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Database: UniProt
Entry: A0A2C9VP23_MANES
LinkDB: A0A2C9VP23_MANES
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ID   A0A2C9VP23_MANES        Unreviewed;       426 AA.
AC   A0A2C9VP23;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Presenilin {ECO:0000256|RuleBase:RU361148};
DE            EC=3.4.23.- {ECO:0000256|RuleBase:RU361148};
GN   ORFNames=MANES_06G084500 {ECO:0000313|EMBL:OAY47502.1};
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY47502.1, ECO:0000313|Proteomes:UP000091857};
RN   [1] {ECO:0000313|EMBL:OAY47502.1, ECO:0000313|Proteomes:UP000091857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY47502.1};
RA   Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA   Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA   Stites J., Rounsley S., Rokhsar D.S.;
RT   "WGS assembly of Manihot esculenta.";
RL   Submitted (FEB-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}.
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DR   EMBL; CM004392; OAY47502.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9VP23; -.
DR   STRING; 3983.A0A2C9VP23; -.
DR   EnsemblPlants; OAY47502; OAY47502; MANES_06G084500.
DR   Gramene; OAY47502; OAY47502; MANES_06G084500.
DR   OMA; YEARPVN; -.
DR   OrthoDB; 205653at2759; -.
DR   Proteomes; UP000091857; Chromosome lg6.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IEA:InterPro.
DR   GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
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:UP000091857};
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..39
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..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        132..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        160..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        185..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        367..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
SQ   SEQUENCE   426 AA;  46919 MW;  620D3A51305A9FF4 CRC64;
     MAQIQRPKSI IDSLGEEIIR IITPVSICMF IVVILVSILN TDSSSASTTI NTIATMAYTE
     TTSDSFWDKL GGALLNSLVF VAVVTVVTFL LVLLFYLRCT QFLKIYMGFS SFIVLGFMGG
     EIALFLIRDF SVPIDCFTFL VVLFNFSIVG VLAVFMSKMA IFVTQAYMVV IGVLVAYWFT
     LLPEWTTWAL LVAMALYDLA AVLLPVGPLR LLVELAISRD EDIPALVYEA RPVTNHDSSS
     RNGVGHRRLW RERRNVGNGS EENLSSESIL DSNLTNATVD VSHNTTRLVR AEEGQLLERD
     GELSAPLIDH RSSVQLRGEG NAVLSENLLL EGIGLGSTGA IKLGLGDFIF YSVLVGRAAM
     YDFMTVYACY FAIIAGLGIT LMLLAFYQKV LPALPVSVAL GVLFYFLTRL LLEVFVVQCS
     LNLVMF
//
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