ID A0A2K5NYU1_CERAT Unreviewed; 447 AA.
AC A0A2K5NYU1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Presenilin {ECO:0000256|RuleBase:RU361148};
DE EC=3.4.23.- {ECO:0000256|RuleBase:RU361148};
GN Name=PSEN2 {ECO:0000313|Ensembl:ENSCATP00000042531.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000042531.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000042531.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_011895892.1; XM_012040502.1.
DR RefSeq; XP_011895893.1; XM_012040503.1.
DR AlphaFoldDB; A0A2K5NYU1; -.
DR Ensembl; ENSCATT00000066965.1; ENSCATP00000042531.1; ENSCATG00000043861.1.
DR GeneID; 105576920; -.
DR CTD; 5664; -.
DR GeneTree; ENSGT00940000157923; -.
DR OMA; MICIHWQ; -.
DR OrthoDB; 205653at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000043861; Expressed in spleen and 12 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IEA:InterPro.
DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
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; IPR001493; Pept_A22A_PS2.
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; 2.
DR PRINTS; PR01072; PRESENILIN.
DR PRINTS; PR01074; PRESENILIN2.
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 Reference proteome {ECO:0000313|Proteomes:UP000233060};
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 88..106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 139..160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 201..219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 226..244
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 250..269
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 414..433
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 50004 MW; BAABFB2FFF919EFD CRC64;
MLTFMASDSE EEVCDERTSL MSAESPTPRS CQEGRQGPED GENIAQWRSQ ENEEDGEEDP
DHYVCSGVPG RPPGLEEELT LKYGAKHVIM LFVPVTLCMI VVVATIKSVR FYTEKNGQLI
YTPFTEDTPS VGQRLLNSVL NTLIMISVIV VMTIFLVVLY KYRCYKFIHG WLIMSSLMLL
FLFTYIYLGE VLKTYNVAMD YPTLLLTVWN FGAVGMVCIH WKGPLVLQQA YLIMISALMA
LVFIKYLPEW SAWVILGAIS VYDLVAVLCP KGPLRMLVET AQERNEPIFP ALIYSSAMVW
TVGMAKLDPS SQGALQLPYD PEMEDSYDSF GEPSYPEVFE PPLTGYPGEE LEEEEERGVK
LGLGDFIFYS VLVGKAAATG SGDWNTTLAC FVAILIGLCL TLLLLAVFKK ALPALPISIT
FGLIFYFSTD NLVRPFMDTL ASHQLYI
//
