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Database: UniProt
Entry: Q24940
LinkDB: Q24940
Original site: Q24940 
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   16-APR-2014, entry version 61.
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:0004175; F: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
//
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