ID P92005_CAEEL Unreviewed; 467 AA.
AC P92005;
DT 01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=cathepsin X {ECO:0000256|ARBA:ARBA00012516};
DE EC=3.4.18.1 {ECO:0000256|ARBA:ARBA00012516};
GN Name=cpz-2 {ECO:0000313|EMBL:CAB03209.1,
GN ECO:0000313|WormBase:M04G12.2};
GN ORFNames=CELE_M04G12.2 {ECO:0000313|EMBL:CAB03209.1}, M04G12.2
GN {ECO:0000313|WormBase:M04G12.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAB03209.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAB03209.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB03209.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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:0000256|ARBA:ARBA00001594};
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; BX284605; CAB03209.1; -; Genomic_DNA.
DR PIR; T23720; T23720.
DR RefSeq; NP_506318.1; NM_073917.6.
DR AlphaFoldDB; P92005; -.
DR SMR; P92005; -.
DR STRING; 6239.M04G12.2.1; -.
DR MEROPS; C01.A41; -.
DR EPD; P92005; -.
DR PaxDb; 6239-M04G12-2; -.
DR PeptideAtlas; P92005; -.
DR EnsemblMetazoa; M04G12.2.1; M04G12.2.1; WBGene00000789.
DR GeneID; 179818; -.
DR KEGG; cel:CELE_M04G12.2; -.
DR UCSC; M04G12.2; c. elegans.
DR AGR; WB:WBGene00000789; -.
DR WormBase; M04G12.2; CE12424; WBGene00000789; cpz-2.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000155569; -.
DR HOGENOM; CLU_568891_0_0_1; -.
DR InParanoid; P92005; -.
DR OMA; ATKKFEY; -.
DR OrthoDB; 2877448at2759; -.
DR PhylomeDB; P92005; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000789; Expressed in larva and 4 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd02698; Peptidase_C1A_CathepsinX; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR033157; CTSZ.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR PANTHER; PTHR12411:SF406; CATHEPSIN X; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|EPD:P92005,
KW ECO:0007829|PeptideAtlas:P92005};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..467
FT /note="cathepsin X"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018538428"
FT DOMAIN 221..459
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 467 AA; 53173 MW; 8E136D6C656F3C39 CRC64;
MNLKLIGFLF VIGTCQANLF NLPRAAIRLT REFTGMDKLP APEELGGEEY DMKIEVNNVV
EEMVDDMEDS SEEDTPLARV VNDDDLLYKK GFHLDSPFEL NKKVNKPVVR YPNIAKNNQK
IREEIVYPAD FDEHVVEILD SRKERKIDLS PMIKAKLEKG YYEPNDEALV DMSSESEESS
EEWEEARPYL KCGCLKKSGK VFESKTAPRE WESSSFKSND LPTGWDWRNV SGVNYCSPTR
NQHIPVYCGS CWVFGTTGAL NDRFNVARKG RWPMTQLSPQ EIIDCNGKGN CQGGEIGNVL
EHAKIQGLVE EGCNVYRATN GECNPYHRCG SCWPNECFSL TNYTRYYVKD YGQVQGRDKI
MSEIKKGGPI ACAIGATKKF EYEYVKGVYS EKSDLESNHI ISLTGWGVDE NGVEYWIARN
SWGEAWGELG WFRVVTSKFK DGQGDQYNMG IERDCYYADV DVSNLTF
//
