ID   A0A1B0GV23_HUMAN        Unreviewed;       406 AA.
AC   A0A1B0GV23;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   16-JAN-2019, entry version 15.
DE   SubName: Full=Cathepsin D {ECO:0000313|Ensembl:ENSP00000490344};
GN   Name=CTSD {ECO:0000313|Ensembl:ENSP00000490344};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000490344, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000490344, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [2] {ECO:0000213|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [3] {ECO:0000213|PubMed:25944712}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [4] {ECO:0000313|Ensembl:ENSP00000490344}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01103,
CC       ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS01079896}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01103}.
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DR   EMBL; AC068580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; A0A1B0GV23; -.
DR   jPOST; A0A1B0GV23; -.
DR   PeptideAtlas; A0A1B0GV23; -.
DR   Ensembl; ENST00000637815; ENSP00000490344; ENSG00000117984.
DR   HGNC; HGNC:2529; CTSD.
DR   OpenTargets; ENSG00000117984; -.
DR   GeneTree; ENSGT00940000155733; -.
DR   ChiTaRS; CTSD; human.
DR   Proteomes; UP000005640; Chromosome 11.
DR   ExpressionAtlas; A0A1B0GV23; baseline and differential.
DR   GO; GO:0005764; C:lysosome; IEA:InterPro.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd05490; Cathepsin_D2; 1.
DR   Gene3D; 2.40.70.10; -; 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; PTHR13683; PTHR13683; 1.
DR   Pfam; PF07966; A1_Propeptide; 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 {ECO:0000256|PROSITE-ProRule:PRU01103,
KW   ECO:0000256|RuleBase:RU000454};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00670207};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01103,
KW   ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01103,
KW   ECO:0000256|RuleBase:RU000454};
KW   Proteomics identification {ECO:0000213|EPD:A0A1B0GV23,
KW   ECO:0000213|MaxQB:A0A1B0GV23, ECO:0000213|PeptideAtlas:A0A1B0GV23};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    406       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008408647.
FT   DOMAIN       79    401       Peptidase A1.
FT                                {ECO:0000259|PROSITE:PS51767}.
FT   ACT_SITE     97     97       {ECO:0000256|PROSITE-ProRule:PRU01103}.
FT   ACT_SITE    289    289       {ECO:0000256|PROSITE-ProRule:PRU01103}.
SQ   SEQUENCE   406 AA;  43831 MW;  3EF793C92F82F143 CRC64;
     MQPSSLLPLA LCLLAAPASA LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP
     AVTEGPIPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH
     HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC QSASSASALG GVKVERQVFG
     EATKQPGITF IAAKFDGILG MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ
     PGGELMLGGT DSKYYKGSLS YLNVTRKAYW VEVASGLTLC KEGCEAIVDT GTSLMVGPVD
     EVRELQKAIG AVPLIQGEYM IPCEKVSTLP AITLKLGGKG YKLSPEDYTL KVSQAGKTLC
     LSGFMGMDIP PPSGPLWILG DVFIGRYYTV FDRDNNRVGF AEAARL
//