ID A0A7K9X8F7_9GRUI Unreviewed; 458 AA. AC A0A7K9X8F7; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 27-MAR-2024, entry version 9. DE RecName: Full=Presenilin {ECO:0000256|RuleBase:RU361148}; DE EC=3.4.23.- {ECO:0000256|RuleBase:RU361148}; DE Flags: Fragment; GN Name=Psen2 {ECO:0000313|EMBL:NXI93714.1}; GN ORFNames=PSOCRE_R10364 {ECO:0000313|EMBL:NXI93714.1}; OS Psophia crepitans (common trumpeter). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Gruiformes; Psophiidae; Psophia. OX NCBI_TaxID=54359 {ECO:0000313|EMBL:NXI93714.1, ECO:0000313|Proteomes:UP000587472}; RN [1] {ECO:0000313|EMBL:NXI93714.1, ECO:0000313|Proteomes:UP000587472} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B10K-DU-001-60 {ECO:0000313|EMBL:NXI93714.1}; RC TISSUE=Muscle {ECO:0000313|EMBL:NXI93714.1}; RA Zhang G.; RT "Bird 10,000 Genomes (B10K) Project - Family phase."; RL Submitted (SEP-2019) 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:NXI93714.1}. 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; VWZZ01002725; NXI93714.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7K9X8F7; -. DR Proteomes; UP000587472; 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:UP000587472}; 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 94..112 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 145..166 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 173..195 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 207..227 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 234..250 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 256..275 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 399..419 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 425..444 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT REGION 1..71 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 321..358 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 19..33 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 325..343 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:NXI93714.1" FT NON_TER 458 FT /evidence="ECO:0000313|EMBL:NXI93714.1" SQ SEQUENCE 458 AA; 51326 MW; F5C488E1E3A536E7 CRC64; MITFMNNSDS EEEPCNERTS LMSAESPPVP SYQDGLQASE AGEAQAHRKR RTGSSRGPNN IADGDMSDSG VPVRERALEN EEEELTLKYG AKHVIMLFVP VTLCMIVVVA TIKSVRFYTE KNGQLIYTPF SEDTPSVGQR LLNSVLNTII MISVIVVMTV FLVLLYKYRC YKFIHGWLIL SSLMLLFLFT YIYLGEVLKT YNVAMDYPTL FLVIWNFGAV GMICIHWKGP LQLQQAYLIM ISALMALVFI KYLPEWSAWV ILGAISIYDL MAVLCPKGPL RMLVETAQER NEPIFPALIY SSAMMWTVGM AKPDTAARRS SQQMWDAAED GREDHRSPSH ADSQMSERRS PVSTRPITSF EELEEEERGV KLGLGDFIFY SVLVGKAAAT ASGDWNTTLA CFVAILIGLC LTLLLLAVFK KALPALPISI TFGLVFYFST DNLVRPFMDT LASHQLYI //