GenomeNet

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   26-NOV-2014, entry version 63.
DE   RecName: Full=Cathepsin L-like proteinase;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=Cat-1 {ECO:0000303|PubMed:8192668};
OS   Fasciola hepatica (Liver fluke).
OC   Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea;
OC   Echinostomida; Echinostomata; Echinostomatoidea; Fasciolidae;
OC   Fasciola.
OX   NCBI_TaxID=6192;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAA29136.1}
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 {ECO:0000312|EMBL:AAA29136.1};
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. {ECO:0000269|PubMed:8192668,
CC       ECO:0000303|PubMed:8192668}.
CC   -!- CATALYTIC ACTIVITY: Similar that of papain. Has high activity on
CC       Z-Phe-Arg-NHMec, but no activity on Z-Arg-NHMec.
CC       {ECO:0000269|PubMed:8192668}.
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. {ECO:0000269|PubMed:8192668}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=46 uM for Z-Phe-Arg-NHMec (at pH 7.45)
CC         {ECO:0000269|PubMed:8192668};
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         {ECO:0000269|PubMed:8192668};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8192668}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8192668}.
CC   -!- PTM: Contains cysteine residues involved in intramolecular
CC       disulfide bonding. {ECO:0000269|PubMed:8192668}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
CC       ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
CC   -!- CAUTION: It is not clear whether the mature peptide starts at Ala-
CC       107 or at Val-108. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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       {ECO:0000255}.
FT   PROPEP       16    106       Activation peptide. {ECO:0000255,
FT                                ECO:0000269|PubMed:8192668}.
FT                                /FTId=PRO_0000042858.
FT   CHAIN       107    326       Cathepsin L-like proteinase.
FT                                {ECO:0000269|PubMed:8192668}.
FT                                /FTId=PRO_0000042859.
FT   ACT_SITE    132    132       {ECO:0000250|UniProtKB:P07711}.
FT   ACT_SITE    269    269       {ECO:0000250|UniProtKB:P07711}.
FT   ACT_SITE    289    289       {ECO:0000250|UniProtKB:P07711}.
FT   MOD_RES     109    109       3-hydroxyproline; partial.
FT                                {ECO:0000269|PubMed:8192668}.
FT   MOD_RES     196    196       3-hydroxyproline; partial.
FT                                {ECO:0000269|PubMed:8192668}.
FT   DISULFID    129    172       {ECO:0000250|UniProtKB:P25774}.
FT   DISULFID    163    204       {ECO:0000250|UniProtKB:P25774}.
FT   DISULFID    262    311       {ECO:0000250|UniProtKB:P25774}.
FT   HELIX        18     28       {ECO:0000244|PDB:2O6X}.
FT   HELIX        34     59       {ECO:0000244|PDB:2O6X}.
FT   STRAND       62     67       {ECO:0000244|PDB:2O6X}.
FT   TURN         71     74       {ECO:0000244|PDB:2O6X}.
FT   HELIX        77     84       {ECO:0000244|PDB:2O6X}.
FT   HELIX        91     94       {ECO:0000244|PDB:2O6X}.
FT   STRAND       97    100       {ECO:0000244|PDB:2O6X}.
FT   HELIX       114    117       {ECO:0000244|PDB:2O6X}.
FT   HELIX       132    149       {ECO:0000244|PDB:2O6X}.
FT   HELIX       157    163       {ECO:0000244|PDB:2O6X}.
FT   HELIX       165    167       {ECO:0000244|PDB:2O6X}.
FT   HELIX       171    173       {ECO:0000244|PDB:2O6X}.
FT   HELIX       177    184       {ECO:0000244|PDB:2O6X}.
FT   TURN        192    194       {ECO:0000244|PDB:2O6X}.
FT   HELIX       208    210       {ECO:0000244|PDB:2O6X}.
FT   STRAND      213    221       {ECO:0000244|PDB:2O6X}.
FT   HELIX       226    236       {ECO:0000244|PDB:2O6X}.
FT   STRAND      239    243       {ECO:0000244|PDB:2O6X}.
FT   HELIX       247    250       {ECO:0000244|PDB:2O6X}.
FT   STRAND      252    257       {ECO:0000244|PDB:2O6X}.
FT   STRAND      269    279       {ECO:0000244|PDB:2O6X}.
FT   STRAND      282    288       {ECO:0000244|PDB:2O6X}.
FT   STRAND      300    304       {ECO:0000244|PDB:2O6X}.
FT   STRAND      306    309       {ECO:0000244|PDB:2O6X}.
FT   HELIX       310    312       {ECO:0000244|PDB:2O6X}.
FT   TURN        313    315       {ECO:0000244|PDB:2O6X}.
FT   STRAND      316    324       {ECO:0000244|PDB:2O6X}.
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
//
DBGET integrated database retrieval system