ID A0A176VDM5_MARPO Unreviewed; 554 AA.
AC A0A176VDM5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Presenilin {ECO:0000256|RuleBase:RU361148};
DE EC=3.4.23.- {ECO:0000256|RuleBase:RU361148};
GN ORFNames=AXG93_461s1000 {ECO:0000313|EMBL:OAE18959.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE18959.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE18959.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE18959.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAE18959.1}.
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DR EMBL; LVLJ01003965; OAE18959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VDM5; -.
DR OrthoDB; 205653at2759; -.
DR Proteomes; UP000077202; 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: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:UP000077202};
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 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 67..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 103..124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 467..486
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT REGION 241..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 60064 MW; B05BC9CC2EE23F71 CRC64;
MTEGNILESL GSEIVGIVTP VSICMLLVVL LVQSLAPHGS DAPVNSIAML VYDEQPTDSF
SEKLGGAVLN ALVFVIIVAI VTFLLVLLFY FRCTKCLRAY MGFSAFMVLA YMGGGVAVLL
IQSFSIPIDA VTFAVLLYNF ATVGVLAVFF SKMPIFVTQG YLVMIGVLVA YWFTMLPEWT
TWVLLMAMAL YDVVAVLLPG GPLNMLVELA IARDEDIPAL IYEARPTTRY IASLPTSPSA
VSRNSSASGP AAVATRPPPR WRRRVTTTPV SGNVANLVTG QPAAIDMPEP ARNNDNVRPI
GISALRIESQ VPEQSGQQQQ GVGGLLLNNT NDHQENGPAV VERWTTRRSS SSDEEDTVPL
VSSQAQALIP PHSTVIMDGV ESSFPSAARS EAVNIEALLE DVVGNGESGV LSGAIKLGLG
DFIFYSVLVG RAAMYDMMTV YACYLAIVAG LGSTLILLTV WRRALPALPI SITLGVIFYL
LTRFIVDPFM RKKAPDAIRW DHLWIRKFGT FSILNHHSVA LRLSGETGHG IFDDADEMTV
YTKPKIRPQI HSLK
//
