ID CERC_SCHMA Reviewed; 264 AA. AC P12546; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=Cercarial protease; DE EC=3.4.21.-; DE AltName: Full=Cercarial elastase; DE Flags: Precursor; OS Schistosoma mansoni (Blood fluke). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda; OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6183; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3166457; DOI=10.1016/s0021-9258(18)37688-9; RA Newport G.R., McKerrow J.H., Hedstrom R., Petitt M., McGarrigle L., RA Barr P.J., Agabian N.; RT "Cloning of the proteinase that facilitates infection by schistosome RT parasites."; RL J. Biol. Chem. 263:13179-13184(1988). CC -!- FUNCTION: This protease cleaves elastin and thus facilitates CC penetration of schistosome parasite larvae through elastin-rich tissue CC of the host. CC -!- ACTIVITY REGULATION: Activated by an autocatalytic mechanism. CC -!- TISSUE SPECIFICITY: Acetabular (penetration) glands. 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 EMBL; J03946; AAA29864.1; -; mRNA. DR PIR; A28942; A28942. DR AlphaFoldDB; P12546; -. DR SMR; P12546; -. DR STRING; 6183.P12546; -. DR MEROPS; S01.144; -. DR eggNOG; KOG3627; Eukaryota. DR HOGENOM; CLU_1058926_0_0_1; -. DR InParanoid; P12546; -. DR Proteomes; UP000008854; Unassembled WGS sequence. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. 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; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR PANTHER; PTHR24256:SF470; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR24256; TRYPTASE-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; PS00134; TRYPSIN_HIS; 1. PE 2: Evidence at transcript level; KW Disulfide bond; Hydrolase; Protease; Reference proteome; Serine protease; KW Signal; Zymogen. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT PROPEP 20..27 FT /evidence="ECO:0000255" FT /id="PRO_0000028440" FT CHAIN 28..264 FT /note="Cercarial protease" FT /id="PRO_0000028441" FT DOMAIN 28..264 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 68 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 126 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 218 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT DISULFID 53..69 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 192..202 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" SQ SEQUENCE 264 AA; 28545 MW; E2E5129A7C5D5010 CRC64; MSNRWRFVVV VTLFTYCLTF ERVSTWLIRS GEPVQHPAEF PFIAFLTTER TMCTGSLVST RAVLTAGHCV CSPLPVIRVS FLTLRNGDQQ GIHHQPSGVK VAPGYMPSCM SARQRRPIAQ TLSGFDIAIV MLAQMVNLQS GIRVISLPQP SDIPPPGTGV FIVGYGRDDN DRDPSRKNGG ILKKGRATIM ECRHATNGNP ICVKAGQNFG QLPAPGDSGG PLLPSLQGPV LGVVSHGVTL PNLPDIIVEY ASVARMLDFV RSNI //