ID A0A182P0V2_9DIPT Unreviewed; 1066 AA.
AC A0A182P0V2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 43.
DE RecName: Full=Atrial natriuretic peptide-converting enzyme {ECO:0008006|Google:ProtNLM};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI000534-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI000534-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI000534-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 AlphaFoldDB; A0A182P0V2; -.
DR STRING; 199890.A0A182P0V2; -.
DR EnsemblMetazoa; AEPI000534-RA; AEPI000534-PA; AEPI000534.
DR VEuPathDB; VectorBase:AEPI000534; -.
DR OrthoDB; 3677296at2759; -.
DR Proteomes; UP000075885; 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; 2.
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 Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 197..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 228..350
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 378..504
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 695..1062
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 1..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..166
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 383..444
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 391..437
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 515..530
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 553..568
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1066 AA; 117501 MW; D2527A1F59EA99D9 CRC64;
KPGTKYPESD DCDSLPPPPP PDDDSYFDDE DRLSHGHHHH HHHHHQLQQQ QQQHLAHLAQ
AHHNGMHLAA QQQQQQPLRH HFATGTPPPA LDSDLDASLK KERKLRSNSD SSNATSNGGG
AGGGGGKHKS GGGGLGGGGG GGKTANGGHG HHHHHHHHHH HSRGAMHAKS SRAESVLSSD
SDIRFTRRKL GDNQKCGCAL IAGFLLILLC AGAIVYVGYT YLRPEPLPDR IFRARLRVIE
GDRWTPELAD QNTLRFQHRA RDYRERINLI MRRSDLREPF EGSEILALDG NEEPGDLTLH
FALYFDPYAE LVSAADLRSI LLEEITGQER KYFRNLTIDP NSLVVKEVTG TGDDIVGTSS
SPLGGKDEVT VEIVTTARPP RKCEPLRLGY CRSVGYNVTT YPNFFGHNSL EEVEADLISF
RELVDAECFR QAFDFICRLL QPPCEYRSIE EPTPGMVCRQ YCQSFWAGCG ERLPERLRRY
LDCERFPEST GVQSCHSKPG CTGELQANAL SSRLCDGVAD CADLSDENTC TFCAYGAISC
GRSRACYARN ARCDGKLDCP DGSDEKDCLS ISPQVSFLTF PPPIVPFRPR FYSEGYAVFS
EKGTTGKLCS VGMEGNEYVR NTVAESLCKA LGYERVDYSE IRNDTEPNTS YVRVLDPRAS
EISFVRTQCQ SKQSLYVACS HLECGVQSTL PATQNIGLSK MATPGDWPWL VALLRADTHV
CDGTLVSKDW VLTTESCFQG QAKATWMAVF GAVRLSSNAP WTQRRRIIGM VKSPVEGSTA
AMVRLETPVV YSDFVRPICL PDIPLKETID RNDNSVTPTP HAEKYSTGKA GAGRKLKEYR
QYFEMPGDDE LATGDEYGDL NEAARYVNQY RADFTDEQYQ IPQAEAAHGR TTAAPSAGPA
SPPAAYPLPA NSPQTNNYIS ALNYISAGGA GANVGGPGVA GFQQPTKLGK QSQWTNCNTL
GWSRQRDHLQ RVQLKLIDMS PCENISIATV NSMCAESAYH KQDCGEEEFA GSPVVCLLPT
DRRWALVGIS SWRIACAPNG IERPRMYDKI TPNTPWIRDT ISATVT
//
