ORF4_HHV8P
ID ORF4_HHV8P Reviewed; 550 AA.
AC Q2HRD4; D0UZL0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 02-JUN-2021, entry version 56.
DE RecName: Full=Complement control protein;
DE Short=KCP;
DE Flags: Precursor;
GN Name=ORF4;
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.
RX PubMed=12477863; DOI=10.1128/jvi.77.1.592-599.2003;
RA Spiller O.B., Robinson M., O'Donnell E., Milligan S., Morgan B.P.,
RA Davison A.J., Blackbourn D.J.;
RT "Complement regulation by Kaposi's sarcoma-associated herpesvirus ORF4
RT protein.";
RL J. Virol. 77:592-599(2003).
RN [4]
RP FUNCTION.
RX PubMed=15304516; DOI=10.1074/jbc.m407558200;
RA Mark L., Lee W.H., Spiller O.B., Proctor D., Blackbourn D.J.,
RA Villoutreix B.O., Blom A.M.;
RT "The Kaposi's sarcoma-associated herpesvirus complement control protein
RT mimics human molecular mechanisms for inhibition of the complement
RT system.";
RL J. Biol. Chem. 279:45093-45101(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16571823; DOI=10.1128/jvi.80.8.4068-4078.2006;
RA Spiller O.B., Mark L., Blue C.E., Proctor D.G., Aitken J.A., Blom A.M.,
RA Blackbourn D.J.;
RT "Dissecting the regions of virion-associated Kaposi's sarcoma-associated
RT herpesvirus complement control protein required for complement regulation
RT and cell binding.";
RL J. Virol. 80:4068-4078(2006).
CC -!- FUNCTION: Inhibits the complement component of the host innate immune
CC response. Regulates host C3 convertases, accelerating their decay, and
CC acts as a cofactor for factor I degradation of C4b and C3b. Binds also
CC heparin, and therefore may play two distinct roles when incorporated in
CC virion membranes: immune evasion and host cell binding.
CC {ECO:0000269|PubMed:12477863, ECO:0000269|PubMed:15304516,
CC ECO:0000269|PubMed:16571823}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Virion membrane
CC {ECO:0000269|PubMed:16571823}.
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DR EMBL; AF148805; ABD28848.1; -; Genomic_DNA.
DR RefSeq; YP_001129351.1; NC_009333.1.
DR SMR; Q2HRD4; -.
DR BioGRID; 1776991; 25.
DR PRIDE; Q2HRD4; -.
DR DNASU; 4961488; -.
DR GeneID; 4961488; -.
DR KEGG; vg:4961488; -.
DR Proteomes; UP000000942; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039573; P:suppression by virus of host complement activation; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 4.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 4.
DR SMART; SM00032; CCP; 4.
DR SUPFAM; SSF57535; SSF57535; 4.
DR PROSITE; PS50923; SUSHI; 4.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Host membrane; Host-virus interaction;
KW Inhibition of host complement factors by virus; Membrane;
KW Reference proteome; Repeat; Signal; Sushi; Transmembrane;
KW Transmembrane helix; Viral immunoevasion; Virion.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..550
FT /note="Complement control protein"
FT /id="PRO_0000423837"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 23..83
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 84..150
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 151..209
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 210..268
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 269..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 25..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 53..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 86..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 116..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 153..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 180..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 212..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 240..266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 550 AA; 60661 MW; 068FC1C30ADDDE32 CRC64;
MAFLRQTLWI LWTFTMVIGQ DNEKCSQKTL IGYRLKMSRD GDIAVGETVE LRCRSGYTTY
ARNITATCLQ GGTWSEPTAT CNKKSCPNPG EIQNGKVIFH GGQDALKYGA NISYVCNEGY
FLVGREYVRY CMIGASGQMA WSSSPPFCEK EKCHRPKIEN GDFKPDKDYY EYNDAVHFEC
NEGYTLVGPH SIACAVNNTW TSNMPTCELA GCKFPSVTHG YPIQGFSLTY KHKQSVTFAC
NDGFVLRGSP TITCNVTEWD PPLPKCVLED IDDPNNSNPG RLHPTPNEKP NGNVFQRSNY
TEPPTKPEDT HTAATCDTNC EQPPKILPTS EGFNETTTSN TITKQLEDEK TTSQPNTHIT
SALTSMKAKG NFTNKTNNST DLHIASTPTS QDDATPSIPS VQTPNYNTNA PTRTLTSLHI
EEGPSNSTTS EKATASTLSH NSHKNDTGGI YTTLNKTTQL PSTNKPTNSQ AKSSTKPRVE
THNKTTSNPA ISLTDSADVP QRPREPTLPP IFRPPASKNR YLEKQLVIGL LTAVALTCGL
ITLFHYLFFR
