CPR1_CAEEL
ID CPR1_CAEEL Reviewed; 329 AA.
AC P25807; Q18783;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Gut-specific cysteine proteinase;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=cpr-1; Synonyms=gcp-1; ORFNames=C52E4.1;
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], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=1574082; DOI=10.1016/0166-6851(92)90074-t;
RA Ray C., McKerrow J.H.;
RT "Gut-specific and developmental expression of a Caenorhabditis elegans
RT cysteine protease gene.";
RL Mol. Biochem. Parasitol. 51:239-250(1992).
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 SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9761670; DOI=10.1006/jmbi.1998.2093;
RA Britton C., McKerrow J.H., Johnstone I.L.;
RT "Regulation of the Caenorhabditis elegans gut cysteine protease gene cpr-1:
RT requirement for GATA motifs.";
RL J. Mol. Biol. 283:15-27(1998).
CC -!- FUNCTION: Thiol protease. Has a role as a digestive enzyme.
CC {ECO:0000269|PubMed:1574082}.
CC -!- TISSUE SPECIFICITY: Larvae exhibit strong expression in gut cells and
CC weak expression in hypodermal cells. Adults exhibit the reverse: strong
CC expression in hypodermal cells and weaker expression in gut cells.
CC {ECO:0000269|PubMed:1574082, ECO:0000269|PubMed:9761670}.
CC -!- DEVELOPMENTAL STAGE: Larvae and adults, but not in embryos.
CC {ECO:0000269|PubMed:1574082, ECO:0000269|PubMed:9761670}.
CC -!- INDUCTION: Activated by a GATA-like transcription factor.
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; M74797; AAB88058.1; -; Genomic_DNA.
DR EMBL; Z78012; CAB01410.2; -; Genomic_DNA.
DR PIR; T20148; T20148.
DR RefSeq; NP_506002.2; NM_073601.9.
DR AlphaFoldDB; P25807; -.
DR SMR; P25807; -.
DR BioGRID; 44661; 21.
DR DIP; DIP-25619N; -.
DR STRING; 6239.C52E4.1; -.
DR MEROPS; C01.A32; -.
DR EPD; P25807; -.
DR PaxDb; P25807; -.
DR PeptideAtlas; P25807; -.
DR EnsemblMetazoa; C52E4.1.1; C52E4.1.1; WBGene00000781.
DR GeneID; 179637; -.
DR KEGG; cel:CELE_C52E4.1; -.
DR UCSC; C52E4.1; c. elegans.
DR CTD; 179637; -.
DR WormBase; C52E4.1; CE31896; WBGene00000781; cpr-1.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00970000196739; -.
DR HOGENOM; CLU_012184_3_3_1; -.
DR InParanoid; P25807; -.
DR OMA; KHIRDQA; -.
DR OrthoDB; 865289at2759; -.
DR PhylomeDB; P25807; -.
DR PRO; PR:P25807; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000781; Expressed in adult organism and 6 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: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; Hydrolase; Protease; Reference proteome; Signal;
KW Thiol protease; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..84
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026190"
FT CHAIN 85..329
FT /note="Gut-specific cysteine proteinase"
FT /id="PRO_0000026191"
FT ACT_SITE 113
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /evidence="ECO:0000250"
FT ACT_SITE 295
FT /evidence="ECO:0000250"
FT DISULFID 98..127
FT /evidence="ECO:0000250"
FT DISULFID 110..155
FT /evidence="ECO:0000250"
FT DISULFID 146..204
FT /evidence="ECO:0000250"
FT DISULFID 147..151
FT /evidence="ECO:0000250"
FT DISULFID 183..208
FT /evidence="ECO:0000250"
FT DISULFID 191..196
FT /evidence="ECO:0000250"
SQ SEQUENCE 329 AA; 35397 MW; 4FFD6F1B717B537D CRC64;
MKFLILTALC AVTLAFVPIN HQSAVETLTG QALVDYVNSA QSLFKTEHVE ITEEEMKFKL
MDGKYAAAHS DEIRATEQEV VLASVPATFD SRTQWSECKS IKLIRDQATC GSCWAFGAAE
MISDRTCIET KGAQQPIISP DDLLSCCGSS CGNGCEGGYP IQALRWWDSK GVVTGGDYHG
AGCKPYPIAP CTSGNCPESK TPSCSMSCQS GYSTAYAKDK HFGVSAYAVP KNAASIQAEI
YANGPVEAAF SVYEDFYKYK SGVYKHTAGK YLGGHAIKII GWGTESGSPY WLVANSWGVN
WGESGFFKIY RGDDQCGIES AVVAGKAKV
