ID E9PJG7_HUMAN Unreviewed; 467 AA. AC E9PJG7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 2. DT 13-FEB-2019, entry version 64. DE SubName: Full=Beta-secretase 1 {ECO:0000313|Ensembl:ENSP00000431848}; GN Name=BACE1 {ECO:0000313|Ensembl:ENSP00000431848}; 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:ENSP00000431848, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000431848, 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:0000313|Ensembl:ENSP00000431848} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) 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; AP000892; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877486; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; E9PJG7; -. DR jPOST; E9PJG7; -. DR PeptideAtlas; E9PJG7; -. DR PRIDE; E9PJG7; -. DR Ensembl; ENST00000528053; ENSP00000431848; ENSG00000186318. DR UCSC; uc058htj.1; human. DR EuPathDB; HostDB:ENSG00000186318.16; -. DR HGNC; HGNC:933; BACE1. DR OpenTargets; ENSG00000186318; -. DR GeneTree; ENSGT00940000157786; -. DR ChiTaRS; BACE1; human. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000186318; Expressed in 223 organ(s), highest expression level in C1 segment of cervical spinal cord. DR ExpressionAtlas; E9PJG7; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-UniRule. DR CDD; cd05473; beta_secretase_like; 1. DR Gene3D; 2.40.70.10; -; 3. DR InterPro; IPR001461; Aspartic_peptidase_A1. DR InterPro; IPR001969; Aspartic_peptidase_AS. DR InterPro; IPR009119; BACE. DR InterPro; IPR009120; BACE1. DR InterPro; IPR033874; Memapsin-like. DR InterPro; IPR033121; PEPTIDASE_A1. DR InterPro; IPR021109; Peptidase_aspartic_dom_sf. DR PANTHER; PTHR13683; PTHR13683; 2. DR PANTHER; PTHR13683:SF245; PTHR13683:SF245; 2. DR Pfam; PF00026; Asp; 2. DR PRINTS; PR01816; BACE1. DR PRINTS; PR01815; BACEFAMILY. 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 {ECO:0000256|PROSITE-ProRule:PRU01103, KW ECO:0000256|RuleBase:RU000454}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01103, KW ECO:0000256|RuleBase:RU000454}; Membrane {ECO:0000256|SAM:Phobius}; KW Protease {ECO:0000256|PROSITE-ProRule:PRU01103, KW ECO:0000256|RuleBase:RU000454}; KW Proteomics identification {ECO:0000213|MaxQB:E9PJG7, KW ECO:0000213|PeptideAtlas:E9PJG7}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 467 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003244096. FT TRANSMEM 424 444 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 75 382 Peptidase A1. FT {ECO:0000259|PROSITE:PS51767}. FT ACT_SITE 93 93 {ECO:0000256|PROSITE-ProRule:PRU01103}. FT ACT_SITE 277 277 {ECO:0000256|PROSITE-ProRule:PRU01103}. SQ SEQUENCE 467 AA; 52080 MW; 25E46ECDABCC864C CRC64; MAQALPWLLL WMGAGVLPAH GTQHGIRLPL RSGLGGAPLG LRLPRETDEE PEEPGRRGSF VEMVDNLRGK SGQGYYVEMT VGSPPQTLNI LVDTGSSNFA VGAAPHPFLH RYYQRQLSST YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH GPNVTVRANI AAITESDKFF INGSNWEGIL GLAYAEIARP DDSLEPFFDS LVKQTHVPNL FSLQLCGAGF PLNQSEVLAS VGGSMIIGGI DHSLYTGSLW YTPIRREWYY EVIIVRVEIN GQDLKMDCKE TEKFPDGFWL GEQLVCWQAG TTPWNIFPVI SLYLMGEVTN QSFRITILPQ QYLRPVEDVA TSQDDCYKFA ISQSSTGTVM GAVIMEGFYV VFDRARKRIG FAVSACHVHD EFRTAAVEGP FVTLDMEDCG YNIPQTDEST LMTIAYVMAA ICALFMLPLC LMVCQWRCLR CLRQQHDDFA DDISLLK //