ID A0A1B0GW44_HUMAN Unreviewed; 405 AA. AC A0A1B0GW44; 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:ENSP00000490770}; GN Name=CTSD {ECO:0000313|Ensembl:ENSP00000490770}; 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:ENSP00000490770, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000490770, 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:ENSP00000490770} 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; A0A1B0GW44; -. DR PeptideAtlas; A0A1B0GW44; -. DR Ensembl; ENST00000636571; ENSP00000490770; ENSG00000117984. DR HGNC; HGNC:2529; CTSD. DR OpenTargets; ENSG00000117984; -. DR GeneTree; ENSGT00940000155733; -. DR ChiTaRS; CTSD; human. DR Proteomes; UP000005640; Chromosome 11. DR ExpressionAtlas; A0A1B0GW44; 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:A0A1B0GW44, KW ECO:0000213|MaxQB:A0A1B0GW44, ECO:0000213|PeptideAtlas:A0A1B0GW44}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 405 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008408761. FT DOMAIN 72 400 Peptidase A1. FT {ECO:0000259|PROSITE:PS51767}. FT ACT_SITE 90 90 {ECO:0000256|PROSITE-ProRule:PRU01103}. FT ACT_SITE 288 288 {ECO:0000256|PROSITE-ProRule:PRU01103}. SQ SEQUENCE 405 AA; 43688 MW; 5C06A6AE9C48AD79 CRC64; MQPSSLLPLA LCLLAAPASA LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP AVTEGPIPEA QYYGEIGIGT PPQCFTVVFD TGSSNLWVPS IHCKLLDIAC WIHHKYNSDK SSTYVKNGTS FDIHYGSGSL SGYLSQDTVS VPCQSASSAS ALGGVKVERQ VFGEATKQPG ITFIAAKFDG ILGMAYPRIS VNNVLPVFDN LMQQKLVDQN IFSFYLSRDP DAQPGGELML GGTDSKYYKG SLSYLNVTRK AYWQVHLDQV EVASGLTLCK EGCEAIVDTG TSLMVGPVDE VRELQKAIGA VPLIQGEYMI PCEKVSTLPA ITLKLGGKGY KLSPEDYTLK VSQAGKTLCL SGFMGMDIPP PSGPLWILGD VFIGRYYTVF DRDNNRVGFA EAARL //