PSN1_BOVIN
ID PSN1_BOVIN Reviewed; 478 AA.
AC Q9XT97;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Presenilin-1;
DE Short=PS-1;
DE EC=3.4.23.-;
DE Contains:
DE RecName: Full=Presenilin-1 NTF subunit;
DE Contains:
DE RecName: Full=Presenilin-1 CTF subunit;
DE Contains:
DE RecName: Full=Presenilin-1 CTF12;
DE Short=PS1-CTF12;
GN Name=PSEN1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Sahara N., Shirasawa T., Mori H.;
RT "Molecular cloning of bovine presenilin 1 gene.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of the gamma-secretase complex, an
CC endoprotease complex that catalyzes the intramembrane cleavage of
CC integral membrane proteins such as Notch receptors and APP (amyloid-
CC beta precursor protein). Requires the presence of the other members of
CC the gamma-secretase complex for protease activity. Plays a role in
CC Notch and Wnt signaling cascades and regulation of downstream processes
CC via its role in processing key regulatory proteins, and by regulating
CC cytosolic CTNNB1 levels. Stimulates cell-cell adhesion via its
CC interaction with CDH1; this stabilizes the complexes between CDH1 (E-
CC cadherin) and its interaction partners CTNNB1 (beta-catenin), CTNND1
CC and JUP (gamma-catenin). Under conditions of apoptosis or calcium
CC influx, cleaves CDH1. This promotes the disassembly of the complexes
CC between CDH1 and CTNND1, JUP and CTNNB1, increases the pool of
CC cytoplasmic CTNNB1, and thereby negatively regulates Wnt signaling (By
CC similarity). Required for normal embryonic brain and skeleton
CC development, and for normal angiogenesis (By similarity). Mediates the
CC proteolytic cleavage of EphB2/CTF1 into EphB2/CTF2 (By similarity). The
CC holoprotein functions as a calcium-leak channel that allows the passive
CC movement of calcium from endoplasmic reticulum to cytosol and is
CC therefore involved in calcium homeostasis. Involved in the regulation
CC of neurite outgrowth (By similarity). Is a regulator of presynaptic
CC facilitation, spike transmission and synaptic vesicles replenishment in
CC a process that depends on gamma-secretase activity. It acts through the
CC control of SYT7 presynaptic expression (By similarity).
CC {ECO:0000250|UniProtKB:P49768, ECO:0000250|UniProtKB:P49769}.
CC -!- SUBUNIT: Homodimer. The functional gamma-secretase complex is composed
CC of at least four polypeptides: a presenilin homodimer (PSEN1 or PSEN2),
CC nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2. Such minimal complex
CC is sufficient for secretase activity. Other components which are
CC associated with the complex include SLC25A64, SLC5A7 and PHB. As part
CC of the gamma-secretase complex, interacts with CRB2 (via transmembrane
CC domain) (By similarity). Predominantly heterodimer of a N-terminal
CC (NTF) and a C-terminal (CTF) endoproteolytical fragment. Associates
CC with proteolytic processed C-terminal fragments C83 and C99 of the
CC amyloid precursor protein (APP). Associates with NOTCH1. Associates
CC with cadherin/catenin adhesion complexes through direct binding to CDH1
CC or CDH2. Interaction with CDH1 stabilizes the complex and stimulates
CC cell-cell aggregation. Interaction with CDH2 is essential for
CC trafficking of CDH2 from the endoplasmic reticulum to the plasma
CC membrane. Interacts with CTNND2, CTNNB1, CTNND1, JUP, HERPUD1, FLNA,
CC FLNB, MTCH1, PKP4 and PARL. Interacts through its N-terminus with GFAP
CC (By similarity). Interacts with DOCK3 (By similarity). Interacts with
CC UBQLN1 (By similarity). {ECO:0000250|UniProtKB:P49768,
CC ECO:0000250|UniProtKB:P49769}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P49768}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P49768}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P49768}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:P49768}. Cell membrane
CC {ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P49768}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:P49768}. Early endosome
CC {ECO:0000250|UniProtKB:P49768}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P49768}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:P49768}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q4JIM4}. Synapse {ECO:0000250|UniProtKB:Q4JIM4}.
