CYSP4_DICDI
ID CYSP4_DICDI Reviewed; 442 AA.
AC P54639; Q54XR7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cysteine proteinase 4;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=cprD; Synonyms=CP4; ORFNames=DDB_G0278721;
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].
RC STRAIN=AX4;
RX PubMed=7499424; DOI=10.1074/jbc.270.48.28938;
RA Souza G.M., Hirai J., Mehta D.P., Freeze H.H.;
RT "Identification of two novel Dictyostelium discoideum cysteine proteinases
RT that carry N-acetylglucosamine-1-P-modification.";
RL J. Biol. Chem. 270:28938-28945(1995).
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.
CC -!- DEVELOPMENTAL STAGE: Present in the vegetative phase and decreases with
CC the start development, reappears in low levels when the fruiting body
CC is formed.
CC -!- PTM: Glycosylated; contains GlcNAc-alpha-1-P-Ser residues and fucose.
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; L36204; AAA92019.1; -; mRNA.
DR EMBL; AAFI02000024; EAL67962.1; -; Genomic_DNA.
DR RefSeq; XP_641963.1; XM_636871.1.
DR AlphaFoldDB; P54639; -.
DR SMR; P54639; -.
DR STRING; 44689.DDB0214999; -.
DR MEROPS; C01.A57; -.
DR PaxDb; P54639; -.
DR EnsemblProtists; EAL67962; EAL67962; DDB_G0278721.
DR GeneID; 8621695; -.
DR KEGG; ddi:DDB_G0278721; -.
DR dictyBase; DDB_G0278721; cprD.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; P54639; -.
DR OMA; RYGREYN; -.
DR PhylomeDB; P54639; -.
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:P54639; -.
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 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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Repeat; 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_0000026362"
FT CHAIN 112..442
FT /note="Cysteine proteinase 4"
FT /id="PRO_0000026363"
FT REGION 286..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /evidence="ECO:0000250"
FT ACT_SITE 277
FT /evidence="ECO:0000250"
FT ACT_SITE 406
FT /evidence="ECO:0000250"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 132..178
FT /evidence="ECO:0000250"
FT DISULFID 169..212
FT /evidence="ECO:0000250"
FT DISULFID 270..428
FT /evidence="ECO:0000250"
FT CONFLICT 186
FT /note="A -> G (in Ref. 1; AAA92019)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="S -> T (in Ref. 1; AAA92019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 45690 MW; A261D815087CFCBF CRC64;
MRVLSFLCLL LVSYASAKQQ FSELQYRNAF TNWMQAHQRT YSSEEFNARY QIFKSNMDYV
HQWNSKGGET VLGLNVFADI TNQEYRTTYL GTPFDGSALI GTEEEKIFST PAPTVDWRAQ
GAVTPIKNQG QCGGCWSFST TGSTEGAHFI ASGTKKDLVS LSEQNLIDCS KSYGNNGCEG
GLMTLAFEYI INNKGIDTES SYPYTAEDGK ECKFKTSNIG AQIVSYQNVT SGSEASLQSA
SNNAPVSVAI DASNESFQLY ESGIYYEPAC SPTQLDHGVL VVGYGSGSSS SSGSSSGKSS
SSSSTGGKTS SSSSSGKASS SSSGKASSSS SSGKTSSAAS STSGSQSGSQ SGSQSGQSTG
SQSGQTSASG QASASGSGSG SGSGSGSGSG SGAVEASSGN YWIVKNSWGT SWGMDGYIFM
SKDRNNNCGI ATMASFPTAS SN
