P24268 (CATD_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cathepsin D
EC=3.4.23.5

Cleaved into the following 4 chains:

1. Cathepsin D 12 kDa light chain
2. Cathepsin D 9 kDa light chain
3. Cathepsin D 34 kDa heavy chain
4. Cathepsin D 30 kDa heavy chain

Gene names

Name:

Ctsd

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › 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. Melanosome By similarity. Secreted › extracellular space By similarity.
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Cellular component	Lysosome Secreted
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	autophagy Inferred from expression pattern PubMed 17665967. Source: RGD proteolysis Inferred from direct assay PubMed 12666874. Source: RGD
Cellular_component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from direct assay PubMed 11687729PubMed 12666874PubMed 8702598. Source: RGD melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW endopeptidase activity Inferred from direct assay PubMed 11687729PubMed 12666874PubMed 8702598. Source: RGD peptide binding Inferred from direct assay PubMed 8702598. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Propeptide	21 – 64	44	Activation peptide Potential		PRO_0000025958
	Chain	65 – 407	343	Cathepsin D		PRO_0000025959
	Chain	65 – 164	100	Cathepsin D 12 kDa light chain		PRO_0000025960
	Chain	65 – 117	53	Cathepsin D 9 kDa light chain		PRO_0000025961
	Chain	118 – 407	290	Cathepsin D 34 kDa heavy chain		PRO_0000025962
	Chain	165 – 407	243	Cathepsin D 30 kDa heavy chain		PRO_0000025963
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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X54467 mRNA. Translation: CAA38349.1.
IPI	IPI00212731.
PIR	KHRTD. S13111.
UniGene	Rn.11085.
3D structure databases
ProteinModelPortal	P24268.
SMR	P24268. Positions 66-405.
ModBase	Search...
Protein-protein interaction databases
IntAct	P24268. 1 interaction.
MINT	MINT-1775033.
STRING	10116.ENSRNOP00000029248.
Protein family/group databases
MEROPS	A01.009.
Proteomic databases
PaxDb	P24268.
PRIDE	P24268.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	RGD:621511. rat.
Organism-specific databases
RGD	621511. Ctsd.
Phylogenomic databases
eggNOG	NOG248684.
HOGENOM	HOG000197681.
HOVERGEN	HBG000482.
OrthoDB	EOG40GCR5.
Gene expression databases
ArrayExpress	P24268.
Genevestigator	P24268.
GermOnline	ENSRNOG00000020206. Rattus norvegicus.
Family and domain databases
Gene3D	2.40.70.10. 2 hits.
InterPro	IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. IPR012848. Propep_A1. [Graphical view]
PANTHER	PTHR13683. PTHR13683. 1 hit.
Pfam	PF07966. A1_Propeptide. 1 hit. PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
SUPFAM	SSF50630. Pept_Aspartic. 1 hit.
PROSITE	PS00141. ASP_PROTEASE. 2 hits. [Graphical view]
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:	April 3, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program