CPR6_CAEEL
ID CPR6_CAEEL Reviewed; 379 AA.
AC P43510;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Cathepsin B-like cysteine proteinase 6;
DE EC=3.4.22.-;
DE AltName: Full=Cysteine protease-related 6;
DE Flags: Precursor;
GN Name=cpr-6; ORFNames=C25B8.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Bristol N2;
RX PubMed=8561899; DOI=10.1089/dna.1996.15.75;
RA Larminie C.G.C., Johnstone I.L.;
RT "Isolation and characterization of four developmentally regulated cathepsin
RT B-like cysteine protease genes from the nematode Caenorhabditis elegans.";
RL DNA Cell Biol. 15:75-82(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196 AND ASN-201, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196 AND ASN-201, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; L39894; AAA98787.1; -; mRNA.
DR EMBL; L39939; AAA98789.1; -; Genomic_DNA.
DR EMBL; FO080666; CCD65628.1; -; Genomic_DNA.
DR PIR; T37274; T37274.
DR RefSeq; NP_741818.1; NM_171708.6.
DR AlphaFoldDB; P43510; -.
DR SMR; P43510; -.
DR BioGRID; 45860; 4.
DR DIP; DIP-25139N; -.
DR IntAct; P43510; 1.
DR STRING; 6239.C25B8.3a; -.
DR MEROPS; C01.A51; -.
DR iPTMnet; P43510; -.
DR EPD; P43510; -.
DR PaxDb; P43510; -.
DR PeptideAtlas; P43510; -.
DR EnsemblMetazoa; C25B8.3.1; C25B8.3.1; WBGene00000786.
DR GeneID; 180931; -.
DR KEGG; cel:CELE_C25B8.3; -.
DR UCSC; C25B8.3a; c. elegans.
DR CTD; 180931; -.
DR WormBase; C25B8.3; CE04078; WBGene00000786; cpr-6.
DR eggNOG; KOG1543; Eukaryota.
DR InParanoid; P43510; -.
DR OMA; CCKSCGF; -.
DR OrthoDB; 865289at2759; -.
DR PhylomeDB; P43510; -.
DR BRENDA; 3.4.22.B6; 1045.
DR Reactome; R-CEL-2132295; MHC class II antigen presentation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:P43510; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000786; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:WormBase.
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 InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
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.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal; Thiol protease; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..104
FT /evidence="ECO:0000255"
FT /id="PRO_0000026198"
FT CHAIN 105..379
FT /note="Cathepsin B-like cysteine proteinase 6"
FT /id="PRO_0000026199"
FT ACT_SITE 133
FT /evidence="ECO:0000250"
FT ACT_SITE 305
FT /evidence="ECO:0000250"
FT ACT_SITE 325
FT /evidence="ECO:0000250"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:15888633, ECO:0000269|PubMed:17761667"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine; atypical"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT DISULFID 118..147
FT /evidence="ECO:0000250"
FT DISULFID 130..174
FT /evidence="ECO:0000250"
FT DISULFID 166..233
FT /evidence="ECO:0000250"
FT DISULFID 167..170
FT /evidence="ECO:0000250"
FT DISULFID 203..237
FT /evidence="ECO:0000250"
FT DISULFID 211..223
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 42404 MW; 4087369E06192F5F CRC64;
MKTLLFLSCI VVAAYCACND NLESVLDKYR NREIDSEAAE LDGDDLIDYV NENQNLWTAK
KQRRFSSVYG ENDKAKWGLM GVNHVRLSVK GKQHLSKTKD LDLDIPESFD SRDNWPKCDS
IKVIRDQSSC GSCWAFGAVE AMSDRICIAS HGELQVTLSA DDLLSCCKSC GFGCNGGDPL
AAWRYWVKDG IVTGSNYTAN NGCKPYPFPP CEHHSKKTHF DPCPHDLYPT PKCEKKCVSD
YTDKTYSEDK FFGASAYGVK DDVEAIQKEL MTHGPLEIAF EVYEDFLNYD GGVYVHTGGK
LGGGHAVKLI GWGIDDGIPY WTVANSWNTD WGEDGFFRIL RGVDECGIES GVVGGIPKLN
SLTSRLHRHH RRHVYDDNY
