ID A0A0L8G1S6_OCTBM Unreviewed; 507 AA.
AC A0A0L8G1S6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 02-OCT-2024, entry version 36.
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}.
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DR EMBL; KQ424738; KOF70540.1; -; Genomic_DNA.
DR RefSeq; XP_014785182.1; XM_014929696.1.
DR AlphaFoldDB; A0A0L8G1S6; -.
DR EnsemblMetazoa; XM_014929696.2; 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
//