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Protein

Cathepsin D

Gene

ctsD

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protease that may act during cell growth and/or development.

Catalytic activityi

Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei81 – 811PROSITE-ProRule annotation
Active sitei268 – 2681PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • programmed cell death Source: dictyBase
  • protein catabolic process Source: GO_Central
  • proteolysis Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

ReactomeiR-DDI-2132295. MHC class II antigen presentation.
R-DDI-5683826. Surfactant metabolism.

Protein family/group databases

MEROPSiA01.A89.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin D (EC:3.4.23.5)
Alternative name(s):
Ddp44
Gene namesi
Name:ctsD
Synonyms:CatD
ORF Names:DDB_G0279411
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 3, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0279411. ctsD.

Subcellular locationi

  • Lysosome 1 Publication
  • Secreted 1 Publication

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • lysosome Source: dictyBase
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 48301 PublicationPRO_0000327788Add
BLAST
Chaini49 – 383335Cathepsin DPRO_5000147291Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi94 ↔ 101By similarity
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence analysis
Glycosylationi238 – 2381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi259 ↔ 263By similarity
Disulfide bondi302 ↔ 339By similarity
Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated on 2 out of the 3 potential sites. Glycans contain sulfated Mannose.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiO76856.
PRIDEiO76856.

Expressioni

Developmental stagei

Expressed in both vegetative and differentiating cells, with a higher level in vegetative cells.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi44689.DDB0215012.

Structurei

3D structure databases

ProteinModelPortaliO76856.
SMRiO76856. Positions 50-290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 378316Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
InParanoidiO76856.
KOiK01379.
OMAiASIQVER.
PhylomeDBiO76856.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 1 hit.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O76856-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLILTLFL ATIVLAQALT VPLNFHQASR ESRRRVPQKW SNRLSALNAG
60 70 80 90 100
TTIPISDFED AQYYGAITIG TPGQAFKVVF DTGSSNLWIP SKKCPITVVA
110 120 130 140 150
CDLHNKYNSG ASSTYVANGT DFTIQYGSGA MSGFVSQDSV TVGSLTVKDQ
160 170 180 190 200
LFAEATAEPG IAFDFAKFDG ILGLAFQSIS VNSIPPVFYN MLSQGLVSST
210 220 230 240 250
LFSFWLSRTP GANGGELSFG SIDNTKYTGD ITYVPLTNET YWEFVMDDFA
260 270 280 290 300
IDGQSAGFCG TTCHAICDSG TSLIAGPMAD ITALNEKLGA VILNGEGVFS
310 320 330 340 350
DCSVINTLPN VTITVAGREF VLTPKEYVLE VTEFGKTECL SGFMGIELNM
360 370 380
GNFWILGDVF ISAYYTVFDF GNKQVGFATA IQG
Length:383
Mass (Da):41,121
Last modified:November 1, 1998 - v1
Checksum:iCC8DE423AEA1A280
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16962 mRNA. Translation: CAA76563.1.
AJ243946 Genomic DNA. Translation: CAB57223.1.
AAFI02000031 Genomic DNA. Translation: EAL67644.1.
RefSeqiXP_641645.1. XM_636553.1.

Genome annotation databases

EnsemblProtistsiDDB0215012; DDB0215012; DDB_G0279411.
GeneIDi8622052.
KEGGiddi:DDB_G0279411.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16962 mRNA. Translation: CAA76563.1.
AJ243946 Genomic DNA. Translation: CAB57223.1.
AAFI02000031 Genomic DNA. Translation: EAL67644.1.
RefSeqiXP_641645.1. XM_636553.1.

3D structure databases

ProteinModelPortaliO76856.
SMRiO76856. Positions 50-290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0215012.

Protein family/group databases

MEROPSiA01.A89.

Proteomic databases

PaxDbiO76856.
PRIDEiO76856.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0215012; DDB0215012; DDB_G0279411.
GeneIDi8622052.
KEGGiddi:DDB_G0279411.

Organism-specific databases

dictyBaseiDDB_G0279411. ctsD.

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
InParanoidiO76856.
KOiK01379.
OMAiASIQVER.
PhylomeDBiO76856.

Enzyme and pathway databases

ReactomeiR-DDI-2132295. MHC class II antigen presentation.
R-DDI-5683826. Surfactant metabolism.

Miscellaneous databases

PROiO76856.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 1 hit.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of Dictyostelium discoideum cathepsin D. Molecular cloning, gene disruption, endo-lysosomal localization and sugar modifications."
    Journet A., Chapel A., Jehan S., Adessi C., Freeze H., Klein G., Garin J.
    J. Cell Sci. 112:3833-3843(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 49-56; 77-92; 103-116; 269-278; 325-336 AND 370-383, SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, GLYCOSYLATION.
    Strain: AX2.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.

Entry informationi

Entry nameiCATD_DICDI
AccessioniPrimary (citable) accession number: O76856
Secondary accession number(s): Q54WS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.