ID CATLL_FASHE Reviewed; 326 AA.
AC Q24940; P91727;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-APR-2013, entry version 60.
DE RecName: Full=Cathepsin L-like proteinase;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=Cat-1;
OS Fasciola hepatica (Liver fluke).
OC Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea;
OC Echinostomida; Echinostomata; Echinostomatoidea; Fasciolidae;
OC Fasciola.
OX NCBI_TaxID=6192;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 107-122; 188-206 AND
RP 277-291, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND
RP HYDROXYLATION AT PRO-109 AND PRO-196.
RC STRAIN=Crompton;
RX PubMed=8192668;
RA Wijffels G.L., Panaccio M., Salvatore L., Wilson L., Walker I.D.,
RA Spithill T.W.;
RT "The secreted cathepsin L-like proteinases of the trematode Fasciola
RT hepatica, contain 3-hydroxyproline residues.";
RL Biochem. J. 299:781-790(1994).
CC -!- FUNCTION: Thiol protease. Probably involved in interaction with
CC host tissues.
CC -!- CATALYTIC ACTIVITY: Similar that of papain. Has high activity on
CC Z-Phe-Arg-NHMec, but no activity on Z-Arg-NHMec.
CC -!- ENZYME REGULATION: Strongly inhibited by Antipain, E64 and
CC Leupeptin, and weakly inhibited by iodoacetic acid (IAA) and
CC phenylmethylsulfonyl fluoride (PMSF). Requires the presence of
CC dithiothreitol (DTT) for activity.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=46 uM for Z-Phe-Arg-NHMec (at pH 7.45);
CC pH dependence:
CC Optimum pH is 7-9 in a mixed-buffer system. In a Tris buffer
CC high levels of activity were detected at very alkaline pHs;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Contains cysteine residues involved in intramolecular
CC disulfide bonding.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC -!- CAUTION: It is not clear whether the mature peptide starts at Ala-
CC 107 or at Val-108.
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DR EMBL; L33771; AAA29136.1; -; mRNA.
DR PIR; S43991; S43991.
DR PDB; 2O6X; X-ray; 1.40 A; A=17-326.
DR PDBsum; 2O6X; -.
DR ProteinModelPortal; Q24940; -.
DR SMR; Q24940; 17-326.
DR MEROPS; C01.033; -.
DR EvolutionaryTrace; Q24940; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411; PTHR12411; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Hydroxylation; Protease; Secreted; Signal; Thiol protease; Zymogen.
FT SIGNAL 1 15 Potential.
FT PROPEP 16 106 Activation peptide.
FT /FTId=PRO_0000042858.
FT CHAIN 107 326 Cathepsin L-like proteinase.
FT /FTId=PRO_0000042859.
FT ACT_SITE 132 132 By similarity.
FT ACT_SITE 269 269 By similarity.
FT ACT_SITE 289 289 By similarity.
FT MOD_RES 109 109 3-hydroxyproline; partial.
FT MOD_RES 196 196 3-hydroxyproline; partial.
FT DISULFID 129 172 By similarity.
FT DISULFID 163 204 By similarity.
FT DISULFID 262 311 By similarity.
FT HELIX 18 28
FT HELIX 34 59
FT STRAND 62 67
FT TURN 71 74
FT HELIX 77 84
FT HELIX 91 94
FT STRAND 97 100
FT HELIX 114 117
FT HELIX 132 149
FT HELIX 157 163
FT HELIX 165 167
FT HELIX 171 173
FT HELIX 177 184
FT TURN 192 194
FT HELIX 208 210
FT STRAND 213 221
FT HELIX 226 236
FT STRAND 239 243
FT HELIX 247 250
FT STRAND 252 257
FT STRAND 269 279
FT STRAND 282 288
FT STRAND 300 304
FT STRAND 306 309
FT HELIX 310 312
FT TURN 313 315
FT STRAND 316 324
SQ SEQUENCE 326 AA; 36896 MW; 7FDDB3094D3134A6 CRC64;
MRLFILAVLT VGVLGSNDDL WHQWKRMYNK EYNGADDQHR RNIWEKNVKH IQEHNLRHDL
GLVTYTLGLN QFTDMTFEEF KAKYLTEMSR ASDILSHGVP YEANNRAVPD KIDWRESGYV
TEVKDQGNCG SCWAFSTTGT MEGQYMKNER TSISFSEQQL VDCSGPWGNN GCSGGLMENA
YQYLKQFGLE TESSYPYTAV EGQCRYNKQL GVAKVTGYYT VHSGSEVELK NLVGARRPAA
VAVDVESDFM MYRSGIYQSQ TCSPLRVNHA VLAVGYGTQG GTDYWIVKNS WGTYWGERGY
IRMARNRGNM CGIASLASLP MVARFP
//
