KEGG   ENZYME: 3.4.23.5Help
Entry
EC 3.4.23.5                 Enzyme                                 

Name
cathepsin D
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Aspartic endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Specificity similar to, but narrower than, that of pepsin A. Does not cleave the Gln4-His bond in B chain of insulin
Comment
Occurs intracellularly, in lysosomes. A zymogen form is known [4]. In peptidase family A1 (pepsin A family).
History
EC 3.4.23.5 created 1965 as EC 3.4.4.23, transferred 1972 to EC 3.4.23.5, modified 1986
Orthology
K01379  cathepsin D
Genes
HSA: 1509(CTSD)
PTR: 746637(CTSD)
PPS: 100974319(CTSD)
GGO: 101125251(CTSD)
PON: 100172401(CTSD)
NLE: 100582697(CTSD)
MCC: 703534(CTSD)
MCF: 102125635(CTSD)
CSAB: 103236841(CTSD)
RRO: 104677092(CTSD)
RBB: 108531312(CTSD)
CJC: 100397061(CTSD)
SBQ: 101033575(CTSD)
MMU: 13033(Ctsd)
RNO: 171293(Ctsd)
CGE: 100766628(Ctsd)
NGI: 103738995(Ctsd)
HGL: 101716979(Ctsd)
CCAN: 109689769(Ctsd)
OCU: 100101595(CTSD)
TUP: 102474582(CTSD)
CFA: 483662(CTSD)
AML: 100464994(CTSD)
UMR: 103671118(CTSD)
ORO: 101381080(CTSD)
FCA: 101094625(CTSD)
PTG: 102954120(CTSD)
AJU: 106971074(CTSD)
BTA: 282883(CTSD)
BOM: 102275829(CTSD)
BIU: 109554428(CTSD)
PHD: 102343491(CTSD)
CHX: 106504021(CTSD)
SSC: 494568(CTSD)
CFR: 102523939(CTSD)
CDK: 105105228 105106414(CTSD)
BACU: 103017977(CTSD)
LVE: 103083086(CTSD)
OOR: 101280086(CTSD)
ECB: 100629639(CTSD)
EPZ: 103542275(CTSD)
EAI: 106824102(CTSD)
MYB: 102255890(CTSD)
MYD: 102752567(CTSD)
HAI: 109395931(CTSD)
RSS: 109438596(CTSD)
PALE: 102888325(CTSD)
LAV: 100663561(CTSD)
TMU: 101346448
SHR: 100917285(CTSD)
OAA: 100090301
GGA: 396090(CTSD)
MGP: 100543618(CTSD)
CJO: 107314535(CTSD)
APLA: 101792449(CTSD)
ACYG: 106042625(CTSD)
TGU: 100232592(CTSD)
GFR: 102032764(CTSD)
FAB: 101814740(CTSD)
PHI: 102106589 102113116(CTSD)
PMAJ: 107206041(CTSD)
CCW: 104688249(CTSD)
FPG: 101917516(CTSD)
FCH: 102054100(CTSD)
CLV: 102090198(CTSD)
EGZ: 104124913(CTSD)
AAM: 106496991(CTSD)
ASN: 102387475(NAPSA) 102387859(CTSD)
AMJ: 102558679(CTSD) 102576563
PSS: 102448444(CTSD)
CMY: 102948221(CTSD)
CPIC: 101953135 101953957(CTSD)
ACS: 100563621 100567238(ctsd)
PVT: 110076569(CTSD) 110078570
XLA: 398557 398994(napsa.L) 443721(ctsd.S) 443829
DRE: 336746(zgc:63831) 65225(ctsd)
IPU: 100528208(catd) 100862736(ctsd)
TRU: 777955(ctsd) 777956(ctsd2)
NCC: 104966021(ctsd) 104967883
MZE: 101473375(ctsd) 101475375
XMA: 102221671(ctsd) 102225207
CSEM: 103378862(ctsd) 103393287
HCQ: 109514434(ctsd) 109520249
LCM: 102351433(CTSD) 102355307
CMK: 103174885(ctsd)
SPU: 575021
