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Presenilin-1 (PS-1) (EC 3.4.23.-) [Cleaved into: Presenilin-1 NTF subunit; Presenilin-1 CTF subunit; Presenilin-1 CTF12 (PS1-CTF12)]

 PSN1_CANLF              Reviewed;         466 AA.
Q6RH31; Q6RH32;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 2.
23-MAY-2018, entry version 85.
RecName: Full=Presenilin-1;
Short=PS-1;
EC=3.4.23.-;
Contains:
RecName: Full=Presenilin-1 NTF subunit;
Contains:
RecName: Full=Presenilin-1 CTF subunit;
Contains:
RecName: Full=Presenilin-1 CTF12;
Short=PS1-CTF12;
Name=PSEN1;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS I-462 AND I-466).
Nakata M.;
"Sequence analysis and chromosomal mapping of presenilin-1 and amyloid
precursor protein genes in dogs.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[2]
IDENTIFICATION IN COMPLEX WITH CDH1; CTNNB1; CTNND1 AND JUP.
PubMed=11226248; DOI=10.1073/pnas.041603398;
Baki L., Marambaud P., Efthimiopoulos S., Georgakopoulos A., Wen P.,
Cui W., Shioi J., Koo E., Ozawa M., Friedrich V.L., Robakis N.K.;
"Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits
cadherin/p120 association, and regulates stability and function of the
cadherin/catenin adhesion complex.";
Proc. Natl. Acad. Sci. U.S.A. 98:2381-2386(2001).
-!- FUNCTION: Catalytic subunit of the gamma-secretase complex, an
endoprotease complex that catalyzes the intramembrane cleavage of
integral membrane proteins such as Notch receptors and APP
(amyloid-beta precursor protein). Requires the presence of the
other members of the gamma-secretase complex for protease
activity. Plays a role in Notch and Wnt signaling cascades and
regulation of downstream processes via its role in processing key
regulatory proteins, and by regulating cytosolic CTNNB1 levels.
Stimulates cell-cell adhesion via its interaction with CDH1; this
stabilizes the complexes between CDH1 (E-cadherin) and its
interaction partners CTNNB1 (beta-catenin), CTNND1 and JUP (gamma-
catenin). Under conditions of apoptosis or calcium influx, cleaves
CDH1. This promotes the disassembly of the complexes between CDH1
and CTNND1, JUP and CTNNB1, increases the pool of cytoplasmic
CTNNB1, and thereby negatively regulates Wnt signaling (By
similarity). Required for normal embryonic brain and skeleton
development, and for normal angiogenesis (By similarity).
{ECO:0000250|UniProtKB:P49768, ECO:0000250|UniProtKB:P49769}.
-!- SUBUNIT: Homodimer. The functional gamma-secretase complex is
composed of at least four polypeptides: a presenilin homodimer
(PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and
PEN2. Such minimal complex is sufficient for secretase activity.
Other components which are associated with the complex include
SLC25A64, SLC5A7, PHB and PSEN1 isoform 3. Predominantly
heterodimer of a N-terminal (NTF) and a C-terminal (CTF)
endoproteolytical fragment. Associates with proteolytic processed
C-terminal fragments C83 and C99 of the amyloid precursor protein
(APP). Associates with NOTCH1. Associates with cadherin/catenin
adhesion complexes through direct binding to CDH1 or CDH2
(PubMed:11226248). Interaction with CDH1 stabilizes the complex
and stimulates cell-cell aggregation. Interaction with CDH2 is
essential for trafficking of CDH2 from the endoplasmic reticulum
to the plasma membrane. Interacts with CTNND2, CTNNB1, CTNND1,
JUP, HERPUD1, FLNA, FLNB, MTCH1, PKP4 and PARL. Interacts through
its N-terminus with isoform 3 of GFAP (By similarity). Interacts
with DOCK3 (By similarity). Interacts with isoform 1 and isoform 3
of UBQLN1 (By similarity). {ECO:0000250|UniProtKB:P49768,
ECO:0000250|UniProtKB:P49769, ECO:0000269|PubMed:11226248}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P49768}. Golgi apparatus membrane
{ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P49768}. Cytoplasmic granule
{ECO:0000250|UniProtKB:P49768}. Cell membrane
{ECO:0000250|UniProtKB:P49768}. Note=Translocates with bound
NOTCH1 from the endoplasmic reticulum and/or Golgi to the cell
surface. Colocalizes with CDH1/2 at sites of cell-cell contact.
