ID Q16ZR3_AEDAE Unreviewed; 281 AA. AC Q16ZR3; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=trypsin {ECO:0000256|ARBA:ARBA00038868}; DE EC=3.4.21.4 {ECO:0000256|ARBA:ARBA00038868}; 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:ACV07664.1}; RN [1] {ECO:0000313|EMBL:ACV07664.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rockefeller {ECO:0000313|EMBL:ACV07664.1}; RX PubMed=20100490; DOI=10.1016/j.jinsphys.2010.01.003; RA Brackney D.E., Isoe J., W C B.IV., Zamora J., Foy B.D., Miesfeld R.L., RA Olson K.E.; RT "Expression profiling and comparative analyses of seven midgut serine RT proteases from the yellow fever mosquito, Aedes aegypti."; RL J. Insect Physiol. 56:736-744(2010). 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; GQ398047; ACV07664.1; -; mRNA. DR RefSeq; XP_001653092.1; XM_001653042.1. DR AlphaFoldDB; Q16ZR3; -. DR SMR; Q16ZR3; -. DR STRING; 7159.Q16ZR3; -. DR MEROPS; S01.A35; -. DR PaxDb; 7159-AAEL008085-PA; -. DR VEuPathDB; VectorBase:AAEL013628; -. DR eggNOG; KOG3627; Eukaryota. DR HOGENOM; CLU_006842_7_0_1; -. DR OMA; EIILHEA; -. DR PhylomeDB; Q16ZR3; -. 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; IPR033116; TRYPSIN_SER. 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; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. PE 2: Evidence at transcript level; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Hydrolase {ECO:0000313|EMBL:ACV07664.1}; KW Protease {ECO:0000313|EMBL:ACV07664.1}. FT DOMAIN 29..270 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" SQ SEQUENCE 281 AA; 29761 MW; 216DF2693624E83C CRC64; MWFSVKISKL LLLVAVSSVA ASVDNDVKII GGFPAQQSST RHQVSIRQKS VDLALFGSGH FCGGSLINDR TVLTAALCLV NEEGKRRVAS YFRVVGGGLN RLLQTQNTVI ANVSKVIIHE NYDPNTVAND IGLLILDKPV ESSHQTLRTI ELATSRPVAG SICQTTGWGT TVYGLPMVTV ELMAVNVTIQ PIESCNGTGS YNGIILDGML CAGEITGGKD SCQGDSGGPL VCGGFLAGIV SYGKGCGLAS YPGIYSDVVH FREWIDKHKH TSGGENVKFT V //