Reviewed, UniProtKB/Swiss-Prot Q54QD9 (CTSB_DICDI)

Names and origin

Protein names

Recommended name:
    Cathepsin B
    EC=3.4.22.1
Alternative name(s):
    Cathepsin B1

Gene names

Name:	ctsB
ORF Names:	DDB_G0283921

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	311 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Thiol protease which is believed to participate in intracellular degradation and turnover of proteins By similarity.
Catalytic activity	Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.
Subcellular location	Lysosome By similarity.
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Propeptide	20 – 78	59	By similarity		PRO_0000330869
	Chain	79 – 311	233	Cathepsin B		PRO_0000330870
Sites
	Active site	107	1	By similarity
	Active site	261	1	By similarity
	Active site	281	1	By similarity
Amino acid modifications
	Glycosylation	91	1	N-linked (GlcNAc...) Potential
	Glycosylation	198	1	N-linked (GlcNAc...) Potential
	Glycosylation	290	1	N-linked (GlcNAc...) Potential
	Disulfide bond	92 ↔ 121		By similarity
	Disulfide bond	104 ↔ 145		By similarity
	Disulfide bond	138 ↔ 191		By similarity
	Disulfide bond	167 ↔ 195		By similarity
	Disulfide bond	175 ↔ 182		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54QD9-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: A5B3D459B5D60E24	FASTA	311	34,437
	10 20 30 40 50 60 MRVLLSLVVI LFIINSAFAV KINIGRPTKS HKTIHHETWV EEQTDQFDNI KVGQLLGFKR 70 80 90 100 110 120 SPNRPKLQIK SYDPLGVQIP TSFNAQTNWP NCTTISQIQN QARCGSCWAF GATESATDRL 130 140 150 160 170 180 CIHNNENVQL SFMDMVTCDE TDNGCEGGDA FSAWNWLRKQ GAVSEECLPY TIPTCPPAQQ 190 200 210 220 230 240 PCLNFVNTPS CTKECQSNSS LIYSQDKHKM AKIYSFDSDE AIMQEIVTNG PVEACFTVFE 250 260 270 280 290 300 DFLAYKSGVY VHTTGKDLGG HCVKLVGFGT LNGVDYYAAN NQWTTSWGDN GTFLIKRGDC 310 GISDDVVAGL P

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000058 Genomic DNA. Translation: EAL65448.1.
RefSeq	XP_638805.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q54QD9.
Genome annotation databases
GeneID	3390374.
GenomeReviews	Gene locus ctsB in contig CM000153_GR.
KEGG	ddi:DDB_0233997.
Organism-specific databases
dictyBase	DDB_G0283921. ctsB.
Phylogenomic databases
OMA	CGIESEM.
Family and domain databases
InterPro	IPR000169. Pept_cys_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR015643. Peptidase_C1A_cathepsin-B. [Graphical view]
PANTHER	PTHR12411:SF16. CathepsinB_like. 1 hit. PTHR12411. Peptidase_C1A. 1 hit.
Pfam	PF00112. Peptidase_C1. 1 hit. [Graphical view]
ProDom	PD000158. Peptidase_C1. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00645. Pept_C1. 1 hit. [Graphical view]
PROSITE	PS00640. THIOL_PROTEASE_ASN. False negative. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CTSB_DICDI

Accession

Primary (citable) accession number: Q54QD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	May 24, 2005
Last modified:	November 3, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)