Colocalizes with CTNNB1 in the endoplasmic reticulum and the
proximity of the plasma membrane. Also present in azurophil
granules of neutrophils. Colocalizes with UBQLN1 in the cell
membrane and in cytoplasmic juxtanuclear structures called
aggresomes. {ECO:0000250|UniProtKB:P49768}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=I-466;
IsoId=Q6RH31-1; Sequence=Displayed;
Name=I-462;
IsoId=Q6RH31-2; Sequence=VSP_018569;
-!- DOMAIN: The PAL motif is required for normal active site
conformation. {ECO:0000250|UniProtKB:P49768}.
-!- PTM: Heterogeneous proteolytic processing generates N-terminal
(NTF) and C-terminal (CTF) fragments of approximately 35 and 20
kDa, respectively. During apoptosis, the C-terminal fragment (CTF)
is further cleaved by caspase-3 to produce the fragment, PS1-
CTF12. {ECO:0000250|UniProtKB:P49768}.
-!- PTM: After endoproteolysis, the C-terminal fragment (CTF) is
phosphorylated on serine residues by PKA and/or PKC.
Phosphorylation on Ser-345 inhibits endoproteolysis.
{ECO:0000250|UniProtKB:P49768}.
-!- SIMILARITY: Belongs to the peptidase A22A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY498704; AAR97724.1; -; mRNA.
EMBL; AY498705; AAR97725.1; -; mRNA.
RefSeq; NP_001002943.2; NM_001002943.2.
RefSeq; NP_001280213.1; NM_001293284.1.
UniGene; Cfa.107; -.
STRING; 9615.ENSCAFP00000031755; -.
MEROPS; A22.001; -.
PaxDb; Q6RH31; -.
PRIDE; Q6RH31; -.
GeneID; 403408; -.
KEGG; cfa:403408; -.
CTD; 5663; -.
eggNOG; KOG2736; Eukaryota.
eggNOG; ENOG410XPZD; LUCA.
HOGENOM; HOG000240228; -.
HOVERGEN; HBG011375; -.
InParanoid; Q6RH31; -.
KO; K04505; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0016235; C:aggresome; ISS:UniProtKB.
GO; GO:0030424; C:axon; IBA:GO_Central.
GO; GO:0005938; C:cell cortex; IBA:GO_Central.
GO; GO:0009986; C:cell surface; IBA:GO_Central.
GO; GO:0035253; C:ciliary rootlet; IBA:GO_Central.
GO; GO:0043198; C:dendritic shaft; IBA:GO_Central.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0070765; C:gamma-secretase complex; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0030426; C:growth cone; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IBA:GO_Central.
GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:GOC.
GO; GO:0030018; C:Z disc; IBA:GO_Central.
GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; ISS:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
GO; GO:0042987; P:amyloid precursor protein catabolic process; IBA:GO_Central.
GO; GO:0042982; P:amyloid precursor protein metabolic process; ISS:UniProtKB.
GO; GO:0034205; P:amyloid-beta formation; ISS:UniProtKB.
GO; GO:0050435; P:amyloid-beta metabolic process; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
GO; GO:0007220; P:Notch receptor processing; IBA:GO_Central.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0016485; P:protein processing; ISS:UniProtKB.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0051563; P:smooth endoplasmic reticulum calcium ion homeostasis; IBA:GO_Central.
InterPro; IPR002031; Pept_A22A_PS1.
InterPro; IPR001108; Peptidase_A22A.
InterPro; IPR006639; Preselin/SPP.
PANTHER; PTHR10202; PTHR10202; 1.
Pfam; PF01080; Presenilin; 1.
PRINTS; PR01072; PRESENILIN.
PRINTS; PR01073; PRESENILIN1.
SMART; SM00730; PSN; 1.
2: Evidence at transcript level;
Alternative splicing; Apoptosis; Cell adhesion; Cell membrane;
Complete proteome; Endoplasmic reticulum; Golgi apparatus; Hydrolase;
Membrane; Notch signaling pathway; Phosphoprotein; Protease;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 297 Presenilin-1 NTF subunit. {ECO:0000250}.
/FTId=PRO_0000236052.
CHAIN 298 466 Presenilin-1 CTF subunit. {ECO:0000250}.
/FTId=PRO_0000236053.
CHAIN 345 466 Presenilin-1 CTF12. {ECO:0000250}.
/FTId=PRO_0000236054.
TOPO_DOM 1 81 Cytoplasmic.
{ECO:0000250|UniProtKB:P49768}.
