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Cathepsin D (EC 3.4.23.5) [Cleaved into: Cathepsin D light chain; Cathepsin D heavy chain]

 CATD_CHICK              Reviewed;         398 AA.
Q05744;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
12-SEP-2018, entry version 135.
RecName: Full=Cathepsin D;
EC=3.4.23.5;
Contains:
RecName: Full=Cathepsin D light chain;
Contains:
RecName: Full=Cathepsin D heavy chain;
Flags: Precursor;
Name=CTSD;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 64-97.
TISSUE=Follicular cell;
PubMed=1418623; DOI=10.1089/dna.1992.11.661;
Retzek H., Steyrer E., Sanders E.J., Nimpf J., Schneider W.J.;
"Molecular cloning and functional characterization of chicken
cathepsin D, a key enzyme for yolk formation.";
DNA Cell Biol. 11:661-672(1992).
-!- FUNCTION: Acid protease active in intracellular protein breakdown.
In chicken it is a key enzyme for yolk formation as it is capable
of catalyzing intra oocytic break down of protein components of
both vitellogenin and VLDL.
-!- 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: Consists of a light chain and a heavy chain.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- TISSUE SPECIFICITY: Oocytic yolk, preovulatory follicles, liver.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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EMBL; S49650; AAB24157.1; -; mRNA.
PIR; I51185; I51185.
RefSeq; NP_990508.1; NM_205177.1.
UniGene; Gga.1094; -.
ProteinModelPortal; Q05744; -.
SMR; Q05744; -.
STRING; 9031.ENSGALP00000010662; -.
MEROPS; A01.009; -.
PaxDb; Q05744; -.
PRIDE; Q05744; -.
Ensembl; ENSGALT00000010676; ENSGALP00000010662; ENSGALG00000006613.
GeneID; 396090; -.
KEGG; gga:396090; -.
CTD; 1509; -.
eggNOG; KOG1339; Eukaryota.
eggNOG; ENOG410XNV7; LUCA.
GeneTree; ENSGT00760000118929; -.
HOGENOM; HOG000197681; -.
HOVERGEN; HBG000482; -.
InParanoid; Q05744; -.
KO; K01379; -.
OMA; WNGQYTV; -.
OrthoDB; EOG091G0JP7; -.
PhylomeDB; Q05744; -.
TreeFam; TF314990; -.
Reactome; R-GGA-1442490; Collagen degradation.
Reactome; R-GGA-2022377; Metabolism of Angiotensinogen to Angiotensins.
Reactome; R-GGA-2132295; MHC class II antigen presentation.
Reactome; R-GGA-6798695; Neutrophil degranulation.
PRO; PR:Q05744; -.
Proteomes; UP000000539; Chromosome 5.
Bgee; ENSGALG00000006613; Expressed in 11 organ(s), highest expression level in spleen.
GO; GO:0005764; C:lysosome; IDA:AgBase.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
GO; GO:0006914; P:autophagy; IBA:GO_Central.
GO; GO:0008219; P:cell death; IEP:AgBase.
GO; GO:0012501; P:programmed cell death; IDA:AgBase.
GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
GO; GO:0006508; P:proteolysis; IBA:GO_Central.
CDD; cd05490; Cathepsin_D2; 1.
Gene3D; 2.40.70.10; -; 3.
InterPro; IPR001461; Aspartic_peptidase_A1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR033144; Cathepsin_D.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
PANTHER; PTHR13683; PTHR13683; 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; Signal; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 63 Activation peptide. {ECO:0000255}.
/FTId=PRO_0000025966.
CHAIN 64 398 Cathepsin D.
/FTId=PRO_0000025967.
CHAIN 64 157 Cathepsin D light chain. {ECO:0000305}.
/FTId=PRO_0000025968.
CHAIN 158 398 Cathepsin D heavy chain. {ECO:0000305}.
/FTId=PRO_0000025969.
DOMAIN 78 395 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
ACT_SITE 96 96 {ECO:0000255|PROSITE-ProRule:PRU10094}.
ACT_SITE 283 283 {ECO:0000255|PROSITE-ProRule:PRU10094}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 251 251 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 109 116 {ECO:0000250}.
DISULFID 274 278 {ECO:0000250}.
DISULFID 317 354 {ECO:0000250}.
SEQUENCE 398 AA; 43298 MW; 584C99E2755AA2B1 CRC64;
MAPRGLLVLL LLALVGPCAA LIRIPLTKFT STRRMLTEVG SEIPDMNAIT QFLKFKLGFA
DLAEPTPEIL KNYMDAQYYG EIGIGTPPQK FTVVFDTGSS NLWVPSVHCH LLDIACLLHH
KYDASKSSTY VENGTEFAIH YGTGSLSGFL SQDTVTLGNL KIKNQIFGEA VKQPGITFIA
AKFDGILGMA FPRISVDKVT PFFDNVMQQK LIEKNIFSFY LNRDPTAQPG GELLLGGTDP
KYYSGDFSWV NVTRKAYWQV HMDSVDVANG LTLCKGGCEA IVDTGTSLIT GPTKEVKELQ
TAIGAKPLIK GQYVISCDKI SSLPVVTLML GGKPYQLTGE QYVFKVSAQG ETICLSGFSG
LDVPPPGGPL WILGDVFIGP YYTVFDRDND SVGFAKCV


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