ID Q16TM1_AEDAE Unreviewed; 266 AA. AC Q16TM1; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=trypsin {ECO:0000256|ARBA:ARBA00038868}; DE EC=3.4.21.4 {ECO:0000256|ARBA:ARBA00038868}; GN ORFNames=AAEL010196 {ECO:0000313|EMBL:EAT37856.1}; 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:EAT37856.1, ECO:0000313|Proteomes:UP000682892}; RN [1] {ECO:0000313|EMBL:EAT37856.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT37856.1}; 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:EAT37856.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT37856.1}; 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:EAT37856.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT37856.1}; RG VectorBase; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4; CC Evidence={ECO:0000256|ARBA:ARBA00036320}; CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily. CC {ECO:0000256|ARBA:ARBA00024195}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH477645; EAT37856.1; -; Genomic_DNA. DR RefSeq; XP_001660673.1; XM_001660623.1. DR AlphaFoldDB; Q16TM1; -. DR MEROPS; S01.130; -. DR PaxDb; 7159-AAEL010196-PA; -. DR GeneID; 5573025; -. DR KEGG; aag:5573025; -. DR VEuPathDB; VectorBase:AAEL010196; -. DR eggNOG; KOG3627; Eukaryota. DR HOGENOM; CLU_006842_7_0_1; -. DR OMA; KYKQYGG; -. DR OrthoDB; 3175984at2759; -. DR PhylomeDB; Q16TM1; -. DR Proteomes; UP000682892; Unassembled WGS sequence. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1. 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; PTHR24264:SF65; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Digestion {ECO:0000256|ARBA:ARBA00022757}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, KW ECO:0000256|RuleBase:RU363034}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..266 FT /note="trypsin" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5030175184" FT DOMAIN 40..265 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" SQ SEQUENCE 266 AA; 28255 MW; E10CAE56FEA1C8BE CRC64; MVRIILILSA TFFSCALGAS TGGSHPLRPW WNALRSSGRI VGGFEVPVEE VPFQVSLSRV GSSHFCGGSL LSERWVMTAG HCAASGQPNL QVRIGSSQHA SGGQLIKVKE VTRHPKYDDA AIDYDFALLE LEETVTFSDS CAPVKLPQKD APVNEGTCLQ VSGWGNTQNP AESSEVLRAA YVPAVSQEEC HKAYLSFGGV TDRMVCAGFK EGGKDSCQGD SGGPLVHDNT LVGVVSWGYG CAEAGYPGVY ARVASVRDWV QEVSGL //