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Database: UniProt
Entry: B0WJ26_CULQU
LinkDB: B0WJ26_CULQU
Original site: B0WJ26_CULQU 
ID   B0WJ26_CULQU            Unreviewed;       978 AA.
AC   B0WJ26;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   RecName: Full=Atrial natriuretic peptide-converting enzyme {ECO:0008006|Google:ProtNLM};
GN   Name=6039031 {ECO:0000313|EnsemblMetazoa:CPIJ007155-PA};
GN   ORFNames=CpipJ_CPIJ007155 {ECO:0000313|EMBL:EDS28905.1};
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:EDS28905.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS28905.1};
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:CPIJ007155-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ007155-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC       {ECO:0000256|ARBA:ARBA00024195}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR   EMBL; DS231955; EDS28905.1; -; Genomic_DNA.
DR   RefSeq; XP_001848710.1; XM_001848658.1.
DR   AlphaFoldDB; B0WJ26; -.
DR   STRING; 7176.B0WJ26; -.
DR   EnsemblMetazoa; CPIJ007155-RA; CPIJ007155-PA; CPIJ007155.
DR   KEGG; cqu:CpipJ_CPIJ007155; -.
DR   VEuPathDB; VectorBase:CPIJ007155; -.
DR   VEuPathDB; VectorBase:CQUJHB003789; -.
DR   eggNOG; KOG3577; Eukaryota.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_006842_19_1_1; -.
DR   InParanoid; B0WJ26; -.
DR   OMA; WHVALFK; -.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd07066; CRD_FZ; 1.
DR   CDD; cd00112; LDLa; 2.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR000082; SEA_dom.
DR   InterPro; IPR036364; SEA_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   PANTHER; PTHR24258:SF146; -; 1.
DR   PANTHER; PTHR24258; SERINE PROTEASE-RELATED; 1.
DR   Pfam; PF01392; Fz; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF01390; SEA; 1.
DR   Pfam; PF00089; Trypsin; 2.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00063; FRI; 1.
DR   SMART; SM00192; LDLa; 2.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   SUPFAM; SSF82671; SEA domain; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS50024; SEA; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        137..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          168..289
FT                   /note="SEA"
FT                   /evidence="ECO:0000259|PROSITE:PS50024"
FT   DOMAIN          317..443
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          630..975
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          1..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          748..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..28
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..110
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        322..383
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        330..376
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        492..507
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   978 AA;  109366 MW;  ED7C4C8EBAD14814 CRC64;
     MKSSKYPESD DNDSLPPPPP PEDDPYFDDL SPPPGLNHLN HLDTLPQTTT IPAGTTATGM
     SPEKSRKQHR SSSDAKHHHR NGGNGLHHKG SNGAGHHHHH HHHHHRHSKS SRADSVLSSD
     SDIRFTRRKL GDNQKCGCAL IAGFLLILLF AGVIVYVGYT YLRPEPLPDR IFRARLRVVD
     GDHWTPELAD QSTLRFQHKS RDYRERINLI MRRSDLREPY EGSEILALDG NEGEDLTLHF
     AMYFDPYAEL VSAADLHSIM MEEITSDSPR FFRNLTIDPS SLIIKEVLGQ FDDIPGTSSS
     PLGGKDDVVS EVVTTMRPPR KCEPLRLNYC RSVGYNMTTY PNFFGHNSVE EVEADLISFR
     ELVDAECFRQ AFDFICRLLQ PPCEYRRIEE PTAGKVCRQY CQAFWAGCGD RLPERFRRFM
     DCERFPESTG IQSCHSRPGC SGELQSNALS SRMCDGVADC PDLSDENTCT FCAYGAIYCG
     RGRVCYARNA RCDGKIDCPD GADEKDCLSI SPQVTHLTFP PPIVPHRPRF YSEGYAVFSE
     KGTTGKLCSV GMESNEYVRN TVAESLCKAL GFERVDFSEI RNDTEPNTSY VRVLDPRASE
     ISFVRTTCQS KQSLYVSCGQ LECGVQSALP NGGNVGLSKM AAPGDWPWLV ALFRADTHVC
     DGTLVSSDWV LTTESCFQGQ AKATWYAIFG AVRLTSNAPW TQRRRIIGMV KSPVEGSTAA
     LVRLENPVIY SDFVRPICLP DIPLKETIDR SDNVTPTPHA EKFSKSRSKK RIKENRQYFE
     TPGDDETASS DEYSDVTESS KFSVNEFTAE FADEGSQIPK AEAVGAVSGT RNPYPLPENS
     PQTNNYISPS NYIGHSFTPP KAKQTVWTNC NTLGWSRQRD HLQRVQLKIS DMKPCENISI
     ATVNSMCTEA AYHKQDCSEE EFAGSPVVCL LPAERKWALV GVASWRIACA PNGIERPRMY
     DKITSNTQWL RETIAATV
//
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