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Protein

Cathepsin D

Gene

CTSD

Organism
Bos taurus (Bovine)
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 sitei77 – 771
Active sitei273 – 2731

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.009.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin D (EC:3.4.23.5)
Gene namesi
Name:CTSD
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4106.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 4444Activation peptide1 PublicationPRO_0000025947Add
BLAST
Chaini45 – 390346Cathepsin DPRO_0000025948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi71 ↔ 140
Disulfide bondi90 ↔ 97
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence analysis
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence analysis
Disulfide bondi264 ↔ 268
Disulfide bondi307 ↔ 344

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP80209.
PeptideAtlasiP80209.
PRIDEiP80209.

Interactioni

Subunit structurei

Consists of a light chain and a heavy chain.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000010022.

Chemistry

BindingDBiP80209.

Structurei

3D structure databases

ProteinModelPortaliP80209.
SMRiP80209. Positions 45-388.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 385327Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP80209.

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.

P80209-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VIRIPLHKFT SIRRTMSEAA GXVXXLIAKG PISKYATGEP AVRQGPIPEL
60 70 80 90 100
LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS ANLWVPSIHC KLLDIACWTH
110 120 130 140 150
RKYNSDKSST YVKNGTTFDI HYGSGSLSGY LSQDTVSVPC NPSSSSPGGV
160 170 180 190 200
TVQRQTFGEA IKQPGVVFIA AKFDGILGMA YPRISVNNVL PVFDNLMQQK
210 220 230 240 250
LVDKNVFSFF LNRDPKAQPG GELMLGGTDS KYYRGSLMFH NVTRQAYWQI
260 270 280 290 300
HMDQLDVGSS LTVCKGGCEA IVDTGTSLIV GPVEEVRELQ KAIGAVPLIQ
310 320 330 340 350
GEYMIPCEKV SSLPEVTVKL GGKDYALSPE DYALKVSQAE TTVCLSGFMG
360 370 380 390
MDIPPPGGPL WILGDVFIGR YYTVFDRDQN RVGLAEAARL
Length:390
Mass (Da):42,491
Last modified:April 27, 2001 - v2
Checksum:i5B38AA1C33C48D35
GO

Sequence databases

PIRiS32383.
UniGeneiBt.20121.

Cross-referencesi

Sequence databases

PIRiS32383.
UniGeneiBt.20121.

3D structure databases

ProteinModelPortaliP80209.
SMRiP80209. Positions 45-388.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000010022.

Chemistry

BindingDBiP80209.
ChEMBLiCHEMBL4106.

Protein family/group databases

MEROPSiA01.009.

Proteomic databases

PaxDbiP80209.
PeptideAtlasiP80209.
PRIDEiP80209.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP80209.

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. "Procathepsin D cannot autoactivate to cathepsin D at acid pH."
    Larsen L.B., Boisen A., Petersen T.E.
    FEBS Lett. 319:54-58(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-48.
    Tissue: Milk.
  2. "Two crystal structures for cathepsin D: the lysosomal targeting signal and active site."
    Metcalf P., Fusek M.
    EMBO J. 12:1293-1302(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 45-390, X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
    Tissue: Liver.

Entry informationi

Entry nameiCATD_BOVIN
AccessioniPrimary (citable) accession number: P80209
Secondary accession number(s): Q9TS27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: April 27, 2001
Last modified: July 6, 2016
This is version 108 of the entry and version 2 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.