K7_HHV8P
ID K7_HHV8P Reviewed; 126 AA.
AC F5HDA4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 23-FEB-2022, entry version 25.
DE RecName: Full=Protein K7;
GN Name=K7;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [3]
RP FUNCTION, INTERACTION WITH HOST CAMLG, AND SUBCELLULAR LOCATION.
RX PubMed=12388711; DOI=10.1128/jvi.76.22.11491-11504.2002;
RA Feng P., Park J., Lee B.S., Lee S.H., Bram R.J., Jung J.U.;
RT "Kaposi's sarcoma-associated herpesvirus mitochondrial K7 protein targets a
RT cellular calcium-modulating cyclophilin ligand to modulate intracellular
RT calcium concentration and inhibit apoptosis.";
RL J. Virol. 76:11491-11504(2002).
RN [4]
RP FUNCTION, AND INTERACTION WITH PROTEIN ORF74.
RX PubMed=18802460; DOI=10.1371/journal.ppat.1000157;
RA Feng H., Dong X., Negaard A., Feng P.;
RT "Kaposi's sarcoma-associated herpesvirus K7 induces viral G protein-coupled
RT receptor degradation and reduces its tumorigenicity.";
RL PLoS Pathog. 4:E1000157-E1000157(2008).
CC -!- FUNCTION: Plays a role in the inhibition of host apoptosis to allow
CC completion of the viral lytic replication and may thus favor the
CC maintenance of persistent infection in infected host.
CC {ECO:0000269|PubMed:12388711, ECO:0000269|PubMed:18802460}.
CC -!- SUBUNIT: Interacts with host CAMLG; this interaction allows efficient
CC apoptosis inhibition. Additionally, interacts with vGPCR/ORF74 and
CC induces its proteasomeal degradation. {ECO:0000269|PubMed:12388711,
CC ECO:0000269|PubMed:18802460}.
CC -!- INTERACTION:
CC F5HDA4; Q98146: ORF74; NbExp=5; IntAct=EBI-9002986, EBI-7930093;
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Host mitochondrion
CC {ECO:0000269|PubMed:12388711}.
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DR EMBL; AF148805; ABD28865.1; -; Genomic_DNA.
DR RefSeq; YP_001129367.1; NC_009333.1.
DR IntAct; F5HDA4; 1.
DR PRIDE; F5HDA4; -.
DR DNASU; 4961500; -.
DR GeneID; 4961500; -.
DR KEGG; vg:4961500; -.
DR Proteomes; UP000000942; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Host membrane; Host mitochondrion; Host-virus interaction; Membrane;
KW Modulation of host cell apoptosis by virus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..126
FT /note="Protein K7"
FT /id="PRO_0000423844"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 126 AA; 13743 MW; 189A7D9FCEDD91E3 CRC64;
MGTLEIKGAS LSQFSTGTAQ SPWLPLHLWI LCSLLAFLPL LVFIGAADCG LIASLLAIYP
SWLSARFSVL LFPHWPESCS TKNTARSGAL HKPAEQKLRF AQKPCHGNYT VTPCGLLHWI
QSPGQL