ID Q17MA3_AEDAE Unreviewed; 648 AA.
AC Q17MA3;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=AAEL001077-PA {ECO:0000313|EMBL:EAT47846.1};
GN Name=CLIPB45 {ECO:0000313|EMBL:EAT47846.1};
GN ORFNames=AAEL001077 {ECO:0000313|EMBL:EAT47846.1};
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:EAT47846.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EAT47846.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT47846.1};
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:EAT47846.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT47846.1};
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:EAT47846.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT47846.1};
RG VectorBase;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
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DR EMBL; CH477207; EAT47846.1; -; Genomic_DNA.
DR RefSeq; XP_001658015.1; XM_001657965.2.
DR AlphaFoldDB; Q17MA3; -.
DR STRING; 7159.Q17MA3; -.
DR PaxDb; 7159-AAEL001077-PA; -.
DR GeneID; 5568363; -.
DR KEGG; aag:5568363; -.
DR VEuPathDB; VectorBase:AAEL001077; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_004497_6_1_1; -.
DR OMA; CTIAQTI; -.
DR OrthoDB; 3450516at2759; -.
DR PhylomeDB; Q17MA3; -.
DR Proteomes; UP000682892; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.30.1640.30; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR InterPro; IPR022700; CLIP.
DR InterPro; IPR038565; CLIP_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24260; -; 1.
DR PANTHER; PTHR24260:SF153; GH19262P-RELATED; 1.
DR Pfam; PF12032; CLIP; 1.
DR Pfam; PF00089; Trypsin; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00680; CLIP; 1.
DR SMART; SM00020; Tryp_SPc; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS51888; CLIP; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..648
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030175543"
FT DOMAIN 40..284
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 298..351
FT /note="Clip"
FT /evidence="ECO:0000259|PROSITE:PS51888"
FT DOMAIN 391..647
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 648 AA; 71868 MW; 4382BECD7159EC17 CRC64;
MLGVLSSALL LLVGACSAAE VFKNAQFQCG IPKNANTLLI VNGVDAKISD WPWHAAVRQH
VAANGQPEYV CGGTLISERF VVTAAHCTMD PDNPNKRIQL SVQVGVNAVG SPEGKVFNAL
KIHRHPGFSL FDLKDDIALI ELESPVQFSE SILPVCISER TSLDPGKLGA VVGWGFTEND
IKSTKLKLAK LPVIEEIECK RKEPELYGRV LTSKVFCAGY TNGTSACNGD SGGGIVFERG
DAWYLGGIVS FTKAKEGEDR CLSTTYTVFT KVTSYLSWIE SVTNTDFSNE YGIEKTVPCS
APGQSNGHCV PVQQCRNLFD ELRSPLLTKQ TANELRQKVC ELRGVRRSVC CDPSEVERIP
IHRNAVLLPK ECGVAKRPQT TTTAIRAGVF EFPWVAMVRS SKATPDHDPY CTGSLINNRY
VLTSAACLKA KERRDLDYVR LGEHTLNSQR DCDTFTHPRT RQSVQECAPA PVDVKAVLPF
TIHPQAGKPF RGNDFALVRM VDKVQFTDTV QPICLPIRED LRNHLPTNFV LSMYEITVTN
NRYAQELYKT RSVFTEREEC EERFEDYGYT PWVTDKMFCA LAQGPSFICT PHLGAPLVSM
VKQGPIERAV MYGLSMMGPS NCTIAQTIAK TYLRVPLYVD WILENIEK
//
