ID   U21_HHV7J               Reviewed;         430 AA.
AC   P60505; Q69503;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=U21 glycoprotein;
GN   Name=U21;
OS   Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=57278;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA   Nicholas J.;
RT   "Determination and analysis of the complete nucleotide sequence of human
RT   herpesvirus.";
RL   J. Virol. 70:5975-5989(1996).
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   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the herpesviridae U21 family. {ECO:0000305}.
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DR   EMBL; U43400; AAC54683.1; -; Genomic_DNA.
DR   PIR; T41923; T41923.
DR   RefSeq; YP_073761.1; NC_001716.2.
DR   PRIDE; P60505; -.
DR   DNASU; 3289479; -.
DR   GeneID; 3289479; -.
DR   KEGG; vg:3289479; -.
DR   Proteomes; UP000009246; 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..430
FT                   /note="U21 glycoprotein"
FT                   /id="PRO_0000116357"
FT   TOPO_DOM        1..362
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        384..430
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        31
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"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   430 AA;  49571 MW;  BCCCAF674543AF94 CRC64;
     MWTILLFCVP VIYGELYPDF CPLAVVDFDV NATVDDLLLF DISLSKQCSD DKIRHSAVAA
     MTDNAFFFGN SETQIETDFG KYLAFNCYQV FSTLNHFLFK NFKKTKGLMK RYDKLCLDVE
     SYIHIQIICS PFKSFIRLRR MNETGISPRI LETTFYLQNK RNSTWVAIKN YLGEDDPFTY
     RIWHTLTHAK NFLINSCEND FNQLFFWQRK YLSLAKTFEA TFKQGFNPMI EQRNEQRYRT
     NNIDCSFSKF RQNGVKVAVC KYTGWGVSGF GSLEVLQKIK SPFGEEWKRV GFNSTGAFTP
     LYGSDVLWGL IFLRVEMTTY VCTCTNKNTG TQIQVTLPDV DLDLLDSEKT SSNVFVDMLC
     YTLIAILFLA FVTAVVLLGV SCLDGVQKVL TWPLQHIQKE PVSEKIINLT NLMFGQEPLP
     KKESLKQQCL