CYSP1_DICDI
ID CYSP1_DICDI Reviewed; 343 AA.
AC P04988; Q54FC0;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Cysteine proteinase 1;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=cprA; Synonyms=CP1; ORFNames=DDB_G0290957;
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].
RX PubMed=2990918; DOI=10.1002/j.1460-2075.1985.tb03730.x;
RA Williams J.G., North M.J., Mahbubani H.M.;
RT "A developmentally regulated cysteine proteinase in Dictyostelium
RT discoideum.";
RL EMBO J. 4:999-1006(1985).
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).
RN [3]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=8631906; DOI=10.1074/jbc.271.18.10897;
RA Mehta D.P., Ichikawa M., Salimath P.V., Etchison J.R., Haak R., Manzi A.,
RA Freeze H.H.;
RT "A lysosomal cysteine proteinase from Dictyostelium discoideum contains N-
RT acetylglucosamine-1-phosphate bound to serine but not mannose-6-phosphate
RT on N-linked oligosaccharides.";
RL J. Biol. Chem. 271:10897-10903(1996).
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 -!- PTM: Phosphoglycosylated, contains GlcNAc-alpha-1-P-Ser residues.
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; X02407; CAA26255.1; -; mRNA.
DR EMBL; AAFI02000174; EAL61909.1; -; Genomic_DNA.
DR PIR; A22827; KHDO.
DR RefSeq; XP_635417.1; XM_630325.1.
DR AlphaFoldDB; P04988; -.
DR SMR; P04988; -.
DR STRING; 44689.DDB0201647; -.
DR MEROPS; C01.022; -.
DR GlyConnect; 118; 1 O-Linked glycan.
DR SWISS-2DPAGE; P04988; -.
DR PaxDb; P04988; -.
DR EnsemblProtists; EAL61909; EAL61909; DDB_G0290957.
DR GeneID; 8627918; -.
DR KEGG; ddi:DDB_G0290957; -.
DR dictyBase; DDB_G0290957; cprA.
DR eggNOG; KOG1542; Eukaryota.
DR HOGENOM; CLU_012184_1_3_1; -.
DR InParanoid; P04988; -.
DR OMA; FEGKCHF; -.
DR PhylomeDB; P04988; -.
DR Reactome; R-DDI-114608; Platelet degranulation.
DR PRO; PR:P04988; -.
DR Proteomes; UP000002195; Chromosome 5.
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:0006972; P:hyperosmotic response; IEP:dictyBase.
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; 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; Glycoprotein; Hydrolase; Lysosome; Phosphoprotein;
KW Protease; Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..117
FT /note="Activation peptide"
FT /id="PRO_0000026358"
FT CHAIN 118..343
FT /note="Cysteine proteinase 1"
FT /id="PRO_0000026359"
FT ACT_SITE 142
FT /evidence="ECO:0000250"
FT ACT_SITE 286
FT /evidence="ECO:0000250"
FT ACT_SITE 311
FT /evidence="ECO:0000250"
FT DISULFID 139..190
FT /evidence="ECO:0000250"
FT DISULFID 173..224
FT /evidence="ECO:0000250"
FT DISULFID 279..332
FT /evidence="ECO:0000250"
FT CONFLICT 23
FT /note="L -> P (in Ref. 1; CAA26255)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="Q -> E (in Ref. 1; CAA26255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 38510 MW; 8F70D4907C891021 CRC64;
MKVILLFVLA VFTVFVSSRG IPLEEQSQFL EFQDKFNKKY SHEEYLERFE IFKSNLGKIE
ELNLIAINHK ADTKFGVNKF ADLSSDEFKN YYLNNKEAIF TDDLPVADYL DDEFINSIPT
AFDWRTRGAV TPVKNQGQCG SCWSFSTTGN VEGQHFISQN KLVSLSEQNL VDCDHECMEY
EGEQACDEGC NGGLQPNAYN YIIKNGGIQT ESSYPYTAET GTQCNFNSAN IGAKISNFTM
IPKNETVMAG YIVSTGPLAI AADAVEWQFY IGGVFDIPCN PNSLDHGILI VGYSAKNTIF
RKNMPYWIVK NSWGADWGEQ GYIYLRRGKN TCGVSNFVST SII
