ID A0A0L8G1S6_OCTBM Unreviewed; 507 AA. AC A0A0L8G1S6; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 29-MAY-2024, entry version 35. DE RecName: Full=Presenilin {ECO:0000256|RuleBase:RU361148}; DE EC=3.4.23.- {ECO:0000256|RuleBase:RU361148}; GN ORFNames=OCBIM_22002682mg {ECO:0000313|EMBL:KOF70540.1}; OS Octopus bimaculoides (California two-spotted octopus). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda; OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus. OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF70540.1}; RN [1] {ECO:0000313|EMBL:KOF70540.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF70540.1}; RC TISSUE=Gonad {ECO:0000313|EMBL:KOF70540.1}; RA Tran T., Druce J.; RT "MeaNS - Measles Nucleotide Surveillance Program."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Probable subunit of the gamma-secretase complex, an CC endoprotease complex that catalyzes the intramembrane cleavage of CC integral membrane proteins such as Notch receptors. CC {ECO:0000256|RuleBase:RU361148}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU361148}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU361148}. Golgi apparatus membrane CC {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU361148}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- DOMAIN: The PAL motif is required for normal active site conformation. CC {ECO:0000256|RuleBase:RU361148}. CC -!- SIMILARITY: Belongs to the peptidase A22A family. CC {ECO:0000256|ARBA:ARBA00008604, ECO:0000256|RuleBase:RU361148}. 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; KQ424738; KOF70540.1; -; Genomic_DNA. DR RefSeq; XP_014785182.1; XM_014929696.1. DR AlphaFoldDB; A0A0L8G1S6; -. DR EnsemblMetazoa; Ocbimv22002680m; Ocbimv22002680m.p; Ocbimv22002682m.g. DR EnsemblMetazoa; XM_014929696.1; XP_014785182.1; LOC106879938. DR GeneID; 106879938; -. DR OrthoDB; 205653at2759; -. DR GO; GO:0016324; C:apical plasma membrane; IEA:TreeGrafter. DR GO; GO:0005938; C:cell cortex; IEA:TreeGrafter. DR GO; GO:0009986; C:cell surface; IEA:TreeGrafter. DR GO; GO:0035253; C:ciliary rootlet; IEA:TreeGrafter. DR GO; GO:0043198; C:dendritic shaft; IEA:TreeGrafter. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030426; C:growth cone; IEA:TreeGrafter. DR GO; GO:0005765; C:lysosomal membrane; IEA:TreeGrafter. DR GO; GO:0045121; C:membrane raft; IEA:TreeGrafter. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:TreeGrafter. DR GO; GO:0031594; C:neuromuscular junction; IEA:TreeGrafter. DR GO; GO:0043025; C:neuronal cell body; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:TreeGrafter. DR GO; GO:0030018; C:Z disc; IEA:TreeGrafter. DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IEA:InterPro. DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IEA:TreeGrafter. DR GO; GO:0050435; P:amyloid-beta metabolic process; IEA:TreeGrafter. DR GO; GO:0006816; P:calcium ion transport; IEA:TreeGrafter. DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:TreeGrafter. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:TreeGrafter. DR GO; GO:0007220; P:Notch receptor processing; IEA:TreeGrafter. DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0016485; P:protein processing; IEA:InterPro. DR Gene3D; 1.10.472.100; Presenilin; 1. DR InterPro; IPR001108; Peptidase_A22A. DR InterPro; IPR006639; Preselin/SPP. DR InterPro; IPR042524; Presenilin_C. DR PANTHER; PTHR10202; PRESENILIN; 1. DR PANTHER; PTHR10202:SF13; PRESENILIN-2; 1. DR Pfam; PF01080; Presenilin; 1. DR PRINTS; PR01072; PRESENILIN. DR SMART; SM00730; PSN; 1. PE 3: Inferred from homology; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, KW ECO:0000256|RuleBase:RU361148}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034, KW ECO:0000256|RuleBase:RU361148}; Hydrolase {ECO:0000256|RuleBase:RU361148}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361148}; KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976, KW ECO:0000256|RuleBase:RU361148}; Protease {ECO:0000256|RuleBase:RU361148}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU361148}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU361148}. FT TRANSMEM 103..127 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 154..175 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 182..204 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 216..234 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 241..259 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 447..468 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 474..493 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT REGION 1..86 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 324..360 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 388..419 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..30 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 34..69 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 326..360 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 391..407 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 507 AA; 56517 MW; 9141C80BD9FB4CF4 CRC64; MNQSSSDDEP TERTSLLSSP ASSGSPPRNH PNMETYIDAE RTERMNRRGQ RPDIRGIYDN DREAEVDPSE SEVSIPATVA RRKGYSSGTE EEEETLLYGA KHVIMLFVPV TLCMIVVVAT ISSVTYYTQP GGYLIYTPFH EETDDSGTKV WQSFANAFIL LGVIAVMTVV LLLLYKYRCY KVIHGWLIVS SLLLLFMFSY MYLGEVLKAY NAPMDYITVA ILMWNFGVIG MICIHWKGPL LLQQAYLLMI SALMALIFIK YLPDWTTWSV LGIMVFWDLV AVLCPKGPLR VLVETAQHRN EDIFPALIYS STMVWQIVTM ADESPKRDSG ANSTSTLATD VHSSPATNAT SNPEAGTNIY RNDVDAHNLT NSIDSQTARR AIDALGEMEN DPNSEANNRP PADRNQRSQG SGEEEEEERG VKLGLGDFIF YGVLVGKASS YGDWNTTLAC FVAILIGLCF TLLLLAIFRK ALPALPISIT FGLIFNFATR GLVRPFMDNL ASEQMYI //