CATZ1_CAEEL
ID CATZ1_CAEEL Reviewed; 306 AA.
AC G5EGP8; A0A078BPL2;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cathepsin Z-1 {ECO:0000303|PubMed:14630920, ECO:0000312|WormBase:F32B5.8a};
DE EC=3.4.18.1 {ECO:0000250|UniProtKB:Q9UBR2};
DE Flags: Precursor;
GN Name=cpz-1 {ECO:0000303|PubMed:14630920, ECO:0000312|WormBase:F32B5.8a};
GN ORFNames=F32B5.8 {ECO:0000312|WormBase:F32B5.8a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:DAA01510.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16857685; DOI=10.1074/jbc.m600254200;
RA Hashmi S., Zhang J., Oksov Y., Ji Q., Lustigman S.;
RT "The Caenorhabditis elegans CPI-2a cystatin-like inhibitor has an essential
RT regulatory role during oogenesis and fertilization.";
RL J. Biol. Chem. 281:28415-28429(2006).
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 (PubMed:14630920). Probably, required for the
CC degradation of the old cuticle (PubMed:14630920).
CC {ECO:0000250|UniProtKB:Q9UBR2, ECO:0000269|PubMed:14630920}.
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-38 in the
CC propeptide and the active site residue Cys-95 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: Secreted {ECO:0000269|PubMed:14630920,
CC ECO:0000269|PubMed:16857685}. Cytoplasmic granule
CC {ECO:0000269|PubMed:16857685}. Note=In molting larvae, localizes in
CC both the new and old cuticles, specifically at the interface where the
CC old cuticle is being degraded before ecdysis (PubMed:14630920).
CC Localizes to yolk granules in the developing oocyte (PubMed:16857685).
CC {ECO:0000269|PubMed:14630920, ECO:0000269|PubMed:16857685}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F32B5.8a};
CC IsoId=G5EGP8-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F32B5.8b};
CC IsoId=G5EGP8-2; Sequence=VSP_060183;
CC -!- TISSUE SPECIFICITY: Expressed in hypodermis, cuticle and pharynx (at
CC protein level) (PubMed:14630920, PubMed:16857685). Expressed in germ
CC cells, developing oocytes, sheath cells surrounding germ cells and
CC oocytes, and in the eggshell (at protein level) (PubMed:16857685). Not
CC expressed in sperm (PubMed:16857685). {ECO:0000269|PubMed:14630920,
CC ECO:0000269|PubMed:16857685}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adults (at
CC protein level) (PubMed:14630920, PubMed:16857685). In larvae, only
CC expressed in hypodermis and cuticle (at protein level)
CC (PubMed:14630920, PubMed:16857685). Expressed in the ecdysed cuticle
CC during molting (at protein level) (PubMed:16857685). Expression
CC transiently increases during early embryonic stages and prior to the
CC larval L2/L3, L3/L4 and L4/adult molts (PubMed:14630920,
CC PubMed:16857685). {ECO:0000269|PubMed:14630920,
CC ECO:0000269|PubMed:16857685}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an arrest at the
CC 50-cell embryonic stage. The few surviving animals are arrested at the
CC larval L2 to L3 molt with their cuticle remaining attached to the mid-
CC portion of the body. RNAi-mediated knockdown at various larval stages
CC causes severe defects in molting. {ECO:0000269|PubMed:14630920}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255,
CC ECO:0000255|RuleBase:RU362133}.
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DR EMBL; BK001409; DAA01510.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD70407.1; -; Genomic_DNA.
DR EMBL; BX284601; CDX47496.1; -; Genomic_DNA.
DR PIR; T29872; T29872.
DR RefSeq; NP_001293391.1; NM_001306462.1.
DR RefSeq; NP_491023.2; NM_058622.5. [G5EGP8-1]
DR AlphaFoldDB; G5EGP8; -.
DR SMR; G5EGP8; -.
DR IntAct; G5EGP8; 1.
DR STRING; 6239.F32B5.8; -.
DR MEROPS; C01.A38; -.
DR EPD; G5EGP8; -.
DR PaxDb; G5EGP8; -.
DR PeptideAtlas; G5EGP8; -.
DR EnsemblMetazoa; F32B5.8a.1; F32B5.8a.1; WBGene00000788. [G5EGP8-1]
DR EnsemblMetazoa; F32B5.8b.1; F32B5.8b.1; WBGene00000788. [G5EGP8-2]
DR GeneID; 171829; -.
DR KEGG; cel:CELE_F32B5.8; -.
DR CTD; 171829; -.
DR WormBase; F32B5.8a; CE36646; WBGene00000788; cpz-1. [G5EGP8-1]
DR WormBase; F32B5.8b; CE50019; WBGene00000788; cpz-1. [G5EGP8-2]
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00990000209842; -.
DR InParanoid; G5EGP8; -.
DR OMA; ECHTIQN; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; G5EGP8; -.
DR Reactome; R-CEL-204005; COPII-mediated vesicle transport.
DR Reactome; R-CEL-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-CEL-5694530; Cargo concentration in the ER.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:G5EGP8; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000788; Expressed in adult organism and 4 other tissues.
DR GO; GO:0060102; C:collagen and cuticulin-based cuticle extracellular matrix; IDA:WormBase.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0042718; C:yolk granule; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0042395; P:ecdysis, collagen and cuticulin-based cuticle; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0035262; P:gonad morphogenesis; IMP:WormBase.
DR GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:WormBase.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
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 PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..64
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT /id="PRO_0000447362"
FT CHAIN 65..306
FT /note="Cathepsin Z-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5015019728"
FT ACT_SITE 95
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 DISULFID 38..95
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 92..135
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 129..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 VAR_SEQ 1..136
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060183"
SQ SEQUENCE 306 AA; 34741 MW; F733DBA195A6C10A CRC64;
MRTFVLLLAL CAICILASSA YGKVRKYSNR NRYNLKGCYK QTGRVFEHKR YDRIYETEDF
DSEDLPKTWD WRDANGINYA SADRNQHIPQ YCGSCWAFGA TSALADRINI KRKNAWPQAY
LSVQEVIDCS GAGTCVMGGE PGGVYKYAHE HGIPHETCNN YQARDGKCDP YNRCGSCWPG
ECFSIKNYTL YKVSEYGTVH GYEKMKAEIY HKGPIACGIA ATKAFETYAG GIYKEVTDED
IDHIISVHGW GVDHESGVEY WIGRNSWGEP WGEHGWFKIV TSQYKNAGSK YNLKIEEDCV
WADPIV
