ID CTRP_PENMO Reviewed; 31 AA. AC P35002; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 24-JAN-2024, entry version 88. DE RecName: Full=Chymotrypsin; DE EC=3.4.21.1; DE Flags: Fragment; OS Penaeus monodon (Giant tiger prawn). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata; OC Penaeoidea; Penaeidae; Penaeus. OX NCBI_TaxID=6687; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Midgut; RX PubMed=1657178; DOI=10.1016/0167-4838(91)90112-d; RA Tsai I.H., Lu P.J., Chuang J.L.; RT "The midgut chymotrypsins of shrimps (Penaeus monodon, Penaeus japonicus RT and Penaeus penicillatus)."; RL Biochim. Biophys. Acta 1080:59-67(1991). CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|- CC Xaa.; EC=3.4.21.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10078, CC ECO:0000255|PROSITE-ProRule:PRU10079}; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE- CC ProRule:PRU00274}. 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 PIR; S18356; S18356. DR AlphaFoldDB; P35002; -. DR SMR; P35002; -. DR MEROPS; S01.122; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 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; IPR001254; Trypsin_dom. DR Pfam; PF00089; Trypsin; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease. FT CHAIN 1..>31 FT /note="Chymotrypsin" FT /id="PRO_0000088675" FT DOMAIN 1..>31 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT NON_TER 31 SQ SEQUENCE 31 AA; 3287 MW; 6CCD1D09067D1D78 CRC64; IVGGVEAVPG VWPYQAALFI IDMYFCGGSL I //