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Presenilin-2 (PS-2) (EC 3.4.23.-) [Cleaved into: Presenilin-2 NTF subunit; Presenilin-2 CTF subunit]

 PSN2_CHICK              Reviewed;         451 AA.
Q90X07;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 86.
RecName: Full=Presenilin-2;
Short=PS-2;
EC=3.4.23.-;
Contains:
RecName: Full=Presenilin-2 NTF subunit;
Contains:
RecName: Full=Presenilin-2 CTF subunit;
Name=PSEN2;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=B-cell;
PubMed=11987239; DOI=10.1006/bcmd.2002.0486;
Mirinics Z.K., Calafat J., Udby L., Lovelock J., Kjeldsen L.,
Rothermund K., Sisodia S.S., Borregaard N., Corey S.J.;
"Identification of the presenilins in hematopoietic cells with
localization of presenilin 1 to neutrophil and platelet granules.";
Blood Cells Mol. Dis. 28:28-38(2002).
-!- FUNCTION: Probable 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 other members
of the gamma-secretase complex to have a protease activity. May
play a role in intracellular signaling and gene expression or in
linking chromatin to the nuclear membrane. May function in the
cytoplasmic partitioning of proteins (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Homodimer. Component of the gamma-secretase complex, a
complex composed of a presenilin homodimer (PSEN1 or PSEN2),
nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2. Such minimal
complex is sufficient for secretase activity, although other
components may exist.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi
apparatus membrane {ECO:0000250}; Multi-pass membrane protein
{ECO:0000250}.
-!- DOMAIN: The PAL motif is required for normal active site
conformation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase A22A family. {ECO:0000305}.
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EMBL; AY043493; AAK95409.1; -; mRNA.
UniGene; Gga.2719; -.
STRING; 9031.ENSGALP00000032555; -.
MEROPS; A22.002; -.
PaxDb; Q90X07; -.
PRIDE; Q90X07; -.
eggNOG; KOG2736; Eukaryota.
eggNOG; ENOG410XPZD; LUCA.
HOGENOM; HOG000240228; -.
HOVERGEN; HBG011375; -.
InParanoid; Q90X07; -.
Proteomes; UP000000539; Unplaced.
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:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0030426; C:growth cone; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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:0030018; C:Z disc; IBA:GO_Central.
GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IEA:InterPro.
GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
GO; GO:0042987; P:amyloid precursor protein catabolic process; IBA:GO_Central.
GO; GO:0050435; P:amyloid-beta metabolic process; IBA:GO_Central.
GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IBA:GO_Central.
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:0016485; P:protein processing; IEA:InterPro.
InterPro; IPR001493; Pept_A22A_PS2.
InterPro; IPR001108; Peptidase_A22A.
InterPro; IPR006639; Preselin/SPP.
PANTHER; PTHR10202; PTHR10202; 2.
Pfam; PF01080; Presenilin; 1.
PRINTS; PR01072; PRESENILIN.
PRINTS; PR01074; PRESENILIN2.
SMART; SM00730; PSN; 1.
2: Evidence at transcript level;
Complete proteome; Endoplasmic reticulum; Golgi apparatus; Hydrolase;
Membrane; Notch signaling pathway; Protease; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 303 Presenilin-2 NTF subunit. {ECO:0000250}.
/FTId=PRO_0000236065.
CHAIN 304 451 Presenilin-2 CTF subunit. {ECO:0000250}.
/FTId=PRO_0000236066.
TOPO_DOM 1 93 Cytoplasmic. {ECO:0000255}.
TRANSMEM 94 114 Helical. {ECO:0000255}.
TOPO_DOM 115 144 Lumenal. {ECO:0000255}.
TRANSMEM 145 165 Helical. {ECO:0000255}.
TOPO_DOM 166 172 Cytoplasmic. {ECO:0000255}.
TRANSMEM 173 193 Helical. {ECO:0000255}.
TOPO_DOM 194 202 Lumenal. {ECO:0000255}.
TRANSMEM 203 223 Helical. {ECO:0000255}.
TOPO_DOM 224 229 Cytoplasmic. {ECO:0000255}.
TRANSMEM 230 250 Helical. {ECO:0000255}.
TOPO_DOM 251 255 Lumenal. {ECO:0000255}.
TRANSMEM 256 276 Helical. {ECO:0000255}.
TOPO_DOM 277 366 Cytoplasmic. {ECO:0000255}.
TRANSMEM 367 387 Helical. {ECO:0000255}.
TOPO_DOM 388 396 Lumenal. {ECO:0000255}.
TRANSMEM 397 417 Helical. {ECO:0000255}.
TOPO_DOM 418 421 Cytoplasmic. {ECO:0000255}.
INTRAMEM 422 442 Helical. {ECO:0000255}.
TOPO_DOM 443 451 Cytoplasmic. {ECO:0000255}.
MOTIF 422 424 PAL.
COMPBIAS 79 84 Poly-Glu.
COMPBIAS 359 365 Poly-Glu.
ACT_SITE 269 269 {ECO:0000250}.
ACT_SITE 374 374 {ECO:0000250}.
SEQUENCE 451 AA; 50500 MW; 534E6364C627E8B0 CRC64;
MITFMNNSDS EDEPCNERTS LMSAESPPVP SYQDGLQASE TREAQTHRKR QTGSSRSPNN
VADEDASDSD VRVRESALEN EEEELTLKYG AKHVIMLFVP VTLCMIVVVA TIKSVRFYTE
KNGQLIYTPF SEDTPSVGQR LLNSVLNTII MISVIVVMTV FLVVLYKYRC YKFIHGWLIL
SSFMLLFLFT YIYLGEVLKT YNVAMDYPTV ILIIWNFGAV GMIRIHWKGP LQLQQAYLIM
ISALMVLVFI KYLPEWSAWV ILGAISIYDL IAVLCPKGPL RMLXETAQER NQPIFPALIY
SSAMIWTVGM AKPDTAAKGQ SQQAWDAEDE RENHSSTSHS DSQILDTRSP APSHPITLEE
MEEEERGVKL GLGDFIFYSV LVGKAAATPS GDWNTTLAXX VAILIGLCLT LLLLAVFKKA
LPALPISITF GLIFYFSTDN LVRTDPLEIS V


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