ID D7LLE1_ARALL Unreviewed; 399 AA.
AC D7LLE1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Presenilin {ECO:0000256|RuleBase:RU361148};
DE EC=3.4.23.- {ECO:0000256|RuleBase:RU361148};
GN ORFNames=ARALYDRAFT_481900 {ECO:0000313|EMBL:EFH55498.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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; GL348716; EFH55498.1; -; Genomic_DNA.
DR RefSeq; XP_002879239.1; XM_002879193.1.
DR AlphaFoldDB; D7LLE1; -.
DR STRING; 81972.D7LLE1; -.
DR MEROPS; A22.A02; -.
DR EnsemblPlants; fgenesh2_kg.4__960__AT2G29900.1; fgenesh2_kg.4__960__AT2G29900.1; fgenesh2_kg.4__960__AT2G29900.1.
DR Gramene; fgenesh2_kg.4__960__AT2G29900.1; fgenesh2_kg.4__960__AT2G29900.1; fgenesh2_kg.4__960__AT2G29900.1.
DR eggNOG; KOG2736; Eukaryota.
DR HOGENOM; CLU_022975_3_0_1; -.
DR OrthoDB; 205653at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005798; C:Golgi-associated vesicle; IEA:EnsemblPlants.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000008694};
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 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 73..97
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 109..127
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 133..155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 188..209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 366..385
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
SQ SEQUENCE 399 AA; 44344 MW; BF1719DD1B37ABDA CRC64;
MDRNQRPRSL LDSLGEELIA ILTPVSICMF TVVLLVCILN SDPSSSSASF SSIATAAYAE
SDSDSSWDKF VGALLNSVVF VAAITVATFV LVLLFYLRCV KFLKFYMGFS AFIVLGNLGG
EILVLLIDRF RFPIDSITFL ILLFNFSVVG VFAVFMSKFS ILITQGYLVW IGVLVAYFFT
LLPEWTTWVL LVALALYDIA AVLLPVGPLR LLVEMAISRD EDIPALVYEA RPVIRNDSRL
VQRRVWRERR SNDAENHANR NEVRAVRSEE VEEEHVGSSE RAEISVPLID RRPEQAENSE
TFLEGIGLGS SGAIKLGLGD FIFYSVLVGR AAMYDLMTVY ACYLAIIAGL GITLMLLSVY
QKALPALPVS IMLGVVFYFL ARLLLEVFVV QCSSNLVMF
//
