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Protein

Cathepsin D

Gene

Ctsd

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acid protease active in intracellular protein breakdown.

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 sitei97 – 971PROSITE-ProRule annotation
Active sitei290 – 2901PROSITE-ProRule annotation

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: GO_Central
  • endopeptidase activity Source: RGD
  • peptide binding Source: RGD

GO - Biological processi

  • autophagy Source: RGD
  • protein catabolic process Source: GO_Central
  • proteolysis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.23.5. 5301.

Protein family/group databases

MEROPSiA01.009.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:Ctsd
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621511. Ctsd.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: GO_Central
  • lysosome Source: RGD
  • melanosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 6444Activation peptideSequence analysisPRO_0000025958Add
BLAST
Chaini65 – 407343Cathepsin DPRO_0000025959Add
BLAST
Chaini65 – 164100Cathepsin D 12 kDa light chainPRO_0000025960Add
BLAST
Chaini65 – 11753Cathepsin D 9 kDa light chainPRO_0000025961Add
BLAST
Chaini118 – 407290Cathepsin D 34 kDa heavy chainPRO_0000025962Add
BLAST
Chaini165 – 407243Cathepsin D 30 kDa heavy chainPRO_0000025963Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi91 ↔ 160By similarity
Disulfide bondi110 ↔ 117By similarity
Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence analysis
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence analysis
Disulfide bondi281 ↔ 285By similarity
Disulfide bondi324 ↔ 361By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP24268.
PRIDEiP24268.

PTM databases

iPTMnetiP24268.
SwissPalmiP24268.
UniCarbKBiP24268.

Interactioni

Subunit structurei

Occurs as a mixture of both a single chain form and two types of two chain (light and heavy) forms.

Protein-protein interaction databases

IntActiP24268. 1 interaction.
MINTiMINT-1775033.
STRINGi10116.ENSRNOP00000027407.

Structurei

3D structure databases

ProteinModelPortaliP24268.
SMRiP24268. Positions 66-405.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini79 – 402324Peptidase 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.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP24268.
PhylomeDBiP24268.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR033144. Cathepsin_D.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PTHR13683:SF230. PTHR13683:SF230. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P24268-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTPGVLLLI LGLLDASSSA LIRIPLRKFT SIRRTMTEVG GSVEDLILKG
60 70 80 90 100
PITKYSMQSS PRTKEPVSEL LKNYLDAQYY GEIGIGTPPQ CFTVVFDTGS
110 120 130 140 150
SNLWVPSIHC KLLDIACWVH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY
160 170 180 190 200
LSQDTVSVPC KSDLGGIKVE KQIFGEATKQ PGVVFIAAKF DGILGMGYPF
210 220 230 240 250
ISVNKVLPVF DNLMKQKLVE KNIFSFYLNR DPTGQPGGEL MLGGTDSRYY
260 270 280 290 300
HGELSYLNVT RKAYWQVHMD QLEVGSELTL CKGGCEAIVD TGTSLLVGPV
310 320 330 340 350
DEVKELQKAI GAVPLIQGEY MIPCEKVSSL PIITFKLGGQ NYELHPEKYI
360 370 380 390 400
LKVSQAGKTI CLSGFMGMDI PPPSGPLWIL GDVFIGCYYT VFDREYNRVG

FAKAATL
Length:407
Mass (Da):44,681
Last modified:March 1, 1992 - v1
Checksum:iC423AD4104D95F84
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151D → A AA sequence (PubMed:1883350).Curated
Sequence conflicti163 – 1631D → T AA sequence (PubMed:3182800).Curated
Sequence conflicti205 – 2051K → N AA sequence (PubMed:1883350).Curated
Sequence conflicti262 – 2621K → N AA sequence (PubMed:1883350).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54467 mRNA. Translation: CAA38349.1.
PIRiS13111. KHRTD.
UniGeneiRn.11085.

Genome annotation databases

UCSCiRGD:621511. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54467 mRNA. Translation: CAA38349.1.
PIRiS13111. KHRTD.
UniGeneiRn.11085.

3D structure databases

ProteinModelPortaliP24268.
SMRiP24268. Positions 66-405.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP24268. 1 interaction.
MINTiMINT-1775033.
STRINGi10116.ENSRNOP00000027407.

Protein family/group databases

MEROPSiA01.009.

PTM databases

iPTMnetiP24268.
SwissPalmiP24268.
UniCarbKBiP24268.

Proteomic databases

PaxDbiP24268.
PRIDEiP24268.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:621511. rat.

Organism-specific databases

RGDi621511. Ctsd.

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP24268.
PhylomeDBiP24268.

Enzyme and pathway databases

BRENDAi3.4.23.5. 5301.

Miscellaneous databases

PROiP24268.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR033144. Cathepsin_D.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PTHR13683:SF230. PTHR13683:SF230. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequence and expression of rat cathepsin D."
    Birch N.P., Loh Y.P.
    Nucleic Acids Res. 18:6445-6445(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Pituitary.
  2. "Isolation and sequencing of a cDNA clone encoding rat liver lysosomal cathepsin D and the structure of three forms of mature enzymes."
    Fujita H., Tanaka Y., Noguchi Y., Kono A., Himeno M., Kato K.
    Biochem. Biophys. Res. Commun. 179:190-196(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 65-74; 118-127 AND 165-174.
    Tissue: Liver.
  3. "Structures at the proteolytic processing region of cathepsin D."
    Yonezawa S., Takahashi T., Wang X., Wong R.N.S., Hartsuck J.A., Tang J.
    J. Biol. Chem. 263:16504-16511(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 134-170.
  4. Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 35-62; 65-72; 172-189; 222-248; 283-304 AND 309-348, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.

Entry informationi

Entry nameiCATD_RAT
AccessioniPrimary (citable) accession number: P24268
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: July 6, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.