499 MW; 05F259FD98EDCD6B CRC64;
MMICFVFLCV LTFVRGEIYP STCPALGAGN GEAVRSGEML LEISAYRNWR SGKMELWGSA
AVNNQVFYGG MEDSQIEYDF GKFLVFRCFQ VFHNVHKLLF NTVSSATMHL ARKRVQKCGH
GKMTFISIQV QCSVNKKSIR LSRMNETNLK KQVLRVAFFL DGSNNSWIAD KNFQGEDRTM
LRLWTELSTY RQYLISSCNN DVKVLSELYG EFRRMALSYD EELKLNFMPV IRSSSERLFR
ADDLKCSFSR WLGAEGEFAV CEYSGWGVSK LGKIEIFAEE PLTFDMVWKT VKMRSSGAYT
SLFRDDVTWG LISLDKWVGD KYFCMCTNKE SGDNVIVTLP EKNVEKSIQI YNEGSTMLAF
AEITSIMVNL MFMGAVAVCV GILGISCFVG LKEIIYFIFV SVNSMWPFCN KLLTTAVNCF
FKGRTFLRRE LKI