CYSP3_DICDI
ID CYSP3_DICDI Reviewed; 337 AA.
AC Q23894; Q54QL2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cysteine proteinase 3;
DE EC=3.4.22.-;
DE AltName: Full=Cysteine proteinase II;
DE Flags: Precursor;
GN Name=cprC; Synonyms=CP3; ORFNames=DDB_G0283867;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-198.
RC STRAIN=AX2;
RA Presse F., Bogdanovsky-Sequeval D., Mathieu M., Felenbok B.;
RT "Structural analysis of a developmentally regulated sequence encoding for a
RT cysteine proteinase in Dictyostelium discoideum.";
RL Mol. Gen. Genet. 203:324-332(1986).
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR EMBL; AAFI02000057; EAL65548.1; -; Genomic_DNA.
DR EMBL; X03930; CAA27569.1; -; Genomic_DNA.
DR RefSeq; XP_638859.1; XM_633767.1.
DR AlphaFoldDB; Q23894; -.
DR SMR; Q23894; -.
DR STRING; 44689.DDB0220784; -.
DR MEROPS; C01.A55; -.
DR MEROPS; I29.003; -.
DR PaxDb; Q23894; -.
DR EnsemblProtists; EAL65548; EAL65548; DDB_G0283867.
DR GeneID; 8624257; -.
DR KEGG; ddi:DDB_G0283867; -.
DR dictyBase; DDB_G0283867; cprC.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; Q23894; -.
DR OMA; ETCCCAK; -.
DR PhylomeDB; Q23894; -.
DR Reactome; R-DDI-1442490; Collagen degradation.
DR Reactome; R-DDI-1474228; Degradation of the extracellular matrix.
DR Reactome; R-DDI-2132295; MHC class II antigen presentation.
DR Reactome; R-DDI-5683826; Surfactant metabolism.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q23894; -.
DR Proteomes; UP000002195; Chromosome 4.
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:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Hydrolase; Lysosome; Protease; Reference proteome; Signal;
KW Thiol protease; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..120
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000312513"
FT CHAIN 121..337
FT /note="Cysteine proteinase 3"
FT /id="PRO_0000050544"
FT ACT_SITE 145
FT /evidence="ECO:0000250"
FT ACT_SITE 284
FT /evidence="ECO:0000250"
FT ACT_SITE 304
FT /evidence="ECO:0000250"
FT DISULFID 142..185
FT /evidence="ECO:0000250"
FT DISULFID 176..219
FT /evidence="ECO:0000250"
FT DISULFID 277..326
FT /evidence="ECO:0000250"
FT CONFLICT 118
FT /note="Q -> H (in Ref. 2; CAA27569)"
FT /evidence="ECO:0000305"
FT CONFLICT 146..148
FT /note="YSF -> II (in Ref. 2; CAA27569)"
FT /evidence="ECO:0000305"
FT CONFLICT 175..176
FT /note="DC -> RL (in Ref. 2; CAA27569)"
FT /evidence="ECO:0000305"
FT CONFLICT 191..197
FT /note="TNAFEYI -> KLFVYS (in Ref. 2; CAA27569)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37806 MW; 727566BBFA263F1B CRC64;
MRLSITLIFT LIVLSISFIS AGNVFSHKQY QDSFIDWMRS NNKAYTHKEF MPRYEEFKKN
MDYVHNWNSK GSKTVLGLNQ HADLSNEEYR LNYLGTRAHI KLNGYHKRNL GLRLNRPQFK
QPLNVDWREK DAVTPVKDQG QCGSCYSFST TGSVEGVTAI KTGKLVSLSE QNILDCSSSF
GNEGCNGGLM TNAFEYIIKN NGLNSEEQYP YEMKVNDECK FQEGSVAAKI TSYKEIEAGD
ENDLQNALLL NPVSVAIDAS HNSFQLYTAG VYYEPACSSE DLDHGVLAVG MGTDNGEDYY
IVKNSWGPSW GLNGYIHMAR NKDNNCGIST MASYPIA
