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Database: UniProt/TrEMBL
Entry: B0WYU2_CULQU
LinkDB: B0WYU2_CULQU
Original site: B0WYU2_CULQU 
ID   B0WYU2_CULQU            Unreviewed;      1091 AA.
AC   B0WYU2;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Vitellogenin convertase {ECO:0000313|EMBL:EDS37202.1, ECO:0000313|EnsemblMetazoa:CPIJ011701-PA};
GN   Name=6045170 {ECO:0000313|EnsemblMetazoa:CPIJ011701-PA};
GN   ORFNames=CpipJ_CPIJ011701 {ECO:0000313|EMBL:EDS37202.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000313|EMBL:EDS37202.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS37202.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CPIJ011701-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ011701-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000256|ARBA:ARBA00005325}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; DS232199; EDS37202.1; -; Genomic_DNA.
DR   RefSeq; XP_001862564.1; XM_001862529.1.
DR   AlphaFoldDB; B0WYU2; -.
DR   STRING; 7176.B0WYU2; -.
DR   MEROPS; S08.048; -.
DR   EnsemblMetazoa; CPIJ011701-RA; CPIJ011701-PA; CPIJ011701.
DR   KEGG; cqu:CpipJ_CPIJ011701; -.
DR   VEuPathDB; VectorBase:CPIJ011701; -.
DR   VEuPathDB; VectorBase:CQUJHB002854; -.
DR   eggNOG; KOG3525; Eukaryota.
DR   HOGENOM; CLU_002976_0_0_1; -.
DR   InParanoid; B0WYU2; -.
DR   OMA; AIFHEHY; -.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00064; FU; 2.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR034182; Kexin/furin.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR42884:SF3; FURIN-LIKE PROTEASE 1, ISOFORMS 1_1-X_2; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00261; FU; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        991..1013
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          278..409
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          958..982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1059..1091
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..625
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..977
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1091 AA;  119306 MW;  1F73F7DE172AFC25 CRC64;
     MHDPGASYDV NGNDGDPMPH YDLTDSNRHG TRCAGEVAAT ANNSKCAVGI AYGARVGGVR
     MLDGDVTDVV EAKSLGLHSQ HIDIYSASWG PDDDGKTVDG PGDMATRAFI EGVRKGRGGK
     GSIFIWASGN GGREHDNCNC DGYTNSIWTL SISSASQEGL VPWFSEMCSS TLATTYSSGN
     TNEKQVITTD LHHSCTSSHT GTSASAPLAA GIAALVLEAN RNLTWRDLQH IVVRTAKPGN
     LKDPSWAKNG VGRRVSHSFG YGLMDAAAMV RLARTWKTVP DQQICEINAP HLDKQIPPRT
     KVTLQLLVEH CMGVNYLEHV QAKITLTSQR RGDIQIFLTS PSGTRVTLLT PRSHDLSRSG
     FNQWPFMSVH TWGEAPHGVW LLEIHNEGRL LGYSSIRGWS LILYGTSIPP DPNDPPNTPR
     VFSTPALPPA ALPPIIPASG SFGSSKNFYS SSALGKPNRK QQQQYGGATY TPTFGMTPAY
     QSPQPVTPPR KNNKGKNKPN KSQSSKTTTA RPVSQTTLNV FLNSYGTGKK YEYNTGPRKN
     QTPKPKPMQT INYGRSDKYH AATSNIPEKQ PIAIKAPKQV KQDNAPNSRK LPTTIGTSSS
     TTNSVPSTAT GTTSGGTTSL TTQPPIFNER FSTTNARIPN RFQQYEKIQQ FYPELKPYSS
     IRDDLDHRTT PNKPVAAPPP PKNTPSIVTT NGNGKPSRAN PKIFFPDTDI IDAIAPRKIS
     SSLQQQPVQP AFYGRTQNSQ FVSSSGGKNG KAQITQWNLI FYGTETPAQP DDPTRVGKPG
     FSDSNFGGEI EHNSLEFESG VSSDQWRNMQ QIGESHVDVQ RTASSDVTSL ACARYDRARC
     LECGSASFFY NGHCYSSCPA STFPDTSTME QDEKQQHQQQ RPLPPGSVRR RRGNNLDNEP
     QERDTQPQPG QQHQHFCIPC HATCLECSGP AANQCTECQP EFAFDGLRLC VTINRKQRPQ
     ASSGTNKSSN QTAPTLNDPE SDDKRWLPAD YLIMITVVGV TLVVAFAGIY LLWRRCFRGV
     LLATDHHQYD RVQTSDPAAS GSRGVPSYAE LVRDEIDDIL AESSSEDEED DEHHDGRESR
     SFMPIIAPVE R
//
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