ID H2NCE8_PONAB Unreviewed; 412 AA.
AC H2NCE8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Cathepsin D {ECO:0000256|ARBA:ARBA00015582};
DE EC=3.4.23.5 {ECO:0000256|ARBA:ARBA00011930};
GN Name=CTSD {ECO:0000313|Ensembl:ENSPPYP00000003382.3};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000003382.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000003382.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000003382.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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; Evidence={ECO:0000256|ARBA:ARBA00000585};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR AlphaFoldDB; H2NCE8; -.
DR Ensembl; ENSPPYT00000003499.3; ENSPPYP00000003382.3; ENSPPYG00000002911.3.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000155733; -.
DR HOGENOM; CLU_013253_3_3_1; -.
DR InParanoid; H2NCE8; -.
DR TreeFam; TF314990; -.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05490; Cathepsin_D2; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR033144; Cathepsin_D.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF42; CATHEPSIN D; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 79..407
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 97
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 295
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-3"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-3"
FT DISULFID 91..160
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-2"
FT DISULFID 110..117
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 286..290
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 329..366
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 412 AA; 44829 MW; 4A8C35ADF68CD6E1 CRC64;
QGPLSLLLAS WGLPDMPRPL VDRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQEMP
AVTEGPVPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH
RKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC QSASSASALG GVKVERQVFG
EATKQPGITF IAAKFDGILG MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ
PGGELMLGGT DSKYYKGSLS YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL
MVGPVDEVRE LQKAIGAVPL IQGEYMIPCE KVSTLPAITL KLGGKGYKLS PEDYTLKVSQ
AGKTLCLSGF MGMDIPPPSG PLWILGDVFI GRYYTVFDRD NNRVGFAEAA RV
//