CATD_CHICK
ID CATD_CHICK Reviewed; 398 AA.
AC Q05744;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cathepsin D;
DE EC=3.4.23.5;
DE Contains:
DE RecName: Full=Cathepsin D light chain;
DE Contains:
DE RecName: Full=Cathepsin D heavy chain;
DE Flags: Precursor;
GN Name=CTSD;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 64-97.
RC TISSUE=Follicular cell;
RX PubMed=1418623; DOI=10.1089/dna.1992.11.661;
RA Retzek H., Steyrer E., Sanders E.J., Nimpf J., Schneider W.J.;
RT "Molecular cloning and functional characterization of chicken cathepsin D,
RT a key enzyme for yolk formation.";
RL DNA Cell Biol. 11:661-672(1992).
CC -!- FUNCTION: Acid protease active in intracellular protein breakdown. In
CC chicken it is a key enzyme for yolk formation as it is capable of
CC catalyzing intra oocytic break down of protein components of both
CC vitellogenin and VLDL.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specificity similar to, but narrower than, that of pepsin A.
CC Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.;
CC EC=3.4.23.5;
CC -!- SUBUNIT: Consists of a light chain and a heavy chain.
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- TISSUE SPECIFICITY: Oocytic yolk, preovulatory follicles, liver.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; S49650; AAB24157.1; -; mRNA.
DR PIR; I51185; I51185.
DR RefSeq; NP_990508.1; NM_205177.1.
DR AlphaFoldDB; Q05744; -.
DR SMR; Q05744; -.
DR STRING; 9031.ENSGALP00000010662; -.
DR MEROPS; A01.009; -.
DR PaxDb; Q05744; -.
DR PRIDE; Q05744; -.
DR Ensembl; ENSGALT00000010676; ENSGALP00000010662; ENSGALG00000006613.
DR GeneID; 396090; -.
DR KEGG; gga:396090; -.
DR CTD; 1509; -.
DR VEuPathDB; HostDB:geneid_396090; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000155733; -.
DR HOGENOM; CLU_013253_3_3_1; -.
DR InParanoid; Q05744; -.
DR OMA; GVHDAAC; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; Q05744; -.
DR TreeFam; TF314990; -.
DR Reactome; R-GGA-2132295; MHC class II antigen presentation.
DR Reactome; R-GGA-5683826; Surfactant metabolism.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR PRO; PR:Q05744; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000006613; Expressed in lung and 13 other tissues.
DR GO; GO:0010008; C:endosome membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IDA:AgBase.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
DR GO; GO:0008219; P:cell death; IEP:AgBase.
DR GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0012501; P:programmed cell death; IDA:AgBase.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0070201; P:regulation of establishment of protein localization; IEA:Ensembl.
DR CDD; cd05490; Cathepsin_D2; 1.
DR Gene3D; 2.40.70.10; -; 3.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033144; Cathepsin_D.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lysosome; Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..63
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000025966"
FT CHAIN 64..398
FT /note="Cathepsin D"
FT /id="PRO_0000025967"
FT CHAIN 64..157
FT /note="Cathepsin D light chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000025968"
FT CHAIN 158..398
FT /note="Cathepsin D heavy chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000025969"
FT DOMAIN 78..395
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..116
FT /evidence="ECO:0000250"
FT DISULFID 274..278
FT /evidence="ECO:0000250"
FT DISULFID 317..354
FT /evidence="ECO:0000250"
SQ 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
