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Reviewed, UniProtKB/Swiss-Prot P80209 (CATD_BOVIN)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cathepsin D
    EC=3.4.23.5
Gene names
Name: CTSD
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Acid protease active in intracellular protein breakdown.

Catalytic activity

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

Subunit structure

Consists of a light chain and a heavy chain.

Subcellular location

Lysosome. Melanosome By similarity.

Sequence similarities

Belongs to the peptidase A1 family.

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Ontologies

Keywords
   Cellular componentLysosome
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 4444Activation peptide Ref.2
PRO_0000025947
Chain45 – 390346Cathepsin D
PRO_0000025948

Sites

Active site771
Active site2731

Amino acid modifications

Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Disulfide bond71 ↔ 140
Disulfide bond90 ↔ 97
Disulfide bond264 ↔ 268
Disulfide bond307 ↔ 344

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Sequences

Sequence LengthMass (Da)Tools
P80209-1 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: 5B38AA1C33C48D35

FASTA39042,491
        10         20         30         40         50         60 
VIRIPLHKFT SIRRTMSEAA GXVXXLIAKG PISKYATGEP AVRQGPIPEL LKNYMDAQYY 

        70         80         90        100        110        120 
GEIGIGTPPQ CFTVVFDTGS ANLWVPSIHC KLLDIACWTH RKYNSDKSST YVKNGTTFDI 

       130        140        150        160        170        180 
HYGSGSLSGY LSQDTVSVPC NPSSSSPGGV TVQRQTFGEA IKQPGVVFIA AKFDGILGMA 

       190        200        210        220        230        240 
YPRISVNNVL PVFDNLMQQK LVDKNVFSFF LNRDPKAQPG GELMLGGTDS KYYRGSLMFH 

       250        260        270        280        290        300 
NVTRQAYWQI HMDQLDVGSS LTVCKGGCEA IVDTGTSLIV GPVEEVRELQ KAIGAVPLIQ 

       310        320        330        340        350        360 
GEYMIPCEKV SSLPEVTVKL GGKDYALSPE DYALKVSQAE TTVCLSGFMG MDIPPPGGPL 

       370        380        390 
WILGDVFIGR YYTVFDRDQN RVGLAEAARL

« Hide

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References

[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: 8454061] [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: 8467789] [Abstract]
Cited for: PROTEIN SEQUENCE OF 45-390, X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
Tissue: Liver.

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Cross-references

Sequence databases

IPIIPI00715947.
PIRS32383.
UniGeneBt.20121

3D structure databases

HSSPHSSP built from PDB template 1LYB based on UniProtKB P07339.
SMRP80209. Positions 148-388.
ModBaseSearch...

Protein family/group databases

MEROPSA01.009.

Genome annotation databases

EnsemblENSBTAG00000007622. Bos taurus. [Contig view]

Phylogenomic databases

HOVERGENP80209.

Enzyme and pathway databases

BRENDA3.4.23.5. 251.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
IPR012848. Propep_A1.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCATD_BOVIN
AccessionPrimary (citable) accession number: P80209
Secondary accession number(s): Q9TS27
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: April 27, 2001
Last modified: June 16, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents