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Cathepsin D (EC 3.4.23.5) [Cleaved into: Cathepsin D 12 kDa light chain; Cathepsin D 9 kDa light chain; Cathepsin D 34 kDa heavy chain; Cathepsin D 30 kDa heavy chain]

 CATD_RAT                Reviewed;         407 AA.
P24268;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 1.
20-DEC-2017, entry version 139.
RecName: Full=Cathepsin D;
EC=3.4.23.5;
Contains:
RecName: Full=Cathepsin D 12 kDa light chain;
Contains:
RecName: Full=Cathepsin D 9 kDa light chain;
Contains:
RecName: Full=Cathepsin D 34 kDa heavy chain;
Contains:
RecName: Full=Cathepsin D 30 kDa heavy chain;
Flags: Precursor;
Name=Ctsd;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Pituitary;
PubMed=2243802; DOI=10.1093/nar/18.21.6445;
Birch N.P., Loh Y.P.;
"Cloning, sequence and expression of rat cathepsin D.";
Nucleic Acids Res. 18:6445-6445(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 65-74; 118-127 AND
165-174, AND SUBUNIT.
TISSUE=Liver;
PubMed=1883350; DOI=10.1016/0006-291X(91)91353-E;
Fujita H., Tanaka Y., Noguchi Y., Kono A., Himeno M., Kato K.;
"Isolation and sequencing of a cDNA clone encoding rat liver lysosomal
cathepsin D and the structure of three forms of mature enzymes.";
Biochem. Biophys. Res. Commun. 179:190-196(1991).
[3]
PROTEIN SEQUENCE OF 134-170.
PubMed=3182800;
Yonezawa S., Takahashi T., Wang X., Wong R.N.S., Hartsuck J.A.,
Tang J.;
"Structures at the proteolytic processing region of cathepsin D.";
J. Biol. Chem. 263:16504-16511(1988).
[4]
PROTEIN SEQUENCE OF 35-62; 65-72; 172-189; 222-248; 283-304 AND
309-348, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
-!- FUNCTION: Acid protease active in intracellular protein breakdown.
Plays a role in APP processing following cleavage and activation
by ADAM30 which leads to APP degradation.
{ECO:0000250|UniProtKB:P07339}.
-!- 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: Occurs as a mixture of both a single chain form and two
types of two chain (light and heavy) forms (PubMed:1883350).
Interacts with ADAM30; this leads to activation of CTSD (By
similarity). {ECO:0000250|UniProtKB:P07339,
ECO:0000269|PubMed:1883350}.
-!- SUBCELLULAR LOCATION: Lysosome. Melanosome {ECO:0000250}.
Secreted, extracellular space {ECO:0000250}.
-!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P07339}.
-!- PTM: Undergoes proteolytic cleavage and activation by ADAM30.
{ECO:0000250|UniProtKB:P07339}.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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EMBL; X54467; CAA38349.1; -; mRNA.
PIR; S13111; KHRTD.
UniGene; Rn.11085; -.
ProteinModelPortal; P24268; -.
SMR; P24268; -.
IntAct; P24268; 1.
MINT; MINT-1775033; -.
STRING; 10116.ENSRNOP00000027407; -.
MEROPS; A01.009; -.
iPTMnet; P24268; -.
PhosphoSitePlus; P24268; -.
SwissPalm; P24268; -.
UniCarbKB; P24268; -.
PaxDb; P24268; -.
PRIDE; P24268; -.
UCSC; RGD:621511; rat.
RGD; 621511; Ctsd.
eggNOG; KOG1339; Eukaryota.
eggNOG; ENOG410XNV7; LUCA.
HOGENOM; HOG000197681; -.
HOVERGEN; HBG000482; -.
InParanoid; P24268; -.
PhylomeDB; P24268; -.
BRENDA; 3.4.23.5; 5301.
PRO; PR:P24268; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005576; C:extracellular region; ISO:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0005764; C:lysosome; IDA:RGD.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0045121; C:membrane raft; ISO:RGD.
GO; GO:0005739; C:mitochondrion; ISO:RGD.
GO; GO:0004190; F:aspartic-type endopeptidase activity; ISO:RGD.
GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
GO; GO:0016787; F:hydrolase activity; ISO:RGD.
GO; GO:0008233; F:peptidase activity; ISO:RGD.
GO; GO:0042277; F:peptide binding; IDA:RGD.
GO; GO:0000045; P:autophagosome assembly; ISO:RGD.
GO; GO:0006914; P:autophagy; IBA:GO_Central.
GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
GO; GO:0006508; P:proteolysis; IDA:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
CDD; cd05490; Cathepsin_D2; 1.
Gene3D; 2.40.70.10; -; 2.
InterPro; IPR001461; Aspartic_peptidase_A1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR012848; Aspartic_peptidase_N.
InterPro; IPR033144; Cathepsin_D.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
PANTHER; PTHR13683; PTHR13683; 1.
Pfam; PF07966; A1_Propeptide; 1.
Pfam; PF00026; Asp; 1.
PRINTS; PR00792; PEPSIN.
SUPFAM; SSF50630; SSF50630; 1.
PROSITE; PS00141; ASP_PROTEASE; 2.
PROSITE; PS51767; PEPTIDASE_A1; 1.
1: Evidence at protein level;
Aspartyl protease; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
Reference proteome; Secreted; Signal; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 64 Activation peptide. {ECO:0000255}.
/FTId=PRO_0000025958.
CHAIN 65 407 Cathepsin D.
/FTId=PRO_0000025959.
CHAIN 65 164 Cathepsin D 12 kDa light chain.
/FTId=PRO_0000025960.
CHAIN 65 117 Cathepsin D 9 kDa light chain.
/FTId=PRO_0000025961.
CHAIN 118 407 Cathepsin D 34 kDa heavy chain.
/FTId=PRO_0000025962.
CHAIN 165 407 Cathepsin D 30 kDa heavy chain.
/FTId=PRO_0000025963.
DOMAIN 79 402 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
ACT_SITE 97 97 {ECO:0000255|PROSITE-ProRule:PRU10094}.
ACT_SITE 290 290 {ECO:0000255|PROSITE-ProRule:PRU10094}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 91 160 {ECO:0000250}.
DISULFID 110 117 {ECO:0000250}.
DISULFID 281 285 {ECO:0000250}.
DISULFID 324 361 {ECO:0000250}.
CONFLICT 15 15 D -> A (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 163 163 D -> T (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 205 205 K -> N (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 262 262 K -> N (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 407 AA; 44681 MW; C423AD4104D95F84 CRC64;
MQTPGVLLLI LGLLDASSSA LIRIPLRKFT SIRRTMTEVG GSVEDLILKG PITKYSMQSS
PRTKEPVSEL LKNYLDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWVH
HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC KSDLGGIKVE KQIFGEATKQ
PGVVFIAAKF DGILGMGYPF ISVNKVLPVF DNLMKQKLVE KNIFSFYLNR DPTGQPGGEL
MLGGTDSRYY HGELSYLNVT RKAYWQVHMD QLEVGSELTL CKGGCEAIVD TGTSLLVGPV
DEVKELQKAI GAVPLIQGEY MIPCEKVSSL PIITFKLGGQ NYELHPEKYI LKVSQAGKTI
CLSGFMGMDI PPPSGPLWIL GDVFIGCYYT VFDREYNRVG FAKAATL


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