U21_HHV6U
ID U21_HHV6U Reviewed; 433 AA.
AC Q69556; Q69045;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Glycoprotein U21;
GN Name=U21; Synonyms=EJLF2;
OS Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=10370;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8289364; DOI=10.1128/jvi.68.2.597-610.1994;
RA Nicholas J., Martin M.E.D.;
RT "Nucleotide sequence analysis of a 38.5-kilobase-pair region of the genome
RT of human herpesvirus 6 encoding human cytomegalovirus immediate-early gene
RT homologs and transactivating functions.";
RL J. Virol. 68:597-610(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT genome evolution.";
RL Virology 209:29-51(1995).
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 herpesviruses U21 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16728.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L25528; AAA16728.1; ALT_INIT; Genomic_DNA.
DR EMBL; X83413; CAA58401.1; -; Genomic_DNA.
DR PIR; T09315; T09315.
DR RefSeq; NP_042914.1; NC_001664.2.
DR PRIDE; Q69556; -.
DR DNASU; 1487967; -.
DR GeneID; 1487967; -.
DR KEGG; vg:1487967; -.
DR Proteomes; UP000009295; 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="Glycoprotein U21"
FT /id="PRO_0000116355"
FT TOPO_DOM 1..364
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 433 AA; 49395 MW; 054834689F77A436 CRC64;
MMICLVFLCV LTLARGEIYP PICPAPGVGN DEAVRAGELL LEISAYRNQR SGRVELWGSA
AVNNQVFYGG MENSQIDYDF GKFLVFRCFQ VFNNVHKLLF NTVSSATMHL ARKRVQKCGH
GKMTFISIQV QCSVNKKSIR LSRMSEASLK KQVLRVAFFL DRNNNSWIAD KNFQGEDRTM
LRLWNELSTY QQYLISSCNN DVKILSELYG EFRQIALPYD EKLNLNFMPV IRSSSERLFR
ADDLKCSFSR WLGAEGEFAV CEYSGWGVSR LGKIEIFAEK PLTFDMAWKT VKMRSSGAYT
SLFRDDVTWG LIPLDKWVGD KYFCMCTNKE SGDNVIVTLP EKNVEKSIQI YDEGSAMLSF
AEMTSIILNL MFMGAVAVSV GILGISCFVG LKEIIYFIFV SVDYMWPFCD TLLTTAVNCF
FKGRTFLRRE LKI