CATZ_ONCVO
ID CATZ_ONCVO Reviewed; 306 AA.
AC Q6PN98; A0A2K6VYR4; P91771;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Cathepsin Z {ECO:0000305};
DE EC=3.4.18.1 {ECO:0000250|UniProtKB:Q9UBR2};
DE AltName: Full=L3 cysteine protease {ECO:0000303|PubMed:8939969};
DE Short=LOVCP {ECO:0000303|PubMed:8939969};
DE Flags: Precursor;
GN Name=cpz {ECO:0000303|PubMed:14630920};
OS Onchocerca volvulus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=6282 {ECO:0000312|EMBL:AAT00789.1};
RN [1] {ECO:0000312|EMBL:AAC47348.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=8939969; DOI=10.1074/jbc.271.47.30181;
RA Lustigman S., McKerrow J.H., Shah K., Lui J., Huima T., Hough M.,
RA Brotman B.;
RT "Cloning of a cysteine protease required for the molting of Onchocerca
RT volvulus third stage larvae.";
RL J. Biol. Chem. 271:30181-30189(1996).
RN [2] {ECO:0000312|EMBL:AAC47348.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Forest {ECO:0000312|EMBL:AAC47348.1};
RX PubMed=16186127; DOI=10.1074/jbc.m504434200;
RA Ford L., Guiliano D.B., Oksov Y., Debnath A.K., Liu J., Williams S.A.,
RA Blaxter M.L., Lustigman S.;
RT "Characterization of a novel filarial serine protease inhibitor, Ov-SPI-1,
RT from Onchocerca volvulus, with potential multifunctional roles during
RT development of the parasite.";
RL J. Biol. Chem. 280:40845-40856(2005).
RN [3] {ECO:0000312|EMBL:AAT00789.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15555728; DOI=10.1016/j.molbiopara.2004.08.003;
RA Lustigman S., Zhang J., Liu J., Oksov Y., Hashmi S.;
RT "RNA interference targeting cathepsin L and Z-like cysteine proteases of
RT Onchocerca volvulus confirmed their essential function during L3 molting.";
RL Mol. Biochem. Parasitol. 138:165-170(2004).
RN [4] {ECO:0000312|Proteomes:UP000024404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Cotton J., Tsai J., Stanley E., Tracey A., Holroyd N., Lustigman S.,
RA Berriman M.;
RT "Genome sequencing of Onchocerca volvulus.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE NAME.
RX PubMed=14630920; DOI=10.1074/jbc.m312346200;
RA Hashmi S., Zhang J., Oksov Y., Lustigman S.;
RT "The Caenorhabditis elegans cathepsin Z-like cysteine protease, Ce-CPZ-1,
RT has a multifunctional role during the worms' development.";
RL J. Biol. Chem. 279:6035-6045(2004).
CC -!- FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase
CC activity (By similarity). Plays an essential role in molting, a process
CC during larval stages in which a new cuticle is formed and the old
CC cuticle is shed (Probable) (PubMed:15555728). Required for the
CC degradation and shedding of the old cuticle (Probable)
CC (PubMed:15555728). {ECO:0000250|UniProtKB:Q9UBR2,
CC ECO:0000269|PubMed:15555728, ECO:0000305|PubMed:8939969}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of C-terminal amino acid residues with broad
CC specificity, but lacks action on C-terminal proline. Shows weak
CC endopeptidase activity.; EC=3.4.18.1;
CC Evidence={ECO:0000250|UniProtKB:Q9UBR2};
CC -!- ACTIVITY REGULATION: The disulfide bridge formed between Cys-39 in the
CC propeptide and the active site residue Cys-96 may prevent activation of
CC the zymogen through formation of a reversible covalent bond with the
CC active site residue. {ECO:0000250|UniProtKB:Q9UBR2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000269|PubMed:8939969}. Secreted {ECO:0000269|PubMed:8939969}.
CC Note=Localizes in secretory vesicles in the hypodermis of L3 larvae.
CC {ECO:0000269|PubMed:8939969}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larvae during the L3/L4 molting
CC stage, specifically in both the old and new cuticles (PubMed:8939969,
CC PubMed:16186127, PubMed:15555728). In L3 larvae, expressed in the
CC hypodermis, the basal lamina of the pseudocoelom, the glandular part of
CC the esophagus and in cells of the epidermal cord (PubMed:8939969,
CC PubMed:15555728). {ECO:0000269|PubMed:15555728,
CC ECO:0000269|PubMed:16186127, ECO:0000269|PubMed:8939969}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in L3 larvae impairs the
CC separation between the L3 cuticle and the newly synthesized L4 cuticle
CC resulting in incomplete molting. {ECO:0000269|PubMed:15555728}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255,
CC ECO:0000255|RuleBase:RU362133}.
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DR EMBL; U71150; AAC47348.1; -; mRNA.
DR EMBL; AY591516; AAT00789.1; -; Genomic_DNA.
DR EMBL; CMVM020000017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q6PN98; -.
DR SMR; Q6PN98; -.
DR STRING; 6282.Q6PN98; -.
DR MEROPS; C01.087; -.
DR HOGENOM; CLU_012184_2_1_1; -.
DR Proteomes; UP000024404; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0099503; C:secretory vesicle; IDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042395; P:ecdysis, collagen and cuticulin-based cuticle; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02698; Peptidase_C1A_CathepsinX; 1.
DR InterPro; IPR033157; CTSZ.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR PANTHER; PTHR12411:SF569; PTHR12411:SF569; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..65
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT /id="PRO_0000447511"
FT CHAIN 66..306
FT /note="Cathepsin Z"
FT /evidence="ECO:0000255"
FT /id="PRO_5005400853"
FT ACT_SITE 96
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT ACT_SITE 243
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT ACT_SITE 265
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 39..96
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 93..136
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 130..168
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 158..174
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 177..182
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 217..299
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT CONFLICT 247
FT /note="A -> V (in Ref. 2; AAC47348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 34424 MW; 8AF4E4FDC6FB0E01 CRC64;
MLAILFNFFL LTYFTNITLG KVGKSIDLDT RNGYNVHGCY KQTGKIYAHK TYPRQYEAEN
YNFDDLPVAW DWRNINGVNY ASVDRNQHIP QYCGSCWAFG STSALADRFN IKRKGAWPPA
YLSVQEVIDC ANAGSCEGGE PGPVYKYAHE FGIPHETCNN YQARDGTCSS YNKCGSCWPG
SCFSIKNYTI YRVKNYGAVS GLHKMKAEIY HHGPIACGIA ATKAFETYAG GIYNERTNED
IDHIISAHGW GVDSESGVPY WIGRNSWGTP WGENGWFRIV TSEYKNSSSK YNLKIEEDCV
WADPIA
