CATD_DICDI
ID CATD_DICDI Reviewed; 383 AA.
AC O76856; Q54WS2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cathepsin D;
DE EC=3.4.23.5;
DE AltName: Full=Ddp44;
DE Flags: Precursor;
GN Name=ctsD; Synonyms=CatD; ORFNames=DDB_G0279411;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 49-56; 77-92;
RP 103-116; 269-278; 325-336 AND 370-383, SUBUNIT, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RC STRAIN=AX2;
RX PubMed=10523518; DOI=10.1242/jcs.112.21.3833;
RA Journet A., Chapel A., Jehan S., Adessi C., Freeze H., Klein G., Garin J.;
RT "Characterization of Dictyostelium discoideum cathepsin D. Molecular
RT cloning, gene disruption, endo-lysosomal localization and sugar
RT modifications.";
RL J. Cell Sci. 112:3833-3843(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Protease that may act during cell growth and/or development.
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: Monomer. {ECO:0000269|PubMed:10523518}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:10523518}. Secreted
CC {ECO:0000269|PubMed:10523518}.
CC -!- DEVELOPMENTAL STAGE: Expressed in both vegetative and differentiating
CC cells, with a higher level in vegetative cells.
CC {ECO:0000269|PubMed:10523518}.
CC -!- PTM: N-glycosylated on 2 out of the 3 potential sites. Glycans contain
CC sulfated Mannose. {ECO:0000269|PubMed:10523518}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; Y16962; CAA76563.1; -; mRNA.
DR EMBL; AJ243946; CAB57223.1; -; Genomic_DNA.
DR EMBL; AAFI02000031; EAL67644.1; -; Genomic_DNA.
DR RefSeq; XP_641645.1; XM_636553.1.
DR AlphaFoldDB; O76856; -.
DR SMR; O76856; -.
DR STRING; 44689.DDB0215012; -.
DR MEROPS; A01.A89; -.
DR PaxDb; O76856; -.
DR EnsemblProtists; EAL67644; EAL67644; DDB_G0279411.
DR GeneID; 8622052; -.
DR KEGG; ddi:DDB_G0279411; -.
DR dictyBase; DDB_G0279411; ctsD.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_2_1; -.
DR InParanoid; O76856; -.
DR OMA; GVECANL; -.
DR PhylomeDB; O76856; -.
DR Reactome; R-DDI-1442490; Collagen degradation.
DR Reactome; R-DDI-2132295; MHC class II antigen presentation.
DR Reactome; R-DDI-5683826; Surfactant metabolism.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:O76856; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005769; C:early endosome; IDA:dictyBase.
DR GO; GO:0032009; C:early phagosome; IDA:dictyBase.
DR GO; GO:0005576; C:extracellular region; IDA:dictyBase.
DR GO; GO:0005764; C:lysosome; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0012501; P:programmed cell death; IDA:dictyBase.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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; 1.
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; Secreted; Signal;
KW Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..48
FT /evidence="ECO:0000269|PubMed:10523518"
FT /id="PRO_0000327788"
FT CHAIN 49..383
FT /note="Cathepsin D"
FT /id="PRO_5000147291"
FT DOMAIN 63..378
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..101
FT /evidence="ECO:0000250"
FT DISULFID 259..263
FT /evidence="ECO:0000250"
FT DISULFID 302..339
FT /evidence="ECO:0000250"
SQ SEQUENCE 383 AA; 41121 MW; CC8DE423AEA1A280 CRC64;
MKLLILTLFL ATIVLAQALT VPLNFHQASR ESRRRVPQKW SNRLSALNAG TTIPISDFED
AQYYGAITIG TPGQAFKVVF DTGSSNLWIP SKKCPITVVA CDLHNKYNSG ASSTYVANGT
DFTIQYGSGA MSGFVSQDSV TVGSLTVKDQ LFAEATAEPG IAFDFAKFDG ILGLAFQSIS
VNSIPPVFYN MLSQGLVSST LFSFWLSRTP GANGGELSFG SIDNTKYTGD ITYVPLTNET
YWEFVMDDFA IDGQSAGFCG TTCHAICDSG TSLIAGPMAD ITALNEKLGA VILNGEGVFS
DCSVINTLPN VTITVAGREF VLTPKEYVLE VTEFGKTECL SGFMGIELNM GNFWILGDVF
ISAYYTVFDF GNKQVGFATA IQG