DSI: Dsimw501_GD10217(Dsim_GD10217) Dsimw501_GD11051(Dsim_GD11051) Dsimw501_GD19153(Dsim_GD19153) Dsimw501_GD19154(Dsim_GD19154) Dsimw501_GD19155(Dsim_GD19155) Dsimw501_GD23098(Dsim_GD23098) Dsimw501_GD23099(Dsim_GD23099) Dsimw501_GD23100(Dsim_GD23100) Dsimw501_GD23101(Dsim_GD23101) Dsimw501_GD23735(Dsim_GD23735) Dsimw501_GD23736(Dsim_GD23736) Dsimw501_GD27017(Dsim_GD27017)
AAG: 5567565
AME: 409341(cathD)
BIM: 100742346
BTER: 100646691
PBAR: 105434351
HST: 105184786
LHU: 105680170
PGC: 109852740
NVI: 100114169
NVL: 108559999
BMOR: 692768(CatD)
PMAC: 106716172
PRAP: 110999719
API: 100168373(Cathd) 100169529
FCD: 110852010
CEL: CELE_H22K11.1(asp-3) CELE_R12H7.2(asp-4)
CBR: CBG05258(Cbr-asp-4) CBG10895(Cbr-asp-3)
BMY: Bm1_12055
TSP: Tsp_06028
CRG: 105337691
MYI: 110466152
OBI: 106870172
EPA: 110238202
ADF: 107346156
HMG: 100203582
THJ: 104806799
GMX: 100812865
LJA: Lj4g3v3095020.1(Lj4g3v3095020.1)
LANG: 109361088
PPER: 18775368
PAVI: 110749445
CSV: 101207249
CMO: 103504612
CMAX: 111469001
HBR: 110642485
JRE: 108993255
VVI: 100256020
NTA: 107807180
SIND: 105170058
OEU: 111398970
BVG: 104885553
PDA: 103698137
ABP: AGABI1DRAFT112343(AGABI1DRAFT_112343) AGABI1DRAFT70451(AGABI1DRAFT_70451) AGABI1DRAFT91098(AGABI1DRAFT_91098)
ABV: AGABI2DRAFT142735(AGABI2DRAFT_142735) AGABI2DRAFT149875(AGABI2DRAFT_149875) AGABI2DRAFT186102(AGABI2DRAFT_186102) AGABI2DRAFT192307(AGABI2DRAFT_192307)
DDI: DDB_G0279411(ctsD)
DFA: DFA_06766(ctsD)
SMIN: v1.2.002327.t1(symbB.v1.2.002327.t1) v1.2.005246.t1(symbB.v1.2.005246.t1) v1.2.010189.t1(symbB.v1.2.010189.t1) v1.2.033392.t1(symbB.v1.2.033392.t1) v1.2.033392.t2(symbB.v1.2.033392.t2)
 » show all
Taxonomy
Reference
1
  Authors
Barrett, A.J.
  Title
Cathepsin D and other carboxyl proteinases.
  Journal
In: Barrett, A.J. (Ed.), Proteinases in Mammalian Cells and Tissues, North-Holland Publishing Co., Amsterdam, 1977, p. 209-248.
Reference
2  [PMID:7341918]
  Authors
Takahashi T, Tang J.
  Title
Cathepsin D from porcine and bovine spleen.
  Journal
Methods. Enzymol. 80 Pt C (1981) 565-81.
Reference
3  [PMID:3927292]
  Authors
Faust PL, Kornfeld S, Chirgwin JM.
  Title
Cloning and sequence analysis of cDNA for human cathepsin D.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 4910-4.
  Sequence
[hsa:1509]
Reference
4  [PMID:2512908]
  Authors
Conner GE.
  Title
Isolation of procathepsin D from mature cathepsin D by pepstatin affinity chromatography. Autocatalytic proteolysis of the zymogen form of the enzyme.
  Journal
Biochem. J. 263 (1989) 601-4.
Other DBs
ExplorEnz - The Enzyme Database: 3.4.23.5
IUBMB Enzyme Nomenclature: 3.4.23.5
ExPASy - ENZYME nomenclature database: 3.4.23.5
BRENDA, the Enzyme Database: 3.4.23.5
CAS: 9025-26-7

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