U24_HHV6U
ID U24_HHV6U Reviewed; 87 AA.
AC Q69559; Q69048;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 67.
DE RecName: Full=U24 protein;
GN Name=U24; Synonyms=EoLF1;
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).
RN [3]
RP FUNCTION.
RC STRAIN=GS;
RX PubMed=17977973; DOI=10.1128/jvi.01571-07;
RA Sullivan B.M., Coscoy L.;
RT "Downregulation of the T-cell receptor complex and impairment of T-cell
RT activation by human herpesvirus 6 u24 protein.";
RL J. Virol. 82:602-608(2008).
RN [4]
RP FUNCTION, MUTAGENESIS OF 8-PRO--TYR-11; 7-PRO--PRO-9 AND 53-ARG--ARG-55,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=GS;
RX PubMed=19923186; DOI=10.1128/jvi.01775-09;
RA Sullivan B.M., Coscoy L.;
RT "The U24 protein from human herpesvirus 6 and 7 affects endocytic
RT recycling.";
RL J. Virol. 84:1265-1275(2010).
RN [5]
RP PHOSPHORYLATION AT THR-6, AND INTERACTION WITH NEDD4 WW DOMAINS.
RX PubMed=28051106; DOI=10.1038/srep39776;
RA Sang Y., Zhang R., Scott W.R., Creagh A.L., Haynes C.A., Straus S.K.;
RT "U24 from Roseolovirus interacts strongly with Nedd4 WW Domains.";
RL Sci. Rep. 7:39776-39776(2017).
RN [6]
RP INTERACTION WITH HOST ITCH, DOMAIN, AND MUTAGENESIS OF TYR-11.
RX PubMed=29535361; DOI=10.1038/s41598-018-22682-2;
RA Koshizuka T., Kobayashi T., Ishioka K., Suzutani T.;
RT "Herpesviruses possess conserved proteins for interaction with Nedd4 family
RT ubiquitin E3 ligases.";
RL Sci. Rep. 8:4447-4447(2018).
CC -!- FUNCTION: Down-regulates the TCR/CD3E complex and the transferrin
CC receptor TFRC in host T-cells by blocking them from recycling back to
CC the cell surface. {ECO:0000269|PubMed:17977973,
CC ECO:0000269|PubMed:19923186}.
CC -!- SUBUNIT: Interacts with host ITCH; this interaction probably mediates
CC ITCH degradation (Probable). Interacts probably with NEDD4 (Probable).
CC {ECO:0000305|PubMed:28051106, ECO:0000305|PubMed:29535361}.
CC -!- INTERACTION:
CC Q69559; P28482: MAPK1; Xeno; NbExp=2; IntAct=EBI-8015758, EBI-959949;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19923186}; Single-
CC pass membrane protein {ECO:0000305}.
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle budding. They recruit proteins of the host
CC ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC ESCRT-associated proteins. Contains one L domain: a PPXY motif which is
CC involved in the interaction with Itch, a member of the Nedd4 family.
CC {ECO:0000269|PubMed:29535361}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16731.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L25528; AAA16731.1; ALT_INIT; Genomic_DNA.
DR EMBL; X83413; CAA58404.1; -; Genomic_DNA.
DR PIR; T09318; T09318.
DR RefSeq; NP_042917.1; NC_001664.2.
DR SMR; Q69559; -.
DR IntAct; Q69559; 1.
DR MINT; Q69559; -.
DR iPTMnet; Q69559; -.
DR PRIDE; Q69559; -.
DR DNASU; 1487899; -.
DR GeneID; 1487899; -.
DR KEGG; vg:1487899; -.
DR Proteomes; UP000009295; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..87
FT /note="U24 protein"
FT /id="PRO_0000342579"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 8..11
FT /note="PPXY motif"
FT /evidence="ECO:0000269|PubMed:29535361"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:28051106"
FT MUTAGEN 7..9
FT /note="PPP->AAA: Complete loss of the ability to down-
FT regulate the TCR complex."
FT /evidence="ECO:0000269|PubMed:19923186"
FT MUTAGEN 8..11
FT /note="PPSY->AAA: Complete loss of the ability to down-
FT regulate the TCR complex."
FT /evidence="ECO:0000269|PubMed:19923186"
FT MUTAGEN 11
FT /note="Y->A: Complete loss of interaction with host ITCH."
FT /evidence="ECO:0000269|PubMed:29535361"
FT MUTAGEN 53..55
FT /note="RRK->QQQ: Almost complete loss of the ability to
FT down-regulate the TCR complex."
FT /evidence="ECO:0000269|PubMed:19923186"
SQ SEQUENCE 87 AA; 10091 MW; 494C1B4088A5C923 CRC64;
MDPPRTPPPS YSEVLMMDVM CGQVSPHVIN DTSFVECIPP PQSRPAWNLW NNRRKTFSFL
VLTGLAIAMI LFIVFVLYVF HVNRQRR
