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Database: UniProt
Entry: A0A091K1Y8_COLST
LinkDB: A0A091K1Y8_COLST
Original site: A0A091K1Y8_COLST 
ID   A0A091K1Y8_COLST        Unreviewed;       371 AA.
AC   A0A091K1Y8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Presenilin {ECO:0000256|RuleBase:RU361148};
DE            EC=3.4.23.- {ECO:0000256|RuleBase:RU361148};
DE   Flags: Fragment;
GN   ORFNames=N325_11506 {ECO:0000313|EMBL:KFP31025.1};
OS   Colius striatus (Speckled mousebird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX   NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP31025.1, ECO:0000313|Proteomes:UP000053615};
RN   [1] {ECO:0000313|EMBL:KFP31025.1, ECO:0000313|Proteomes:UP000053615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP31025.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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: Cell projection, axon
CC       {ECO:0000256|ARBA:ARBA00004489}. Cell projection, neuron projection
CC       {ECO:0000256|ARBA:ARBA00004487}. Cytoplasmic granule
CC       {ECO:0000256|ARBA:ARBA00004463}. 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}. Synapse
CC       {ECO:0000256|ARBA:ARBA00034103}.
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; KK541574; KFP31025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091K1Y8; -.
DR   MEROPS; A22.001; -.
DR   Proteomes; UP000053615; Unassembled WGS sequence.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; 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:SF18; PRESENILIN-1; 1.
DR   Pfam; PF01080; Presenilin; 1.
DR   PRINTS; PR01072; PRESENILIN.
DR   SMART; SM00730; PSN; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
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:UP000053615};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
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        16..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        67..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        95..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        129..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        159..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        181..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        338..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   REGION          239..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP31025.1"
FT   NON_TER         371
FT                   /evidence="ECO:0000313|EMBL:KFP31025.1"
SQ   SEQUENCE   371 AA;  41695 MW;  D19E77C2729BF3AE CRC64;
     EEEDEELTLK YGAKHVIMLF VPVTLCMVVV VATIKSVSFY TRKDGQLIYT PFTEETETVG
     QRALNSILNA AIMISVIIVM TILLVVLYKY RCYKVIHGWL IISSLLLLFF FSFIYLGEVF
     KTYNVAMDYI TVALMIWNFG VVGMICIHWK GPLRLQQAYL IMISALMALV FIKYLPEWTA
     WLILAVISVY DLVAVLCPKG PLRMLVETAQ ERNETLFPAL IYSSTMVWLV NMAEEDPEAQ
     RKASKNSTYD KQGPIESTPE SRAAVQALPS NSQTSEDPEE RGVKLGLGDF IFYSVLVGKA
     SATASGDWNT TLACFVAILI GLCLTLLLLA IFKKALPALP ISITFGLVFY FATDNLVQPF
     MDQLAFHQFY I
//
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