Reviewed, UniProtKB/Swiss-Prot Q9DEX3 (CATD_CLUHA)

Names and origin

Protein names

Recommended name:
    Cathepsin D
    EC=3.4.23.5

Gene names

Name:

ctsd

Organism

Clupea harengus (Atlantic herring)

Taxonomic identifier

7950 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Clupeomorpha › Clupeiformes › Clupeidae › Clupea

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. Ref.2
Enzyme regulation	Inhibited by pepstatin. Ref.2
Subunit structure	Monomer. Ref.2
Subcellular location	Lysosome.
Sequence similarities	Belongs to the peptidase A1 family.
Biophysicochemical properties	pH dependence: Optimum pH is 2.5 with hemoglobin as substrate. Temperature dependence: Optimum temperature is 37 degrees Celsius.

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 Inferred from electronic annotation. Source: InterPro
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
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.2 UniProtKB Q05744		PRO_0000025970
	Chain	62 – 396	335	Cathepsin D Ref.2		PRO_0000025971
Sites
	Active site	94	1	By similarity
	Active site	281	1	By similarity UniProtKB Q05744
Amino acid modifications
	Glycosylation	131	1	N-linked (GlcNAc...) Potential
	Disulfide bond	107 ↔ 114		By similarity UniProtKB Q05744
	Disulfide bond	272 ↔ 276		By similarity UniProtKB Q05744
	Disulfide bond	315 ↔ 352		By similarity UniProtKB Q05744

Sequences

	Sequence		Length	Mass (Da)
	Q9DEX3-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: D0375DC38567A31B	FASTA	396	43,316
	10 20 30 40 50 60 MKFLYLFLFA VFAWTSDAIV RIPLKKFRSI RRTLSDSGLN VEQLLAGTNS LQHNQGFPSS 70 80 90 100 110 120 NAPTPETLKN YMDAQYYGEI GLGTPVQMFT VVFDTGSSNL WLPSIHCSFT DIACLLHHKY 130 140 150 160 170 180 NGAKSSTYVK NGTEFAIQYG SGSLSGYLSQ DSCTIGDIVV EKQLFGEAIK QPGVAFIAAK 190 200 210 220 230 240 FDGILGMAYP RISVDGVPPV FDMMMSQKKV EQNVFSFYLN RNPDTEPGGE LLLGGTDPKY 250 260 270 280 290 300 YTGDFNYVPV TRQAYWQIHM DGMSIGSQLT LCKDGCEAIV DTGTSLITGP PAEVRALQKA 310 320 330 340 350 360 IGAIPLIQGE YMIDCKKVPT LPTISFNVGG KTYSLTGEQY VLKESQGGKT ICLSGLMGLE 370 380 390 IPPPAGPLWI LGDVFIGQYY TVFDRESNRV GFAKST

References

[1]	"Cloning and sequence determination of herring muscle cathepsin D." Nielsen L.B., Stougaard P., Andersen P.S., Pedersen L.H. Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Purification and characterization of cathepsin D from herring muscle (Clupea harengus)." Nielsen L.B., Nielsen H.H. Comp. Biochem. Physiol. 128B:351-363(2001) [PubMed: 11207447] [Abstract] Cited for: PROTEIN SEQUENCE OF 62-82. Tissue: Skeletal muscle.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF312364 mRNA. Translation: AAG27733.1.
3D structure databases
HSSP	HSSP built from PDB template 1LYW based on UniProtKB P07339.
SMR	Q9DEX3. Positions 156-395.
ModBase	Search...
Protein family/group databases
MEROPS	A01.009.
Phylogenomic databases
HOVERGEN	Q9DEX3.
Enzyme and pathway databases
BRENDA	3.4.23.5. 267218.
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_CLUHA

Accession

Primary (citable) accession number: Q9DEX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)