Reviewed, UniProtKB/Swiss-Prot O93428 (CATD_CHIHA)

Names and origin

Protein names

Recommended name:
    Cathepsin D
    EC=3.4.23.5

Gene names

Name:

ctsd

Organism

Chionodraco hamatus (Antarctic teleost icefish)

Taxonomic identifier

36188 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Perciformes › Notothenioidei › Channichthyidae › Chionodraco

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Enzyme regulation	Inhibited by pepstatin. Ref.1
Subunit structure	Monomer By similarity. UniProtKB Q9DEX3
Subcellular location	Lysosome By similarity. UniProtKB Q9DEX3
Sequence similarities	Belongs to the peptidase A1 family.
Biophysicochemical properties	pH dependence: Optimum pH is 3.0. Ref.1 Temperature dependence: Highly thermostable. Enzyme activity is maintained up to 45 degrees Celsius. Active at 50 degrees Celsius but with reduced catalytic activity. Ref.1
Sequence caution	The sequence CAA07719.1 differs from that shown. Reason: Frameshift at positions 19 and 55.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aspartic-type endopeptidase activity Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Propeptide	19 – 61	43	Activation peptide Ref.1		PRO_0000285984
	Chain	62 – 396	335	Cathepsin D Ref.1		PRO_5000064481
Sites
	Active site	94	1	By similarity UniProtKB P07339
	Active site	281	1	By similarity UniProtKB P07339
Amino acid modifications
	Glycosylation	131	1	N-linked (GlcNAc...) Potential
	Glycosylation	249	1	N-linked (GlcNAc...) Potential
	Disulfide bond	107 ↔ 114		By similarity UniProtKB P07339
	Disulfide bond	272 ↔ 276		By similarity UniProtKB P07339
	Disulfide bond	315 ↔ 352		By similarity UniProtKB P07339

Sequences

	Sequence		Length	Mass (Da)
	O93428-1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: B660E5E7FBD023FF	FASTA	396	42,958
	10 20 30 40 50 60 MKMLLLCVFS ALALTNDALV RIPLKKFRSI RRQLTDSGKR AEELLADHHS LKYNLSFPAS 70 80 90 100 110 120 NAPTPETLKN YLDAQYYGEI GLGTPPQPFT VVFDTGSSNL WVPSIHCSLL DIACLLHHKY 130 140 150 160 170 180 NSGKSSTYVK NGTAFAIQYG SGSLSGYLSQ DTCTIGDLAI DSQLFGEAIK QPGVAFIAAK 190 200 210 220 230 240 FDGILGMAYP RISVDGVAPV FDNIMSQKKV EQNVFSFYLN RNPDTEPGGE LLLGGTDPKY 250 260 270 280 290 300 YTGDFNYVNV TRQAYWQIRV DSMAVGDQLS LCTGGCEAIV DSGTSLITGP SVEVKALQKA 310 320 330 340 350 360 IGAFPLIQGE YMVNCDTVPS LPVISFTVGG QVYTLTGEQY ILKVTQAGKT MCLSGFMGLD 370 380 390 IPAPAGPLWI LGDVFMGQYY TVFDRDANRV GFAKAK

References

[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: 10209280] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 62-90, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ007878 mRNA. Translation: CAA07719.1. Frameshift.
3D structure databases
HSSP	HSSP built from PDB template 1LYW based on UniProtKB P07339.
ModBase	Search...
Protein family/group databases
MEROPS	A01.009.
Phylogenomic databases
HOVERGEN	O93428.
Enzyme and pathway databases
BRENDA	3.4.23.5. 275374.
Family and domain databases
InterPro	IPR001461. Peptidase_A1. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. IPR012848. Propep_A1. [Graphical view]
Gene3D	G3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
PANTHER	PTHR13683. Peptidase_A1. 1 hit.
Pfam	PF07966. A1_Propeptide. 1 hit. PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
PROSITE	PS00141. ASP_PROTEASE. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATD_CHIHA

Accession

Primary (citable) accession number: O93428

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	May 1, 2007
Last modified:	June 16, 2009
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)