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Reviewed, UniProtKB/Swiss-Prot Q4LAL9 (CATD_CANFA)

Last modified February 9, 2010. Version 36. 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
OrganismCanis familiaris (Dog)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

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Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Subcellular location

Lysosome. Melanosome By similarity.

Sequence similarities

Belongs to the peptidase A1 family.

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Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
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

Signal peptide1 – 1818 By similarity
Propeptide19 – 6446Activation peptide By similarity
PRO_0000045434
Chain65 – 410346Cathepsin D
PRO_0000045435

Sites

Active site971 By similarity
Active site2931 By similarity

Amino acid modifications

Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation2611N-linked (GlcNAc...) Potential
Disulfide bond91 ↔ 160 By similarity
Disulfide bond110 ↔ 117 By similarity
Disulfide bond284 ↔ 288 By similarity
Disulfide bond327 ↔ 364 By similarity

Natural variations

Natural variant2541K → T

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Sequences

Sequence LengthMass (Da)Tools
Q4LAL9-1 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 1E97B7C15BAAF9CD

FASTA41044,320
        10         20         30         40         50         60 
MQPPSLLLLV LGLLAAPAAA LVRIPLHKFT SVRRTMTELG GPVEDLIAKG PISKYAQGAP 

        70         80         90        100        110        120 
AVTGGPIPEM LRNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH 

       130        140        150        160        170        180 
HKYNSGKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC KSALSGLAGI KVERQTFGEA 

       190        200        210        220        230        240 
TKQPGITFIA AKFDGILGMA YPRISVNNVL PVFDNLMQQK LVEKNIFSFY LNRDPNAQPG 

       250        260        270        280        290        300 
GELMLGGTDS KYYKGPLSYL NVTRKAYWQV HMEQVDVGSS LTLCKGGCEA IVDTGTSLIV 

       310        320        330        340        350        360 
GPVDEVRELQ KAIGAVPLIQ GEYMIPCEKV STLPDVTLKL GGKLYKLSSE DYTLKVSQGG 

       370        380        390        400        410 
KTICLSGFMG MDIPPPGGPL WILGDVFIGC YYTVFDRDQN RVGLAQATRL

« Hide

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References

[1]"The canine CTSD gene as a candidate for late-onset neuronal ceroid lipofuscinosis."
Woehlke A., Distl O., Droegemueller C.
Anim. Genet. 36:530-532(2005) [PubMed: 16293139] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-254.
Strain: Beagle.
Tissue: Lung.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM048627 mRNA. Translation: CAJ14973.1.
RefSeqNP_001020792.1.
UniGeneCfa.17547

3D structure databases

SMRQ4LAL9. Positions 65-161, 69-408.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4LAL9.

Protein family/group databases

MEROPSA01.009.

Genome annotation databases

EnsemblENSCAFT00000015991; ENSCAFP00000014791; ENSCAFG00000010052; Canis familiaris. [Genome view]
GeneID483662.
KEGGcfa:483662.

Organism-specific databases

CTD483662.

Phylogenomic databases

eggNOGmaNOG17543.
HOVERGENQ4LAL9.
InParanoidQ4LAL9.
OMASGFMGID.
OrthoDBEOG9HDWCP.
PhylomeDBQ4LAL9.

Enzyme and pathway databases

BRENDA3.4.23.5. 463.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
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_CANFA
AccessionPrimary (citable) accession number: Q4LAL9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: August 2, 2005
Last modified: February 9, 2010
This is version 36 of the entry and version 1 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