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Protein

Presenilin-2

Gene

Psen2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (beta-amyloid 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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei263By similarity1
Active sitei366By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Keywords - Biological processi

Notch signaling pathway

Enzyme and pathway databases

ReactomeiR-RNO-1251985. Nuclear signaling by ERBB4.
R-RNO-193692. Regulated proteolysis of p75NTR.
R-RNO-1980148. Signaling by NOTCH3.
R-RNO-1980150. Signaling by NOTCH4.
R-RNO-205043. NRIF signals cell death from the nucleus.
R-RNO-3928665. EPH-ephrin mediated repulsion of cells.

Protein family/group databases

MEROPSiA22.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Presenilin-2 (EC:3.4.23.-)
Short name:
PS-2
Cleaved into the following 2 chains:
Gene namesi
Name:Psen2
Synonyms:Ps2, Psnl2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi621060. Psen2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 87CytoplasmicSequence analysisAdd BLAST87
Transmembranei88 – 106HelicalSequence analysisAdd BLAST19
Topological domaini107 – 138LumenalSequence analysisAdd BLAST32
Transmembranei139 – 159HelicalSequence analysisAdd BLAST21
Topological domaini160 – 166CytoplasmicSequence analysis7
Transmembranei167 – 187HelicalSequence analysisAdd BLAST21
Topological domaini188 – 200LumenalSequence analysisAdd BLAST13
Transmembranei201 – 221HelicalSequence analysisAdd BLAST21
Topological domaini222 – 223CytoplasmicSequence analysis2
Transmembranei224 – 244HelicalSequence analysisAdd BLAST21
Topological domaini245 – 249LumenalSequence analysis5
Transmembranei250 – 270HelicalSequence analysisAdd BLAST21
Topological domaini271 – 358CytoplasmicSequence analysisAdd BLAST88
Transmembranei359 – 379HelicalSequence analysisAdd BLAST21
Topological domaini380 – 388LumenalSequence analysis9
Transmembranei389 – 409HelicalSequence analysisAdd BLAST21
Topological domaini410 – 413CytoplasmicSequence analysis4
Intramembranei414 – 434HelicalSequence analysisAdd BLAST21
Topological domaini435 – 448CytoplasmicSequence analysisAdd BLAST14

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000256091 – 297Presenilin-2 NTF subunitBy similarityAdd BLAST297
ChainiPRO_0000025610298 – 448Presenilin-2 CTF subunitBy similarityAdd BLAST151

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei22PhosphoserineBy similarity1
Modified residuei25PhosphoserineBy similarity1
Modified residuei30PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated on serine residues.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO88777.
PRIDEiO88777.

PTM databases

iPTMnetiO88777.
PhosphoSitePlusiO88777.

Expressioni

Gene expression databases

BgeeiENSRNOG00000002879.
GenevisibleiO88777. RN.

Interactioni

Subunit structurei

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. Interacts with DOCK3. Interacts with HERPUD1, FLNA and FLNB (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000049605.

Structurei

3D structure databases

ProteinModelPortaliO88777.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi414 – 416PAL3

Domaini

The PAL motif is required for normal active site conformation.By similarity

Sequence similaritiesi

Belongs to the peptidase A22A family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2736. Eukaryota.
ENOG410XPZD. LUCA.
GeneTreeiENSGT00390000016593.
HOGENOMiHOG000240228.
HOVERGENiHBG011375.
InParanoidiO88777.
KOiK04522.
OMAiIEQHEEG.
OrthoDBiEOG091G0C72.
PhylomeDBiO88777.
TreeFamiTF315040.

