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CPR3_CAEEL
ID   CPR3_CAEEL              Reviewed;         370 AA.
AC   P43507; Q9TW93;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Cathepsin B-like cysteine proteinase 3;
DE            EC=3.4.22.-;
DE   AltName: Full=Cysteine protease-related 3;
DE   Flags: Precursor;
GN   Name=cpr-3; ORFNames=T10H4.12;
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).
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; L39890; AAA98788.1; -; mRNA.
DR   EMBL; L39925; AAA98782.1; -; Genomic_DNA.
DR   EMBL; Z81119; CAB61032.2; -; Genomic_DNA.
DR   EMBL; Z82057; CAB61032.2; JOINED; Genomic_DNA.
DR   PIR; T37282; T37282.
DR   RefSeq; NP_506790.1; NM_074389.3.
DR   AlphaFoldDB; P43507; -.
DR   SMR; P43507; -.
DR   STRING; 6239.T10H4.12; -.
DR   MEROPS; C01.A33; -.
DR   EPD; P43507; -.
DR   PaxDb; P43507; -.
DR   PeptideAtlas; P43507; -.
DR   EnsemblMetazoa; T10H4.12.1; T10H4.12.1; WBGene00000783.
DR   GeneID; 180033; -.
DR   KEGG; cel:CELE_T10H4.12; -.
DR   UCSC; T10H4.12; c. elegans.
DR   CTD; 180033; -.
DR   WormBase; T10H4.12; CE27590; WBGene00000783; cpr-3.
DR   eggNOG; KOG1543; Eukaryota.
DR   HOGENOM; CLU_012184_3_3_1; -.
DR   InParanoid; P43507; -.
DR   OMA; DEKIPYW; -.
DR   OrthoDB; 865289at2759; -.
DR   PhylomeDB; P43507; -.
DR   PRO; PR:P43507; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00000783; Expressed in adult organism and 2 other tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; HEP:WormBase.
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   2: Evidence at transcript 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..91
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026192"
FT   CHAIN           92..370
FT                   /note="Cathepsin B-like cysteine proteinase 3"
FT                   /id="PRO_0000026193"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        284
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        105..134
FT                   /evidence="ECO:0000250"
FT   DISULFID        117..162
FT                   /evidence="ECO:0000250"
FT   DISULFID        153..210
FT                   /evidence="ECO:0000250"
FT   DISULFID        154..158
FT                   /evidence="ECO:0000250"
FT   DISULFID        190..214
FT                   /evidence="ECO:0000250"
FT   DISULFID        198..202
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   370 AA;  40770 MW;  E6E50FF7C16F0867 CRC64;
     MLKVYFLALF LAGCSAFVLD EIRGINIGQS PQKVLVDHVN TVQTSWVAEH NEISEFEMKF
     KVMDVKFAEP LEKDSDVASE LFVRGEIVPE PLPDTFDARE KWPDCNTIKL IRNQATCGSC
     WAFGAAEVIS DRVCIQSNGT QQPVISVEDI LSCCGTTCGY GCKGGYSIEA LRFWASSGAV
     TGGDYGGHGC MPYSFAPCTK NCPESTTPSC KTTCQSSYKT EEYKKDKHYG ASAYKVTTTK
     SVTEIQTEIY HYGPVEASYK VYEDFYHYKS GVYHYTSGKL VGGHAVKIIG WGVENGVDYW
     LIANSWGTSF GEKGFFKIRR GTNECQIEGN VVAGIAKLGT HSETYEDDGG AATSCSFIMC
     TLMVLTYYFV
 
 
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