CCPH_SHV21
ID CCPH_SHV21 Reviewed; 360 AA.
AC Q01016;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 02-DEC-2020, entry version 95.
DE RecName: Full=Complement control protein homolog;
DE Short=CCPH;
DE Flags: Precursor;
GN Name=4; Synonyms=CCPH;
OS Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=10383;
OH NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA Honess R.W.;
RT "Primary structure of the herpesvirus saimiri genome.";
RL J. Virol. 66:5047-5058(1992).
RN [2]
RP SIMILARITY TO CCP.
RX PubMed=1316492; DOI=10.1128/jvi.66.6.3937-3940.1992;
RA Albrecht J.-C., Fleckenstein B.;
RT "New member of the multigene family of complement control proteins in
RT herpesvirus saimiri.";
RL J. Virol. 66:3937-3940(1992).
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass membrane
CC protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q01016-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q01016-2; Sequence=VSP_001212, VSP_001213;
CC -!- SIMILARITY: Belongs to the receptors of complement activation (RCA)
CC family. {ECO:0000305}.
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DR EMBL; X64346; CAA45626.1; -; Genomic_DNA.
DR EMBL; X64346; CAA45627.1; -; Genomic_DNA.
DR EMBL; X60283; CAA42823.1; -; Genomic_DNA.
DR EMBL; X60283; CAA42822.1; -; Genomic_DNA.
DR PIR; A42534; WMBE1E.
DR RefSeq; NP_040205.1; NC_001350.1.
DR RefSeq; NP_040206.1; NC_001350.1.
DR SMR; Q01016; -.
DR PRIDE; Q01016; -.
DR GeneID; 1488258; -.
DR GeneID; 1488259; -.
DR KEGG; vg:1488258; -.
DR KEGG; vg:1488259; -.
DR Proteomes; UP000000587; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001848; F:complement binding; IEA:InterPro.
DR GO; GO:0045916; P:negative regulation of complement activation; IEA:InterPro.
DR CDD; cd00033; CCP; 4.
DR InterPro; IPR011176; CCP_VACV_C3/B5.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 4.
DR PIRSF; PIRSF002486; CIP_VAC_C3L; 1.
DR SMART; SM00032; CCP; 4.
DR SUPFAM; SSF57535; SSF57535; 4.
DR PROSITE; PS50923; SUSHI; 4.
PE 3: Inferred from homology;
KW Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Secreted; Signal; Sushi; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..360
FT /note="Complement control protein homolog"
FT /id="PRO_0000006015"
FT TRANSMEM 328..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 21..81
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 82..144
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 145..207
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 208..266
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 23..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 54..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 84..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 111..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 147..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 175..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 210..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 238..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT VAR_SEQ 289..302
FT /note="RICNGNCTTSMPTQ -> AECACPGSNYPISS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001212"
FT VAR_SEQ 303..360
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001213"
SQ SEQUENCE 360 AA; 40006 MW; 6278A6C2ECD49669 CRC64;
MYTLHYICLV LSCVIYFVWT LSCPTRNQYV SVKYVNLTNY SGPYPNGTTL HVTCREGYAK
RPVQTVTCVN GNWTVPKKCQ KKKCSTPQDL LNGRYTVTGN LYYGSVITYT CNSGYSLIGS
TTSACLLKRG GRVDWTPRPP ICDIKKCKPP PQIANGTHTN VKDFYTYLDT VTYSCNDETK
LTLTGPSSKL CSETGSWVPN GETKCEFIFC KLPQVANAYV EVRKSATSMQ YLHINVKCYK
GFMLYGETPN TCNHGVWSPA IPECMKISSP KGDMPGINSN EDNSTPSGRI CNGNCTTSMP
TQTYTIITAR YTSHIYFPTG KTYKLPRGVL VIILTTSFII IGIILTGVCL HRCRVCMSGQ
