CYSP6_DICDI
ID CYSP6_DICDI Reviewed; 434 AA.
AC Q94503; Q54X52;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cysteine proteinase 6;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=cprF; Synonyms=CP6; ORFNames=DDB_G0279185;
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], 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 -!- 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; U72745; AAC47481.1; -; mRNA.
DR EMBL; AAFI02000030; EAL67741.1; -; Genomic_DNA.
DR RefSeq; XP_641725.1; XM_636633.1.
DR AlphaFoldDB; Q94503; -.
DR SMR; Q94503; -.
DR STRING; 44689.DDB0215002; -.
DR MEROPS; C01.081; -.
DR PaxDb; Q94503; -.
DR EnsemblProtists; EAL67741; EAL67741; DDB_G0279185.
DR GeneID; 8621921; -.
DR KEGG; ddi:DDB_G0279185; -.
DR dictyBase; DDB_G0279185; cprF.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; Q94503; -.
DR OMA; MHNEEAD; -.
DR PhylomeDB; Q94503; -.
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:Q94503; -.
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; 2.
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..19
FT /evidence="ECO:0000255"
FT PROPEP 20..113
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000312514"
FT CHAIN 114..434
FT /note="Cysteine proteinase 6"
FT /id="PRO_0000312515"
FT REGION 285..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /evidence="ECO:0000250"
FT ACT_SITE 276
FT /evidence="ECO:0000250"
FT ACT_SITE 394
FT /evidence="ECO:0000250"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 133..178
FT /evidence="ECO:0000250"
FT DISULFID 169..211
FT /evidence="ECO:0000250"
FT DISULFID 269..416
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 45765 MW; 4F2297D8BDF7AFBD CRC64;
MKVLSALCVL LVSVATAKQQ LSELQYRNAF TNWMIAHQRH YSSEEFNGRF NIFKANMDYI
NEWNTKGSET VLGLNVFADI TNEEYRATYL GTPFDASSLE MTPSEKVFGG VQANSVDWRA
KGAVTPIKNQ GECGGCWSFS ATGATEGAQY IANGDSDLTS VSEQQLIDCS GSYGNNGCEG
GLMTLAFEYI INNGGIDTES SYPFTANTEK CKYNPSNIGA ELSSYVNVTS GSESDLAAKV
TQGPTSVAID ASQPSFQFYS SGIYNEPACS STQLDHGVLA VGFGSGSSGS QSQSAGSQSQ
SSNNNWSESS QSQDSNSWSQ SSQSQSSQDS NSWSQSSQSQ GSNSFTGAGT GSGSGSVSGS
GSASGSSSFS GSSNGGNSNS GDYPTDGNYW IVKNSWGLDW GINGYILMSK DKDNQCGIAT
MASIPQAIPK SKWN
