ID Q16VN8_AEDAE Unreviewed; 990 AA.
AC Q16VN8;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 24-JAN-2024, entry version 115.
DE SubName: Full=AAEL009482-PA {ECO:0000313|EMBL:EAT38644.1};
GN ORFNames=AAEL009482 {ECO:0000313|EMBL:EAT38644.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT38644.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EAT38644.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT38644.1};
RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA Rogers Y.-H., Kravitz S., Fraser C.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT38644.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT38644.1};
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0000313|EMBL:EAT38644.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT38644.1};
RG VectorBase;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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; CH477584; EAT38644.1; -; Genomic_DNA.
DR RefSeq; XP_001660107.1; XM_001660057.1.
DR AlphaFoldDB; Q16VN8; -.
DR STRING; 7159.Q16VN8; -.
DR PaxDb; 7159-AAEL009482-PA; -.
DR VEuPathDB; VectorBase:AAEL027371; -.
DR eggNOG; KOG3577; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_19_1_1; -.
DR OMA; WHVALFK; -.
DR PhylomeDB; Q16VN8; -.
DR Proteomes; UP000682892; 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 InterPro; IPR017343; UCP037987.
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 PIRSF; PIRSF037987; UCP037987; 1.
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 151..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 182..303
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 331..457
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 648..987
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 17..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..123
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 336..397
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 344..390
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 468..483
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 506..521
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 990 AA; 111511 MW; D9CEC959CCC6CA7F CRC64;
MQHIENASGS YNKVLRTSLK STKYPDSDDC DSLPPPPPPE DDPYFDDLHS PTTLHHNGHL
HHLNLSLDTS PHGDSSPEKP RKHRSNSDSS QTKHHRNGGL HHKSSNGHHH HHHHHHHHRH
PNKNSRADSV LSSDSDIRFT RRKLGDNQKC GCALIAGFLL ILLFAGVIVY VGYTYLRPEP
LPDRIFRARL RVVDGDSWIP ELADQSTPRF QQRARDYRER INLIMRRSDL REPYEGSEIL
ALDGNEGEDL TLHFAMYFDP YAELVSTADL HSILMEEIIS EHPRYFRNLT IDPSSLIIKE
VLGQFDDIPG TSSSPLGGKD DEISEVVTTV RPPRKCEPLR LNYCRSVGYN MTTYPNFFGH
GSIEEVEADL ISFRELVDAE CFRQAFDFVC RLLQPPCEYR RIEEPVAGKI CRQYCQAFWS
GCGDRLPERF KKFLDCERFP ESTAIQSCHS RPGCASELQS NALSSRLCDG VADCPDLSDE
NTCTFCPYGA IYCGRGRACY AKNARCDGKM DCPDGSDEKD CLSISPQVTY LTFPPPIAPY
RPRFFSEGYA VFSEKGTTGK LCSVGMEGND YVRSTVAESL CKALGFERVD YSQIRNDTEP
NTSYVRVLDP RASEISFVRT TCQSKQSLYV SCGQLECGVQ SALPSNPNVG LSKMASPGDW
PWMVALFRAD THVCDGTLVS SDWVLTTESC FQGQAKATWM AIFGAVRLSS NAPWTQRRRI
IGMVKSPVEG STAALVRLEN PVIYSDFVRP ICLPDIPLKE TIDRSDNIVT PTPHAEKFSK
TRPKKRLKEY RQYFETPGDD DSSDDYTEDA ESSRYTTNEF NVEFTDEGSQ IPKAEAVQVT
GTKNPYPLPE NSPQTNNYIS TLNYIGSGFQ PPKSKQTVWT NCNTLGWSRQ RDHLQRVQLK
ISDMKPCENI SIATVNSMCT EAAYHKQDCS EEEFAGSPVV CLLPTERKWA LVGVASWRIA
CAPNGIERPR MYDKITSNTQ WIRETIAATV
//
