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Protein

Cathepsin D

Gene

ctsd

Organism
Chionodraco hamatus (Antarctic teleost icefish) (Chaenichthys rhinoceratus hamatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acid protease active in intracellular protein breakdown.Curated

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.Curated

Enzyme regulationi

Inhibited by pepstatin.1 Publication

pH dependencei

Optimum pH is 3.0.1 Publication

Temperature dependencei

Highly thermostable. Enzyme activity is maintained up to 45 degrees Celsius. Active at 50 degrees Celsius but with reduced catalytic activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei94 – 941PROSITE-ProRule annotationBy similarity
Active sitei281 – 2811PROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  • proteolysis Source: UniProtKB
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
OrganismiChionodraco hamatus (Antarctic teleost icefish) (Chaenichthys rhinoceratus hamatus)
Taxonomic identifieri36188 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataEupercariaPerciformesNotothenioideiChannichthyidaeChionodraco

Subcellular locationi

  • Lysosome By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 6143Activation peptideSequence analysis1 PublicationPRO_0000285984Add
BLAST
Chaini62 – 396335Cathepsin D1 PublicationPRO_5000064481Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi107 ↔ 114By similarity
Glycosylationi131 – 1311N-linked (GlcNAc...)Sequence analysis
Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence analysis
Disulfide bondi272 ↔ 276By similarity
Disulfide bondi315 ↔ 352By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiO93428.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO93428.
SMRiO93428. Positions 62-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 393318Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG000482.

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.

O93428-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMLLLCVFS ALALTNDALV RIPLKKFRSI RRQLTDSGKR AEELLADHHS
60 70 80 90 100
LKYNLSFPAS NAPTPETLKN YLDAQYYGEI GLGTPPQPFT VVFDTGSSNL
110 120 130 140 150
WVPSIHCSLL DIACLLHHKY NSGKSSTYVK NGTAFAIQYG SGSLSGYLSQ
160 170 180 190 200
DTCTIGDLAI DSQLFGEAIK QPGVAFIAAK FDGILGMAYP RISVDGVAPV
210 220 230 240 250
FDNIMSQKKV EQNVFSFYLN RNPDTEPGGE LLLGGTDPKY YTGDFNYVNV
260 270 280 290 300
TRQAYWQIRV DSMAVGDQLS LCTGGCEAIV DSGTSLITGP SVEVKALQKA
310 320 330 340 350
IGAFPLIQGE YMVNCDTVPS LPVISFTVGG QVYTLTGEQY ILKVTQAGKT
360 370 380 390
MCLSGFMGLD IPAPAGPLWI LGDVFMGQYY TVFDRDANRV GFAKAK
Length:396
Mass (Da):42,958
Last modified:May 1, 2007 - v2
Checksum:iB660E5E7FBD023FF
GO

Sequence cautioni

The sequence CAA07719.1 differs from that shown. Reason: Frameshift at positions 19 and 55. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007878 mRNA. Translation: CAA07719.1. Frameshift.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007878 mRNA. Translation: CAA07719.1. Frameshift.

3D structure databases

ProteinModelPortaliO93428.
SMRiO93428. Positions 62-395.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiA01.009.

Proteomic databases

PRIDEiO93428.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG000482.

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. "Cathepsin D from the liver of the Antarctic icefish Chionodraco hamatus exhibits unusual activity and stability at high temperatures."
    Capasso C., Lees W.E., Capasso A., Scudiero R., Carginale V., Kille P., Kay J., Parisi E.
    Biochim. Biophys. Acta 1431:64-73(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 62-90, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: LiverImported.

Entry informationi

Entry nameiCATD_CHIHA
AccessioniPrimary (citable) accession number: O93428
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: April 13, 2016
This is version 74 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

Direct protein sequencing

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.