ID Q17EY0_AEDAE Unreviewed; 376 AA.
AC Q17EY0;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=CLIP domain-containing serine protease {ECO:0000256|RuleBase:RU366078};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU363034};
GN Name=CLIPB38 {ECO:0000313|EMBL:EAT45079.1};
GN ORFNames=AAEL003628 {ECO:0000313|EMBL:EAT45079.1};
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:EAT45079.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EAT45079.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT45079.1};
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:EAT45079.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT45079.1};
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:EAT45079.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT45079.1};
RG VectorBase;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU366078}.
CC -!- DOMAIN: The clip domain consists of 35-55 residues which are 'knitted'
CC together usually by 3 conserved disulfide bonds forming a clip-like
CC compact structure. {ECO:0000256|RuleBase:RU366078}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195, ECO:0000256|RuleBase:RU366078}.
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DR EMBL; CH477278; EAT45079.1; -; Genomic_DNA.
DR RefSeq; XP_001657086.1; XM_001657036.2.
DR AlphaFoldDB; Q17EY0; -.
DR STRING; 7159.Q17EY0; -.
DR MEROPS; S01.507; -.
DR PaxDb; 7159-AAEL003628-PA; -.
DR GeneID; 5578688; -.
DR KEGG; aag:5578688; -.
DR VEuPathDB; VectorBase:AAEL003628; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_0_3_1; -.
DR OMA; PLVCCPA; -.
DR OrthoDB; 3680196at2759; -.
DR PhylomeDB; Q17EY0; -.
DR Proteomes; UP000682892; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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; 2.
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 InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24260; -; 1.
DR PANTHER; PTHR24260:SF131; CLIP DOMAIN-CONTAINING SERINE PROTEASE-RELATED; 1.
DR Pfam; PF12032; CLIP; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00680; CLIP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366078};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366078}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT CHAIN 22..376
FT /note="CLIP domain-containing serine protease"
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT /id="PRO_5030003980"
FT DOMAIN 110..374
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 376 AA; 41964 MW; 2C2C67B93E8EDFAC CRC64;
MFTVKSSALL LLLSIAGATE AITLLPCEIP NENAIGYCIP KSGCTAYQKL IAAGPLNDEQ
LEFVNQLNCS RTGVCCPPRA NFYQNPRVTT LKDYKDLIAK CGADTTEDRI FGGQVTTIDE
FPWLALLFYE SLQTGMLHPS CGGALVAKRW ILTAAHCVTG KSYTNLGPLK FVRLGEHNLE
TELDCDLNED CNEKPLDIAV EKAIPHPEYD SKSWDRYNDV ALVKLVEEAP FTDFIRHICL
PSYYNLTEQL SKSNVKYMAA GWGRTDFYNT TTSVPSKLKL KVSLPHVDQE RCRAVYAEHT
IRIADSQICA GGQKAHDTCR GDSGSPLMYY NRQFARWFVY GIVSRGPSQC GTEGVPSIYT
NMFKFDDWVK RTIASN
//