Family and domain databases

InterProiIPR001493. Pept_A22A_PS2.
IPR001108. Peptidase_A22A.
IPR006639. Preselin/SPP.
[Graphical view]
PANTHERiPTHR10202. PTHR10202. 1 hit.
PTHR10202:SF20. PTHR10202:SF20. 1 hit.
PfamiPF01080. Presenilin. 2 hits.
[Graphical view]
PRINTSiPR01072. PRESENILIN.
PR01074. PRESENILIN2.
SMARTiSM00730. PSN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O88777-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTFMASDSE EEVCDERTSL MSAESPTSRS CQDSRPGPED GENTAQWRSQ
60 70 80 90 100
ENEDDCEEDP DHYACSGVPG RPSGLEEELT LKYGAKHVIM LFVPVTLCMI
110 120 130 140 150
VVVATIKSVR FYTEKNGQLI YTPFTEDTPS VGQRLLNSVL NTLIMISVIV
160 170 180 190 200
VMTIFLVVLY KYRCYKFIHG WLIMSSLMLL FLFTYIYLGE VFKTYNVAMD
210 220 230 240 250
YPTLFLAVWN FGAVGMVCIH WKGPLVLQQA YLIVISALMA LVFIKYLPEW
260 270 280 290 300
SAWVILGAIS VYDLVAVLCP KGPLRMLVET AQERNEPIFP ALIYSSAMVW
310 320 330 340 350
TVGMAKLDPS SQGALQLPYD PEMEEDSYDS FGEPSYPEAF EAPQPGYPGE
360 370 380 390 400
EPEEEEERGV KLGLGDFIFY SVLVGKAAAT GNGDWSTTLA CFIAILIGLC
410 420 430 440
LTLLLLAVFK KALPALPISI TFGLIFYFST DNLVRPFMDT LASHQLYI
Length:448
Mass (Da):50,051
Last modified:July 15, 1999 - v2
Checksum:i299A7C416405046C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti7S → T in CAA67663 (Ref. 1) Curated1
Sequence conflicti86 – 87KH → ND in BAA20406 (PubMed:9545577).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99267 mRNA. Translation: CAA67663.1.
D83700 mRNA. Translation: BAA22832.1.
AB004454 mRNA. Translation: BAA20406.1.
BC078805 mRNA. Translation: AAH78805.1.
RefSeqiNP_112349.2. NM_031087.2.
XP_006250467.1. XM_006250405.3.
XP_006250469.1. XM_006250407.3.
XP_006250470.1. XM_006250408.3.
XP_008768099.1. XM_008769877.2.
XP_017454428.1. XM_017598939.1.
UniGeneiRn.11045.

Genome annotation databases

EnsembliENSRNOT00000040203; ENSRNOP00000049605; ENSRNOG00000002879.
ENSRNOT00000091715; ENSRNOP00000070964; ENSRNOG00000002879.
GeneIDi81751.
KEGGirno:81751.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99267 mRNA. Translation: CAA67663.1.
D83700 mRNA. Translation: BAA22832.1.
AB004454 mRNA. Translation: BAA20406.1.
BC078805 mRNA. Translation: AAH78805.1.
RefSeqiNP_112349.2. NM_031087.2.
XP_006250467.1. XM_006250405.3.
XP_006250469.1. XM_006250407.3.
XP_006250470.1. XM_006250408.3.
XP_008768099.1. XM_008769877.2.
XP_017454428.1. XM_017598939.1.
UniGeneiRn.11045.

3D structure databases

ProteinModelPortaliO88777.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000049605.

Protein family/group databases

MEROPSiA22.002.

PTM databases

iPTMnetiO88777.
PhosphoSitePlusiO88777.

Proteomic databases

PaxDbiO88777.
PRIDEiO88777.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000040203; ENSRNOP00000049605; ENSRNOG00000002879.
ENSRNOT00000091715; ENSRNOP00000070964; ENSRNOG00000002879.
GeneIDi81751.
KEGGirno:81751.

Organism-specific databases

CTDi5664.
RGDi621060. Psen2.

Phylogenomic databases

eggNOGiKOG2736. Eukaryota.
ENOG410XPZD. LUCA.
GeneTreeiENSGT00390000016593.
HOGENOMiHOG000240228.
HOVERGENiHBG011375.
InParanoidiO88777.
KOiK04522.
OMAiIEQHEEG.
OrthoDBiEOG091G0C72.
PhylomeDBiO88777.
TreeFamiTF315040.

Enzyme and pathway databases

ReactomeiR-RNO-1251985. Nuclear signaling by ERBB4.
R-RNO-193692. Regulated proteolysis of p75NTR.
R-RNO-1980148. Signaling by NOTCH3.
R-RNO-1980150. Signaling by NOTCH4.
R-RNO-205043. NRIF signals cell death from the nucleus.
R-RNO-3928665. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

PROiO88777.

Gene expression databases

BgeeiENSRNOG00000002879.
GenevisibleiO88777. RN.

Family and domain databases

InterProiIPR001493. Pept_A22A_PS2.
IPR001108. Peptidase_A22A.
IPR006639. Preselin/SPP.
[Graphical view]
PANTHERiPTHR10202. PTHR10202. 1 hit.
PTHR10202:SF20. PTHR10202:SF20. 1 hit.
PfamiPF01080. Presenilin. 2 hits.
[Graphical view]
PRINTSiPR01072. PRESENILIN.
PR01074. PRESENILIN2.
SMARTiSM00730. PSN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPSN2_RAT
AccessioniPrimary (citable) accession number: O88777
Secondary accession number(s): O08947, O35546
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: November 30, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.