TRANSMEM 82 102 Helical. {ECO:0000250|UniProtKB:P49768}.
TOPO_DOM 103 131 Lumenal. {ECO:0000250|UniProtKB:P49768}.
TRANSMEM 132 152 Helical. {ECO:0000250|UniProtKB:P49768}.
TOPO_DOM 153 165 Cytoplasmic.
{ECO:0000250|UniProtKB:P49768}.
TRANSMEM 166 188 Helical. {ECO:0000250|UniProtKB:P49768}.
TOPO_DOM 189 193 Lumenal. {ECO:0000250|UniProtKB:P49768}.
TRANSMEM 194 215 Helical. {ECO:0000250|UniProtKB:P49768}.
TOPO_DOM 216 219 Cytoplasmic.
{ECO:0000250|UniProtKB:P49768}.
TRANSMEM 220 240 Helical. {ECO:0000250|UniProtKB:P49768}.
TOPO_DOM 241 247 Lumenal. {ECO:0000250|UniProtKB:P49768}.
TRANSMEM 248 271 Helical. {ECO:0000250|UniProtKB:P49768}.
TOPO_DOM 272 379 Cytoplasmic.
{ECO:0000250|UniProtKB:P49768}.
TRANSMEM 380 400 Helical. {ECO:0000250|UniProtKB:P49768}.
TOPO_DOM 401 406 Lumenal. {ECO:0000250|UniProtKB:P49768}.
TRANSMEM 407 427 Helical. {ECO:0000250|UniProtKB:P49768}.
TOPO_DOM 428 431 Cytoplasmic.
{ECO:0000250|UniProtKB:P49768}.
TRANSMEM 432 452 Helical. {ECO:0000250|UniProtKB:P49768}.
TOPO_DOM 453 466 Lumenal. {ECO:0000250|UniProtKB:P49768}.
REGION 321 449 Required for interaction with CTNNB1.
{ECO:0000250|UniProtKB:P49768}.
REGION 371 398 Required for interaction with CTNND2.
{ECO:0000250|UniProtKB:P49768}.
REGION 463 466 Interaction with MTCH1.
{ECO:0000250|UniProtKB:P49768}.
MOTIF 432 434 PAL. {ECO:0000305}.
COMPBIAS 40 43 Poly-Arg.
COMPBIAS 93 96 Poly-Val.
ACT_SITE 256 256 {ECO:0000250|UniProtKB:P49768}.
ACT_SITE 384 384 {ECO:0000250|UniProtKB:P49768}.
SITE 290 291 Cleavage; alternate.
{ECO:0000250|UniProtKB:P49768}.
SITE 291 292 Cleavage; alternate.
{ECO:0000250|UniProtKB:P49768}.
SITE 297 298 Cleavage. {ECO:0000250|UniProtKB:P49768}.
SITE 344 345 Cleavage; by caspase.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:P97887}.
MOD_RES 309 309 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P49768}.
MOD_RES 328 328 Phosphothreonine.
{ECO:0000250|UniProtKB:P97887}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000250|UniProtKB:P97887}.
MOD_RES 345 345 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P49768}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000250|UniProtKB:P49769}.
VAR_SEQ 26 29 Missing (in isoform I-462).
{ECO:0000303|Ref.1}.
/FTId=VSP_018569.
SEQUENCE 466 AA; 52417 MW; BB78A213744E1F79 CRC64;
MTELPAPLSY FQNAQMSEDN HLSNTVRSQN DSREQHSSER RRRGNPEPLS NGRPQGSSHQ
VVEQDDEEDE ELTLKYGAKH VIMLFVPVTL CMVVVVATIK SVSFYTRKDG QLIYTPFTED
TETVGQRALH SILNAAIMIS VIVVMTILLV VLYKYRCYKV IHAWLIISSL LLLFLFSFIY
LGEVFKTYNV AMDYITVALL IWNFGVVGMI AIHWKGPLRL QQAYLIMISA LMALVFIKYL
PEWTAWLILA VISVYDLVAV LCPKGPLRML VETAQERNET LFPALIYSST MVWLVNMAEG
DPEAQRKVSK NSNYNAQSTE SETQDPVTES DDGGFSEEWE AQRDSRLGPH HSTTETRAAV
QELSSNILAS EDPEERGVKL GLGDFIFYSV LVGKASATAS GDWNTTIACF VAILIGLCLT
LLLLAIFKKA LPALPISITF GLVFYFATDY LVQPFMDQLA FHQFYI


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