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Cathepsin B-like cysteine proteinase 4 (EC 3.4.22.-) (Cysteine protease-related 4)

 CPR4_CAEEL              Reviewed;         335 AA.
P43508;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
23-MAY-2018, entry version 135.
RecName: Full=Cathepsin B-like cysteine proteinase 4;
EC=3.4.22.-;
AltName: Full=Cysteine protease-related 4;
Flags: Precursor;
Name=cpr-4; ORFNames=F44C4.3;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=Bristol N2;
PubMed=8561899; DOI=10.1089/dna.1996.15.75;
Larminie C.G.C., Johnstone I.L.;
"Isolation and characterization of four developmentally regulated
cathepsin B-like cysteine protease genes from the nematode
Caenorhabditis elegans.";
DNA Cell Biol. 15:75-82(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION,
DISRUPTION PHENOTYPE, ACTIVE SITES, MUTAGENESIS OF CYS-109; HIS-281
AND ASN-301, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=28723894; DOI=10.1038/nature23284;
Peng Y., Zhang M., Zheng L., Liang Q., Li H., Chen J.T., Guo H.,
Yoshina S., Chen Y.Z., Zhao X., Wu X., Liu B., Mitani S., Yu J.S.,
Xue D.;
"Cysteine protease cathepsin B mediates radiation-induced bystander
effects.";
Nature 547:458-462(2017).
-!- FUNCTION: Thiol protease which shows activity against the
fluorogenic substrate z-Arg-Arg-AMC.
{ECO:0000269|PubMed:28723894}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28723894}.
Note=Secreted from animals irradiated with ultraviolet or ionizing
gamma rays into the culture medium. {ECO:0000269|PubMed:28723894}.
-!- DEVELOPMENTAL STAGE: Not detected in the embryo, observed in the
intestine of early stage L1-L3 larvae, peaks at the L4 larval
stage and declines in adulthood. {ECO:0000269|PubMed:28723894}.
-!- INDUCTION: Induced by ultraviolet and ionizing radiation through a
cep-1-dependent mechanism. {ECO:0000269|PubMed:28723894}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in greatly
reduced radiation-induced bystander effect (RIBE) activity in the
culture medium of irradiated animals.
{ECO:0000269|PubMed:28723894}.
-!- MISCELLANEOUS: Mediates the radiation-induced bystander effect
(RIBE), a process in which factors released by irradiated cells or
tissues exert effects on unexposed cells or tissues. Following
localized ultraviolet irradiation of the head, mediates RIBE in
multiple unexposed regions including the posterior region. Also
leads to RIBE including inhibition of cell death and increased
embryonic lethality of progeny in unirradiated animals exposed to
the culture medium of irradiated animals. Likely to exert RIBE by
acting through the insulin-like receptor daf-2.
{ECO:0000269|PubMed:28723894}.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
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EMBL; L39895; AAA98785.1; -; mRNA.
EMBL; L39926; AAA98783.1; -; Genomic_DNA.
EMBL; FO081381; CCD71204.1; -; Genomic_DNA.
PIR; T37280; T37280.
RefSeq; NP_504682.1; NM_072281.5.
UniGene; Cel.5404; -.
ProteinModelPortal; P43508; -.
BioGrid; 44098; 2.
DIP; DIP-25376N; -.
IntAct; P43508; 1.
STRING; 6239.F44C4.3; -.
MEROPS; C01.A34; -.
EPD; P43508; -.
PaxDb; P43508; -.
PeptideAtlas; P43508; -.
PRIDE; P43508; -.
EnsemblMetazoa; F44C4.3; F44C4.3; WBGene00000784.
GeneID; 179053; -.
KEGG; cel:CELE_F44C4.3; -.
UCSC; F44C4.3; c. elegans.
CTD; 179053; -.
WormBase; F44C4.3; CE07251; WBGene00000784; cpr-4.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140859; -.
HOGENOM; HOG000241341; -.
InParanoid; P43508; -.
KO; K01363; -.
OMA; LAPCGET; -.
OrthoDB; EOG091G094Z; -.
PhylomeDB; P43508; -.
Reactome; R-CEL-1442490; Collagen degradation.
Reactome; R-CEL-2132295; MHC class II antigen presentation.
Reactome; R-CEL-6798695; Neutrophil degranulation.
PRO; PR:P43508; -.
Proteomes; UP000001940; Chromosome V.
Bgee; WBGene00000784; -.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005764; C:lysosome; IBA:GO_Central.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0071480; P:cellular response to gamma radiation; IMP:UniProtKB.
GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:UniProtKB.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00645; Pept_C1; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Protease;
Reference proteome; Secreted; Signal; Thiol protease; Zymogen.
SIGNAL 1 15 {ECO:0000255}.
PROPEP 16 80 {ECO:0000255}.
/FTId=PRO_0000026194.
CHAIN 81 335 Cathepsin B-like cysteine proteinase 4.
/FTId=PRO_0000026195.
ACT_SITE 109 109 {ECO:0000269|PubMed:28723894}.
ACT_SITE 281 281 {ECO:0000269|PubMed:28723894}.
ACT_SITE 301 301 {ECO:0000250|UniProtKB:P07858}.
CARBOHYD 193 193 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 94 123 {ECO:0000250|UniProtKB:P07858}.
DISULFID 106 150 {ECO:0000250|UniProtKB:P07858}.
DISULFID 142 209 {ECO:0000250|UniProtKB:P07858}.
DISULFID 143 146 {ECO:0000250|UniProtKB:P07858}.
DISULFID 179 213 {ECO:0000250|UniProtKB:P07858}.
DISULFID 187 199 {ECO:0000250|UniProtKB:P07858}.
MUTAGEN 109 109 C->A: Loss of protease and RIBE activity.
{ECO:0000269|PubMed:28723894}.
MUTAGEN 281 281 H->A: Loss of protease and RIBE activity.
{ECO:0000269|PubMed:28723894}.
MUTAGEN 301 301 N->A: No effect on protease or RIBE
activity. {ECO:0000269|PubMed:28723894}.
SEQUENCE 335 AA; 36493 MW; 285900FAB876CED0 CRC64;
MKYLILAALV AVTAGLVIPL VPKTQEAITE YVNSKQSLWK AEIPKDITIE QVKKRLMRTE
FVAPHTPDVE VVKHDINEDT IPATFDARTQ WPNCMSINNI RDQSDCGSCW AFAAAEAASD
RFCIASNGAV NTLLSAEDVL SCCSNCGYGC EGGYPINAWK YLVKSGFCTG GSYEAQFGCK
PYSLAPCGET VGNVTWPSCP DDGYDTPACV NKCTNKNYNV AYTADKHFGS TAYAVGKKVS
QIQAEIIAHG PVEAAFTVYE DFYQYKTGVY VHTTGQELGG HAIRILGWGT DNGTPYWLVA
NSWNVNWGEN GYFRIIRGTN ECGIEHAVVG GVPKV


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