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Reviewed, UniProtKB/Swiss-Prot P24268 (CATD_RAT)

Last modified June 16, 2009. Version 81. 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

Names and origin

Protein namesRecommended name:
    Cathepsin D
    EC=3.4.23.5
Cleaved into the following 4 chains:
    1- Recommended name:
            Cathepsin D 12 kDa light chain
    2- Recommended name:
            Cathepsin D 9 kDa light chain
    3- Recommended name:
            Cathepsin D 34 kDa heavy chain
    4- Recommended name:
            Cathepsin D 30 kDa heavy chain
Gene names
Name: Ctsd
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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

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

Subcellular location

Lysosome. Melanosome By similarity.

Sequence similarities

Belongs to the peptidase A1 family.

Ontologies

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

Inferred from expression pattern. Source: RGD

proteolysis

Inferred from direct assay. Source: RGD

   Cellular componentlysosome

Inferred from direct assay. Source: RGD

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

soluble fraction

Inferred from direct assay. Source: RGD

   Molecular functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

peptide binding

Inferred from direct assay. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 6444Activation peptide Potential
PRO_0000025958
Chain65 – 407343Cathepsin D
PRO_0000025959
Chain65 – 164100Cathepsin D 12 kDa light chain
PRO_0000025960
Chain65 – 11753Cathepsin D 9 kDa light chain
PRO_0000025961
Chain118 – 407290Cathepsin D 34 kDa heavy chain
PRO_0000025962
Chain165 – 407243Cathepsin D 30 kDa heavy chain
PRO_0000025963

Sites

Active site971 By similarity
Active site2901 By similarity

Amino acid modifications

Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Disulfide bond91 ↔ 160 By similarity
Disulfide bond110 ↔ 117 By similarity
Disulfide bond281 ↔ 285 By similarity
Disulfide bond324 ↔ 361 By similarity

Experimental info

Sequence conflict151D → A AA sequence Ref.2
Sequence conflict1631D → T AA sequence Ref.3
Sequence conflict2051K → N AA sequence Ref.2
Sequence conflict2621K → N AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P24268-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: C423AD4104D95F84

FASTA40744,681
        10         20         30         40         50         60 
MQTPGVLLLI LGLLDASSSA LIRIPLRKFT SIRRTMTEVG GSVEDLILKG PITKYSMQSS 

        70         80         90        100        110        120 
PRTKEPVSEL LKNYLDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWVH 

       130        140        150        160        170        180 
HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC KSDLGGIKVE KQIFGEATKQ 

       190        200        210        220        230        240 
PGVVFIAAKF DGILGMGYPF ISVNKVLPVF DNLMKQKLVE KNIFSFYLNR DPTGQPGGEL 

       250        260        270        280        290        300 
MLGGTDSRYY HGELSYLNVT RKAYWQVHMD QLEVGSELTL CKGGCEAIVD TGTSLLVGPV 

       310        320        330        340        350        360 
DEVKELQKAI GAVPLIQGEY MIPCEKVSSL PIITFKLGGQ NYELHPEKYI LKVSQAGKTI 

       370        380        390        400 
CLSGFMGMDI PPPSGPLWIL GDVFIGCYYT VFDREYNRVG FAKAATL 

« Hide

References

[1]"Cloning, sequence and expression of rat cathepsin D."
Birch N.P., Loh Y.P.
Nucleic Acids Res. 18:6445-6445(1990) [PubMed: 2243802] [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: 1883350] [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: 3182800] [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, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Spinal cord.

Cross-references

Sequence databases

X54467 mRNA. Translation: CAA38349.1.
IPIIPI00212731.
PIRKHRTD. S13111.
UniGeneRn.11085

3D structure databases

HSSPHSSP built from PDB template 1LYB based on UniProtKB P07339.
SMRP24268. Positions 165-405.
ModBaseSearch...

Protein family/group databases

MEROPSA01.009.

Proteomic databases

PRIDEP24268.

Genome annotation databases

EnsemblENSRNOG00000020206. Rattus norvegicus. [Contig view]

Organism-specific databases

RGD621511. Ctsd.

Phylogenomic databases

HOVERGENP24268.

Enzyme and pathway databases

BRENDA3.4.23.5. 248.

Gene expression databases

ArrayExpressP24268.
GermOnlineENSRNOG00000020206. Rattus norvegicus.

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...

Entry information

Entry nameCATD_RAT
AccessionPrimary (citable) accession number: P24268
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 16, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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