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CYSP5_DICDI
ID   CYSP5_DICDI             Reviewed;         344 AA.
AC   P54640; Q558T9; Q8MNB1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Cysteine proteinase 5;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=cprE; Synonyms=CP5; ORFNames=DDB_G0272815;
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=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [3]
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.
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; L36205; AAA92018.1; -; mRNA.
DR   EMBL; AAFI02000008; EAL71045.1; -; Genomic_DNA.
DR   RefSeq; XP_644977.1; XM_639885.1.
DR   AlphaFoldDB; P54640; -.
DR   SMR; P54640; -.
DR   BioGRID; 1243657; 1.
DR   STRING; 44689.DDB0185092; -.
DR   MEROPS; C01.A57; -.
DR   MEROPS; I29.003; -.
DR   PaxDb; P54640; -.
DR   EnsemblProtists; EAL71045; EAL71045; DDB_G0272815.
DR   GeneID; 8618654; -.
DR   KEGG; ddi:DDB_G0272815; -.
DR   dictyBase; DDB_G0272815; cprE.
DR   eggNOG; KOG1543; Eukaryota.
DR   HOGENOM; CLU_012184_1_2_1; -.
DR   InParanoid; P54640; -.
DR   OMA; PVGNEKA; -.
DR   PhylomeDB; P54640; -.
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:P54640; -.
DR   Proteomes; UP000002195; Chromosome 2.
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; 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..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..111
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026364"
FT   CHAIN           112..344
FT                   /note="Cysteine proteinase 5"
FT                   /id="PRO_0000026365"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        311
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        133..174
FT                   /evidence="ECO:0000250"
FT   DISULFID        167..207
FT                   /evidence="ECO:0000250"
FT   DISULFID        265..333
FT                   /evidence="ECO:0000250"
FT   CONFLICT        54
FT                   /note="K -> T (in Ref. 1; AAA92018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108..110
FT                   /note="FTT -> HTN (in Ref. 1; AAA92018)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   344 AA;  37237 MW;  1E77FBA4BD8337B7 CRC64;
     MKVLSFLCVL LVSVATAKQQ FSELQYRNAF TDWMITHQKS YTSEEFGARY NIFKANMDYV
     QQWNSKGSET VLGLNNFADI TNEEYRNTYL GTKFDASSLI GTQEEKVFTT SSAASKDWRS
     EGAVTPVKNQ GQCGGCWSFS TTGSTEGAHF QSKGELVSLS EQNLIDCSTE NSGCDGGLMT
     YAFEYIINNN GIDTESSYPY KAENGKCEYK SENSGATLSS YKTVTAGSES SLESAVNVNP
     VSVAIDASHQ SFQLYTSGIY YEPECSSENL DHGVLAVGYG SGSGSSSGQS SGQSSGNLSA
     SSSNEYWIVK NSWGTSWGIE GYILMSRNRD NNCGIASSAS FPVV
 
 
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