CC Note=Translocates with bound NOTCH1 from the endoplasmic reticulum
CC and/or Golgi to the cell surface. Colocalizes with CDH1/2 at sites of
CC cell-cell contact. Colocalizes with CTNNB1 in the endoplasmic reticulum
CC and the proximity of the plasma membrane. Also present in azurophil
CC granules of neutrophils. Colocalizes with UBQLN1 in the cell membrane
CC and in cytoplasmic juxtanuclear structures called aggresomes.
CC {ECO:0000250|UniProtKB:P49768}.
CC -!- DOMAIN: The PAL motif is required for normal active site conformation.
CC {ECO:0000250|UniProtKB:P49768}.
CC -!- DOMAIN: Substrates, such as NOTCH1 and APP peptides, are bound between
CC PSEN1 transmembrane domains and via the first lumenal loop and the
CC cytoplasmic loop between the sixth and seventh transmembrane domains.
CC Substrate binding causes a conformation change and formation of an
CC intermolecular antiparallel beta-sheet between PSEN1 and its
CC substrates. {ECO:0000250|UniProtKB:P49768}.
CC -!- PTM: Heterogeneous proteolytic processing generates N-terminal (NTF)
CC and C-terminal (CTF) fragments of approximately 35 and 20 kDa,
CC respectively. During apoptosis, the C-terminal fragment (CTF) is
CC further cleaved by caspase-3 to produce the fragment, PS1-CTF12.
CC {ECO:0000250|UniProtKB:P49768}.
CC -!- PTM: After endoproteolysis, the C-terminal fragment (CTF) is
CC phosphorylated on serine residues by PKA and/or PKC. Phosphorylation on
CC Ser-357 inhibits endoproteolysis. {ECO:0000250|UniProtKB:P49768}.
CC -!- SIMILARITY: Belongs to the peptidase A22A family. {ECO:0000305}.
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DR EMBL; AF038936; AAD39023.1; -; mRNA.
DR RefSeq; NP_777146.1; NM_174721.2.
DR RefSeq; XP_005211988.1; XM_005211931.3.
DR RefSeq; XP_005211989.1; XM_005211932.3.
DR RefSeq; XP_015328709.1; XM_015473223.1.
DR AlphaFoldDB; Q9XT97; -.
DR SMR; Q9XT97; -.
DR STRING; 9913.ENSBTAP00000040765; -.
DR MEROPS; A22.001; -.
DR PaxDb; Q9XT97; -.
DR PRIDE; Q9XT97; -.
DR Ensembl; ENSBTAT00000043175; ENSBTAP00000040765; ENSBTAG00000011757.
DR Ensembl; ENSBTAT00000068561; ENSBTAP00000057240; ENSBTAG00000011757.
DR GeneID; 282705; -.
DR KEGG; bta:282705; -.
DR CTD; 5663; -.
DR VEuPathDB; HostDB:ENSBTAG00000011757; -.
DR VGNC; VGNC:33434; PSEN1.
DR eggNOG; KOG2736; Eukaryota.
DR GeneTree; ENSGT00940000158751; -.
DR InParanoid; Q9XT97; -.
DR OMA; MQPVADP; -.
DR OrthoDB; 797738at2759; -.
DR TreeFam; TF315040; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000011757; Expressed in spermatid and 103 other tissues.
DR ExpressionAtlas; Q9XT97; baseline and differential.
DR GO; GO:0016235; C:aggresome; ISS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0035253; C:ciliary rootlet; IBA:GO_Central.
DR GO; GO:0043198; C:dendritic shaft; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070765; C:gamma-secretase complex; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005262; F:calcium channel activity; IEA:Ensembl.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0070851; F:growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IBA:GO_Central.
DR GO; GO:0042982; P:amyloid precursor protein metabolic process; ISS:UniProtKB.
DR GO; GO:0034205; P:amyloid-beta formation; ISS:UniProtKB.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IBA:GO_Central.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0002265; P:astrocyte activation involved in immune response; IEA:Ensembl.
DR GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0021870; P:Cajal-Retzius cell differentiation; IEA:Ensembl.
DR GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
DR GO; GO:0021795; P:cerebral cortex cell migration; IEA:Ensembl.
DR GO; GO:0015871; P:choline transport; IEA:Ensembl.
DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IEA:Ensembl.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; IEA:Ensembl.
