CTSB_DICDI
ID CTSB_DICDI Reviewed; 311 AA.
AC Q54QD9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cathepsin B;
DE EC=3.4.22.1;
DE AltName: Full=Cathepsin B1;
DE Flags: Precursor;
GN Name=ctsB; ORFNames=DDB_G0283921;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 -!- FUNCTION: Thiol protease which is believed to participate in
CC intracellular degradation and turnover of proteins. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule
CC substrates (thus differing from cathepsin L). In addition to being an
CC endopeptidase, shows peptidyl-dipeptidase activity, liberating C-
CC terminal dipeptides.; EC=3.4.22.1;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR EMBL; AAFI02000058; EAL65448.1; -; Genomic_DNA.
DR RefSeq; XP_638805.1; XM_633713.1.
DR AlphaFoldDB; Q54QD9; -.
DR SMR; Q54QD9; -.
DR STRING; 44689.DDB0233997; -.
DR MEROPS; C01.A59; -.
DR PaxDb; Q54QD9; -.
DR EnsemblProtists; EAL65448; EAL65448; DDB_G0283921.
DR GeneID; 8624329; -.
DR KEGG; ddi:DDB_G0283921; -.
DR dictyBase; DDB_G0283921; ctsB.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_3_3_1; -.
DR InParanoid; Q54QD9; -.
DR OMA; YFRIIRM; -.
DR PhylomeDB; Q54QD9; -.
DR Reactome; R-DDI-114608; Platelet degranulation.
DR PRO; PR:Q54QD9; -.
DR Proteomes; UP000002195; Chromosome 4.
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:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR Pfam; PF00112; Peptidase_C1; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..78
FT /evidence="ECO:0000250"
FT /id="PRO_0000330869"
FT CHAIN 79..311
FT /note="Cathepsin B"
FT /id="PRO_0000330870"
FT ACT_SITE 107
FT /evidence="ECO:0000250"
FT ACT_SITE 261
FT /evidence="ECO:0000250"
FT ACT_SITE 281
FT /evidence="ECO:0000250"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..121
FT /evidence="ECO:0000250"
FT DISULFID 104..145
FT /evidence="ECO:0000250"
FT DISULFID 138..191
FT /evidence="ECO:0000250"
FT DISULFID 167..195
FT /evidence="ECO:0000250"
FT DISULFID 175..182
FT /evidence="ECO:0000250"
SQ SEQUENCE 311 AA; 34437 MW; A5B3D459B5D60E24 CRC64;
MRVLLSLVVI LFIINSAFAV KINIGRPTKS HKTIHHETWV EEQTDQFDNI KVGQLLGFKR
SPNRPKLQIK SYDPLGVQIP TSFNAQTNWP NCTTISQIQN QARCGSCWAF GATESATDRL
CIHNNENVQL SFMDMVTCDE TDNGCEGGDA FSAWNWLRKQ GAVSEECLPY TIPTCPPAQQ
PCLNFVNTPS CTKECQSNSS LIYSQDKHKM AKIYSFDSDE AIMQEIVTNG PVEACFTVFE
DFLAYKSGVY VHTTGKDLGG HCVKLVGFGT LNGVDYYAAN NQWTTSWGDN GTFLIKRGDC
GISDDVVAGL P
