CYSP2_DICDI
ID CYSP2_DICDI Reviewed; 376 AA.
AC P04989; Q54W98;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cysteine proteinase 2;
DE EC=3.4.22.-;
DE AltName: Full=Prestalk cathepsin;
DE Flags: Precursor;
GN Name=cprB; Synonyms=CP2; ORFNames=DDB_G0279799;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3031453; DOI=10.1128/mcb.7.1.149-159.1987;
RA Datta S., Firtel R.A.;
RT "Identification of the sequences controlling cyclic AMP regulation and
RT cell-type-specific expression of a prestalk-specific gene in Dictyostelium
RT discoideum.";
RL Mol. Cell. Biol. 7:149-159(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3909109; DOI=10.1093/nar/13.24.8853;
RA Pears C.J., Mahbubani H.M., Williams J.G.;
RT "Characterization of two highly diverged but developmentally co-regulated
RT cysteine proteinase genes in Dictyostelium discoideum.";
RL Nucleic Acids Res. 13:8853-8866(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3023394; DOI=10.1083/jcb.103.5.1999;
RA Gomer R.H., Datta S., Firtel R.A.;
RT "Cellular and subcellular distribution of a cAMP-regulated prestalk protein
RT and prespore protein in Dictyostelium discoideum: a study on the ontogeny
RT of prestalk and prespore cells.";
RL J. Cell Biol. 103:1999-2015(1986).
RN [4]
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).
CC -!- FUNCTION: Cysteine proteinases 1 and 2 are believed to participate in
CC the breakdown of protein during differentiation of Dictyostelium as a
CC response to starvation.
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- DEVELOPMENTAL STAGE: Expressed by prestalk cells.
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; M16039; AAA33240.1; -; Genomic_DNA.
DR EMBL; X03344; CAA27050.1; -; mRNA.
DR EMBL; AAFI02000033; EAL67513.1; -; Genomic_DNA.
DR PIR; A25439; KHDOP.
DR RefSeq; XP_641494.1; XM_636402.1.
DR AlphaFoldDB; P04989; -.
DR SMR; P04989; -.
DR STRING; 44689.DDB0214998; -.
DR MEROPS; C01.A63; -.
DR MEROPS; I29.003; -.
DR PaxDb; P04989; -.
DR EnsemblProtists; EAL67513; EAL67513; DDB_G0279799.
DR GeneID; 8622234; -.
DR KEGG; ddi:DDB_G0279799; -.
DR dictyBase; DDB_G0279799; cprB.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; P04989; -.
DR OMA; YSGAEEH; -.
DR PhylomeDB; P04989; -.
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:P04989; -.
DR Proteomes; UP000002195; Chromosome 3.
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 GO; GO:0051591; P:response to cAMP; IDA:dictyBase.
DR CDD; cd02248; Peptidase_C1A; 1.
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 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; 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; Hydrolase; Lysosome; Protease; Reference proteome; Signal;
KW Thiol protease; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..122
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026360"
FT CHAIN 123..376
FT /note="Cysteine proteinase 2"
FT /id="PRO_0000026361"
FT ACT_SITE 147
FT /evidence="ECO:0000250"
FT ACT_SITE 286
FT /evidence="ECO:0000250"
FT ACT_SITE 343
FT /evidence="ECO:0000250"
FT DISULFID 144..187
FT /evidence="ECO:0000250"
FT DISULFID 178..221
FT /evidence="ECO:0000250"
FT DISULFID 279..365
FT /evidence="ECO:0000250"
SQ SEQUENCE 376 AA; 41851 MW; 161B293643456422 CRC64;
MRLLVFLILL IFVNFSFANV RPNGRRFSES QYRTAFTEWT LKFNRQYSSS EFSNRYSIFK
SNMDYVDNWN SKGDSQTVLG LNNFADITNE EYRKTYLGTR VNAHSYNGYD GREVLNVEDL
QTNPKSIDWR TKNAVTPIKD QGQCGSCWSF STTGSTEGAH ALKTKKLVSL SEQNLVDCSG
PEENFGCDGG LMNNAFDYII KNKGIDTESS YPYTAETGST CLFNKSDIGA TIKGYVNITA
GSEISLENGA QHGPVSVAID ASHNSFQLYT SGIYYEPKCS PTELDHGVLV VGYGVQGKDD
EGPVLNRKQT IVIHKNEDNK VESSDDSSDS VRPKANNYWI VKNSWGTSWG IKGYILMSKD
RKNNCGIASV SSYPLA
