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 03-APR-2013, entry version 63.
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; Platyhelminthes; Trematoda; Digenea; Strigeidida;
OC Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3166457;
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
CC tissue of the host.
CC -!- ENZYME REGULATION: Activated by an autocatalytic mechanism.
CC -!- TISSUE SPECIFICITY: Acetabular (penetration) glands.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR EMBL; J03946; AAA29864.1; -; mRNA.
DR PIR; A28942; A28942.
DR ProteinModelPortal; P12546; -.
DR MEROPS; S01.144; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR001254; Peptidase_S1.
DR InterPro; IPR018114; Peptidase_S1_AS.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR009003; Trypsin-like_Pept_dom.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; FALSE_NEG.
PE 2: Evidence at transcript level;
KW Disulfide bond; Hydrolase; Protease; Serine protease; Signal; Zymogen.
FT SIGNAL 1 19 Potential.
FT PROPEP 20 27 Potential.
FT /FTId=PRO_0000028440.
FT CHAIN 28 264 Cercarial protease.
FT /FTId=PRO_0000028441.
FT DOMAIN 28 264 Peptidase S1.
FT ACT_SITE 68 68 Charge relay system (By similarity).
FT ACT_SITE 126 126 Charge relay system (By similarity).
FT ACT_SITE 218 218 Charge relay system (By similarity).
FT DISULFID 53 69 By similarity.
FT DISULFID 192 202 By similarity.
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
//