ID A0A1B0GWE8_HUMAN Unreviewed; 410 AA. AC A0A1B0GWE8; 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:ENSP00000490897}; GN Name=CTSD {ECO:0000313|Ensembl:ENSP00000490897}; 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:ENSP00000490897, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000490897, 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:ENSP00000490897} 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}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC068580; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR jPOST; A0A1B0GWE8; -. DR PeptideAtlas; A0A1B0GWE8; -. DR Ensembl; ENST00000636843; ENSP00000490897; ENSG00000117984. DR HGNC; HGNC:2529; CTSD. DR OpenTargets; ENSG00000117984; -. DR GeneTree; ENSGT00940000155733; -. DR ChiTaRS; CTSD; human. DR Proteomes; UP000005640; Chromosome 11. DR ExpressionAtlas; A0A1B0GWE8; 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:A0A1B0GWE8, KW ECO:0000213|MaxQB:A0A1B0GWE8, ECO:0000213|PeptideAtlas:A0A1B0GWE8}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 410 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008408691. FT DOMAIN 77 405 Peptidase A1. FT {ECO:0000259|PROSITE:PS51767}. FT ACT_SITE 95 95 {ECO:0000256|PROSITE-ProRule:PRU01103}. FT ACT_SITE 293 293 {ECO:0000256|PROSITE-ProRule:PRU01103}. SQ SEQUENCE 410 AA; 44353 MW; 15528FF44B00EDFC CRC64; MQPSSLLPLA LCLLAAPASA LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP AVTEGPIPEV LKNYMDYYGE IGIGTPPQCF TVVFDTGSSN LWVPSIHCKL LDIACWIHHK YNSDKSSTYV KNGTSFDIHY GSGSLSGYLS QDTVSVPCQS ASSASALGGV KVERQVFGEA TKQPGITFIA AKFDGILGMA YPRISVNNVL PVFDNLMQQK LVDQNIFSFY LSRDPDAQPG GELMLGGTDS KYYKGSLSYL NVTRKAYWQV HLDQVEVASG LTLCKEGCEA IVDTGTSLMV GPVDEVRELQ KAIGAVPLIQ GEYMIPCEKV STLPAITLKL GGKGYKLSPE DYTLKVSQAG KTLCLSGFMG MDIPPPSGPL WILGDVFIGR YYTVFDRDNN RVGFAEAARL //