ID Q0MS44_PIG Unreviewed; 467 AA. AC Q0MS44; DT 19-SEP-2006, integrated into UniProtKB/TrEMBL. DT 19-SEP-2006, sequence version 1. DT 29-SEP-2021, entry version 69. DE RecName: Full=Presenilin {ECO:0000256|RuleBase:RU361148}; DE EC=3.4.23.- {ECO:0000256|RuleBase:RU361148}; GN Name=PSEN1 {ECO:0000313|EMBL:ABI15723.1}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ABI15723.1}; RN [1] {ECO:0000313|EMBL:ABI15723.1} RP NUCLEOTIDE SEQUENCE. RA Madsen L.B., Thomsen B., Larsen K., Fredholm M., Joergensen A.L., RA Holm I.E., Nielsen A.L., Bendixen C.; RL Submitted (JUL-2006) 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 junction, synapse CC {ECO:0000256|ARBA:ARBA00004547}. Cell projection, axon CC {ECO:0000256|ARBA:ARBA00004489}. Cell projection, neuron projection CC {ECO:0000256|ARBA:ARBA00004487}. Cytoplasmic granule CC {ECO:0000256|ARBA:ARBA00004463}. Early endosome membrane CC {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004520}. Endoplasmic reticulum membrane CC {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU361148}. Golgi apparatus membrane CC {ECO:0000256|ARBA:ARBA00004653, ECO:0000256|RuleBase:RU361148}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004653, CC ECO:0000256|RuleBase:RU361148}. Endosome membrane CC {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004337}. 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; DQ853416; ABI15723.1; -; mRNA. DR RefSeq; NP_001072135.1; NM_001078667.1. DR MEROPS; A22.001; -. DR GeneID; 780411; -. DR KEGG; ssc:780411; -. DR CTD; 5663; -. DR OMA; MQPVADP; -. DR OrthoDB; 797738at2759; -. DR ChiTaRS; PSEN1; pig. DR Genevisible; Q0MS44; SS. DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell. DR GO; GO:0031901; C:early endosome membrane; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:0042987; P:amyloid precursor protein catabolic process; IEA:InterPro. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0035556; P:intracellular signal transduction; 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; -; 1. DR InterPro; IPR002031; Pept_A22A_PS1. DR InterPro; IPR001108; Peptidase_A22A. DR InterPro; IPR006639; Preselin/SPP. DR InterPro; IPR042524; Presenilin_C. DR PANTHER; PTHR10202; PTHR10202; 1. DR Pfam; PF01080; Presenilin; 1. DR PRINTS; PR01072; PRESENILIN. DR PRINTS; PR01073; PRESENILIN1. DR SMART; SM00730; PSN; 1. PE 2: Evidence at transcript level; KW Apoptosis {ECO:0000256|ARBA:ARBA00022703}; KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889}; KW Cell junction {ECO:0000256|ARBA:ARBA00022949}; 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}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Protease {ECO:0000256|RuleBase:RU361148}; 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 83..101 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 134..155 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 162..184 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 196..214 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 226..242 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 248..269 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 408..428 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT TRANSMEM 434..453 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361148" FT REGION 1..68 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 307..376 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..29 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 30..48 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 309..331 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 337..352 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 467 AA; 52412 MW; 2A4007CA65A097FA CRC64; MTELPAPLSY FQNAQMSEDN HVSNNVSSQN DSRERHEHSI ERRRRGNSES LSNGGAQGNS RQVVEQEEEE DEELTLKYGA KHVIMLFVPV TLCMVVVVAT IKSVSFYTRK DGQLIYTPFT EDTETVGQRA LHSILNAAIM ISVIVVMTIL LVVLYKYRCY KVIHAWLIIS SLLLLFFFSF IYLGEVFKTY NVAMDYITVA LLIWNFGVVG MIAIHWKGPL RLQQAYLIMI SALMALVFIK YLPEWTAWLI LAVISVYDLV AVLCPNGPLR LLVETAQERN ETLFPALIYS STMVWLVNMA EGDPEAQRKV SKNSNYNAQS TGESQDSVTE SDDGGFSEEW EAQRDSRLGP HHSTAESRSA VQDLSRSIPA TEDPEERGVK LGLGDFIFYS VLVGKASATA SGDWNTTIAC FVAILIGLCL TLLLLAIFKK ALPALPISIT FGLVFYFATD YLVQPFMDQL AFHQFYI //