CYSP7_DICDI
ID CYSP7_DICDI Reviewed; 460 AA.
AC Q94504; Q54X57;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cysteine proteinase 7;
DE EC=3.4.22.-;
DE AltName: Full=Proteinase 1;
DE Flags: Precursor;
GN Name=cprG; Synonyms=CP7; ORFNames=DDB_G0279187;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=9056234; DOI=10.1006/abbi.1996.9870;
RA Ord T., Adessi C., Wang L., Freeze H.H.;
RT "The cysteine proteinase gene cprG in Dictyostelium discoideum has a
RT serine-rich domain that contains GlcNAc-1-P.";
RL Arch. Biochem. Biophys. 339:64-72(1997).
RN [2]
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 -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Present in the vegetative phase and decreases with
CC the start development. {ECO:0000269|PubMed:9056234}.
CC -!- PTM: Glycosylated; contains GlcNAc-alpha-1-P-Ser residues. Also N-
CC glycosylated. {ECO:0000269|PubMed:9056234}.
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; U72746; AAC47482.1; -; mRNA.
DR EMBL; AAFI02000030; EAL67742.2; -; Genomic_DNA.
DR RefSeq; XP_641720.2; XM_636628.2.
DR AlphaFoldDB; Q94504; -.
DR SMR; Q94504; -.
DR STRING; 44689.DDB0215005; -.
DR MEROPS; C01.081; -.
DR PaxDb; Q94504; -.
DR ABCD; Q94504; 1 sequenced antibody.
DR EnsemblProtists; EAL67742; EAL67742; DDB_G0279187.
DR GeneID; 8621915; -.
DR KEGG; ddi:DDB_G0279187; -.
DR dictyBase; DDB_G0279187; cprG.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; Q94504; -.
DR OMA; ARITMNN; -.
DR PhylomeDB; Q94504; -.
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:Q94504; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:dictyBase.
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; 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; 2.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Phosphoprotein;
KW Protease; Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..111
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026366"
FT CHAIN 112..460
FT /note="Cysteine proteinase 7"
FT /id="PRO_0000026367"
FT REGION 285..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /evidence="ECO:0000250"
FT ACT_SITE 423
FT /evidence="ECO:0000250"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 131..176
FT /evidence="ECO:0000250"
FT DISULFID 167..210
FT /evidence="ECO:0000250"
FT DISULFID 268..445
FT /evidence="ECO:0000250"
SQ SEQUENCE 460 AA; 47166 MW; 0D71CFA1BAC99B25 CRC64;
MKVLSALCVL LVSVATAKQQ LSEVEYRNAF TNWMIAHQRH YSSEEFNGRY NIFKANMDYV
NEWNTKGSET VLGLNVFADI SNEEYRATYL GTPFDASSLE MTESDKIFDA SAQVDWRTQG
AVTPIKNQGQ CGGCWSFSTT GATEGAQYLA NGKKNLVSLS EQNLIDCSGS YGNNGCEGGL
MTLAFEYIIN NKGIDTESSY PYTAEDGKKC KFNPKNVAAQ LSSYVNVTSG SESDLAAKVT
QGPTSVAIDA SNQSFQLYVS GIYNEPACSS TQLDHGVLAV GFGTGSGSSG SHGGSQSQSA
GSDSQSAGSE SSQSESGSQS QSESGSQSQS QSGSQSFSGS LYSGSYSGSQ SGSQSGNSGA
AVKQTGAGSG SGSGSGSGSG SGSGSVSGSA SGSASGSASG SSSGSNSNGG VYPTAGDYWI
VKNSWGTSWG MDGYILMTKG NNNQCGIATM ASRPTAVASL