DR GO; GO:0040011; P:locomotion; IEA:Ensembl.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0006839; P:mitochondrial transport; IEA:Ensembl.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0050771; P:negative regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:1904797; P:negative regulation of core promoter binding; IEA:Ensembl.
DR GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0070050; P:neuron cellular homeostasis; IEA:Ensembl.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:1990535; P:neuron projection maintenance; IEA:Ensembl.
DR GO; GO:0007220; P:Notch receptor processing; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1905908; P:positive regulation of amyloid fibril formation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:0050820; P:positive regulation of coagulation; IEA:Ensembl.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
DR GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
DR GO; GO:0002038; P:positive regulation of L-glutamate import across plasma membrane; IEA:Ensembl.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0006486; P:protein glycosylation; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:Ensembl.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0060075; P:regulation of resting membrane potential; IEA:Ensembl.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR GO; GO:0051208; P:sequestering of calcium ion; IEA:Ensembl.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
DR GO; GO:0051563; P:smooth endoplasmic reticulum calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR GO; GO:0016080; P:synaptic vesicle targeting; IEA:Ensembl.
DR GO; GO:0002286; P:T cell activation involved in immune response; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
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; Cell adhesion; Cell membrane; Cell projection;
KW Endoplasmic reticulum; Endosome; Golgi apparatus; Hydrolase; Membrane;
KW Notch signaling pathway; Phosphoprotein; Protease; Reference proteome;
KW Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..299
FT /note="Presenilin-1 NTF subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025589"
FT CHAIN 300..478
FT /note="Presenilin-1 CTF subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025590"
FT CHAIN 357..478
FT /note="Presenilin-1 CTF12"
FT /evidence="ECO:0000250"
FT /id="PRO_0000236051"
FT TOPO_DOM 1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TOPO_DOM 105..133
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TOPO_DOM 155..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TRANSMEM 168..190
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TOPO_DOM 191..195
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TRANSMEM 196..217
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TOPO_DOM 218..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TOPO_DOM 243..249
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TRANSMEM 250..273
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TOPO_DOM 274..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TOPO_DOM 413..418
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TOPO_DOM 440..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT TOPO_DOM 465..478
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..291
FT /note="Important for cleavage of target proteins"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT REGION 307..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..461
FT /note="Required for interaction with CTNNB1"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT REGION 383..410
FT /note="Required for interaction with CTNND2"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT REGION 388..392
FT /note="Important for cleavage of target proteins"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT REGION 443..445
FT /note="Important for cleavage of target proteins"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT REGION 475..478
FT /note="Interaction with MTCH1"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT MOTIF 444..446
FT /note="PAL"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 258
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT ACT_SITE 396
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT SITE 292..293
FT /note="Cleavage; alternate"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT SITE 293..294
FT /note="Cleavage; alternate"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT SITE 299..300
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT SITE 356..357
FT /note="Cleavage; by caspase"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97887"
FT MOD_RES 311
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97887"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97887"
FT MOD_RES 357
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49768"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49769"
SQ SEQUENCE 478 AA; 53654 MW; 59E3FC0A1010D906 CRC64;
MTELPAPLSY FQNAQMSEDN HLSNTVRSQN DSRERHEHGN ERRRRGNTES VSNGRAPSSS
QQVVEQEEEE DEELTLKYGA KHVIMLFVPV TLCMVVVVAT IKSVSFYTRK DGQLIYTPFT
EDTETVAQRA LHSILNAVIM ISVIVIMTIL LVVLYKYRCY KVIHAWLIVS SLLLLFFFSF
IYLGEVFKTY NVAMDYISVA LLIWNFGVVG MIAIHWKGPL RLQQAYLIMI SALMALVFIK
YLPEWTAWLI LAVISVYDLV AVLCPKGPLR MLVETAQERN ETLFPALIYS STMVWLVNMA
EGDPEAQRKV SKNSNYNAQR PANSPVTTTG TESESQDPVT ESDDGGFSEE WEAQRDSRLG
PHHSTAESRS AVQDLSSSIL ASEDPEERGV KLGLGDFIFY SVLVGKASAT ASGDWNTTIA
CFVAILIGLC LTLLLLAIFK KALPALPVSI TFGLIFYFAT DYLVQPFMDQ LAFHQFYI
