Reviewed, UniProtKB/Swiss-Prot P24268 (CATD_RAT)

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	407 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.
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. MelanosomeBy similarity.
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Propeptide	21 – 64	44	Activation peptide Potential
	Chain	65 – 407	343	Cathepsin D
	Chain	65 – 164	100	Cathepsin D 12 kDa light chain
	Chain	65 – 117	53	Cathepsin D 9 kDa light chain
	Chain	118 – 407	290	Cathepsin D 34 kDa heavy chain
	Chain	165 – 407	243	Cathepsin D 30 kDa heavy chain
Sites
	Active site	97	1	By similarity
	Active site	290	1	By similarity
Amino acid modifications
	Glycosylation	134	1	N-linked (GlcNAc...) Potential
	Glycosylation	258	1	N-linked (GlcNAc...) Potential
	Disulfide bond	91 ↔ 160		By similarity
	Disulfide bond	110 ↔ 117		By similarity
	Disulfide bond	281 ↔ 285		By similarity
	Disulfide bond	324 ↔ 361		By similarity
Experimental info
	Sequence conflict	15	1	D → A AA sequence Ref.2
	Sequence conflict	163	1	D → T AA sequence Ref.3
	Sequence conflict	205	1	K → N AA sequence Ref.2
	Sequence conflict	262	1	K → N AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P24268-1 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: C423AD4104D95F84	FASTA	407	44,681
	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

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
EMBLGenBankDDBJ	X54467 mRNA. Translation: CAA38349.1.
PIR	KHRTD. S13111.
UniGene	Rn.11085
3D structure databases
HSSP	HSSP built from PDB template 1LYB based on UniProtKB P07339.
SMR	P24268. Positions 165-405.
ModBase	Search...
Protein-protein interaction databases
IntAct	P24268.
Protein family/group databases
MEROPS	A01.009.
Genome annotation databases
Ensembl	ENSRNOG00000020206. Rattus norvegicus. [Contig view]
Organism-specific databases
RGD	621511. Ctsd.
Phylogenomic databases
HOVERGEN	P24268.
Gene expression databases
ArrayExpress	P24268.
GermOnline	ENSRNOG00000020206. Rattus norvegicus.
Family and domain databases
InterPro	IPR001969. Pept_Asp_AS. IPR009007. Pept_Aspartc_cat. IPR001461. Peptidase_A1. 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]
ProDom	P24268. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

CATD_RAT

Accession

Primary (citable) accession number: P24268

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	September 2, 2008
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)