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Cathepsin L-like proteinase (EC 3.4.22.-)

 CATLL_FASHE             Reviewed;         326 AA.
Q24940; P91727;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-JUL-2017, entry version 71.
RecName: Full=Cathepsin L-like proteinase;
EC=3.4.22.-;
Flags: Precursor;
Name=Cat-1 {ECO:0000303|PubMed:8192668};
Fasciola hepatica (Liver fluke).
Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea;
Plagiorchiida; Echinostomata; Echinostomatoidea; Fasciolidae;
Fasciola.
NCBI_TaxID=6192;
[1] {ECO:0000305, ECO:0000312|EMBL:AAA29136.1}
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 107-122; 188-206 AND
277-291, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND
HYDROXYLATION AT PRO-109 AND PRO-196.
STRAIN=Crompton {ECO:0000312|EMBL:AAA29136.1};
PubMed=8192668; DOI=10.1042/bj2990781;
Wijffels G.L., Panaccio M., Salvatore L., Wilson L., Walker I.D.,
Spithill T.W.;
"The secreted cathepsin L-like proteinases of the trematode Fasciola
hepatica, contain 3-hydroxyproline residues.";
Biochem. J. 299:781-790(1994).
-!- FUNCTION: Thiol protease. Probably involved in interaction with
host tissues. Displays a similar activity to that of papain. Has
high activity on Z-Phe-Arg-NHMec, but no activity on Z-Arg-NHMec.
{ECO:0000269|PubMed:8192668, ECO:0000303|PubMed:8192668}.
-!- ENZYME REGULATION: Strongly inhibited by Antipain, E64 and
Leupeptin, and weakly inhibited by iodoacetic acid (IAA) and
phenylmethylsulfonyl fluoride (PMSF). Requires the presence of
dithiothreitol (DTT) for activity. {ECO:0000269|PubMed:8192668}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=46 uM for Z-Phe-Arg-NHMec (at pH 7.45)
{ECO:0000269|PubMed:8192668};
pH dependence:
Optimum pH is 7-9 in a mixed-buffer system. In a Tris buffer
high levels of activity were detected at very alkaline pHs.
{ECO:0000269|PubMed:8192668};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8192668}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8192668}.
-!- PTM: Contains cysteine residues involved in intramolecular
disulfide bonding. {ECO:0000269|PubMed:8192668}.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
-!- CAUTION: It is not clear whether the mature peptide starts at Ala-
107 or at Val-108. {ECO:0000305}.
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EMBL; L33771; AAA29136.1; -; mRNA.
PIR; S43991; S43991.
PDB; 2O6X; X-ray; 1.40 A; A=17-326.
PDBsum; 2O6X; -.
ProteinModelPortal; Q24940; -.
SMR; Q24940; -.
MEROPS; C01.033; -.
BRENDA; 3.4.22.B49; 2230.
BRENDA; 3.4.22.B60; 2230.
EvolutionaryTrace; Q24940; -.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
InterPro; IPR013201; Prot_inhib_I29.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF08246; Inhibitor_I29; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00848; Inhibitor_I29; 1.
SMART; SM00645; Pept_C1; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
Hydroxylation; Protease; Secreted; Signal; Thiol protease; Zymogen.
SIGNAL 1 15 {ECO:0000255}.
PROPEP 16 106 Activation peptide. {ECO:0000255,
ECO:0000269|PubMed:8192668}.
/FTId=PRO_0000042858.
CHAIN 107 326 Cathepsin L-like proteinase.
{ECO:0000269|PubMed:8192668}.
/FTId=PRO_0000042859.
ACT_SITE 132 132 {ECO:0000250|UniProtKB:P07711}.
ACT_SITE 269 269 {ECO:0000250|UniProtKB:P07711}.
ACT_SITE 289 289 {ECO:0000250|UniProtKB:P07711}.
MOD_RES 109 109 3-hydroxyproline; partial.
{ECO:0000269|PubMed:8192668}.
MOD_RES 196 196 3-hydroxyproline; partial.
{ECO:0000269|PubMed:8192668}.
DISULFID 129 172 {ECO:0000250|UniProtKB:P25774}.
DISULFID 163 204 {ECO:0000250|UniProtKB:P25774}.
DISULFID 262 311 {ECO:0000250|UniProtKB:P25774}.
HELIX 18 28 {ECO:0000244|PDB:2O6X}.
HELIX 34 59 {ECO:0000244|PDB:2O6X}.
STRAND 62 67 {ECO:0000244|PDB:2O6X}.
TURN 71 74 {ECO:0000244|PDB:2O6X}.
HELIX 77 84 {ECO:0000244|PDB:2O6X}.
HELIX 91 94 {ECO:0000244|PDB:2O6X}.
STRAND 97 100 {ECO:0000244|PDB:2O6X}.
HELIX 114 117 {ECO:0000244|PDB:2O6X}.
HELIX 132 149 {ECO:0000244|PDB:2O6X}.
HELIX 157 163 {ECO:0000244|PDB:2O6X}.
HELIX 165 167 {ECO:0000244|PDB:2O6X}.
HELIX 171 173 {ECO:0000244|PDB:2O6X}.
HELIX 177 184 {ECO:0000244|PDB:2O6X}.
TURN 192 194 {ECO:0000244|PDB:2O6X}.
HELIX 208 210 {ECO:0000244|PDB:2O6X}.
STRAND 213 221 {ECO:0000244|PDB:2O6X}.
HELIX 226 236 {ECO:0000244|PDB:2O6X}.
STRAND 239 243 {ECO:0000244|PDB:2O6X}.
HELIX 247 250 {ECO:0000244|PDB:2O6X}.
STRAND 252 257 {ECO:0000244|PDB:2O6X}.
STRAND 269 279 {ECO:0000244|PDB:2O6X}.
STRAND 282 288 {ECO:0000244|PDB:2O6X}.
STRAND 300 304 {ECO:0000244|PDB:2O6X}.
STRAND 306 309 {ECO:0000244|PDB:2O6X}.
HELIX 310 312 {ECO:0000244|PDB:2O6X}.
TURN 313 315 {ECO:0000244|PDB:2O6X}.
STRAND 316 324 {ECO:0000244|PDB:2O6X}.
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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