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Q9CQR7 (PEN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Gamma-secretase subunit PEN-2
Alternative name(s):
Presenilin enhancer protein 2
Gene names
Name:Psenen
Synonyms:Pen2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length101 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Essential 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). Probably represents the last step of maturation of gamma-secretase, facilitating endoproteolysis of presenilin and conferring gamma-secretase activity By similarity.

Subunit structure

Component of the gamma-secretase complex, a complex composed of a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PSENEN/PEN2. Such minimal complex is sufficient for secretase activity, although other components may exist By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Golgi apparatus › cis-Golgi network membrane; Multi-pass membrane protein By similarity. Note: Predominantly located in the endoplasmic reticulum and in the cis-Golgi By similarity.

Sequence similarities

Belongs to the PEN-2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 101101Gamma-secretase subunit PEN-2
PRO_0000190901

Regions

Topological domain1 – 1717Lumenal Potential
Transmembrane18 – 3821Helical; Potential
Topological domain39 – 6022Cytoplasmic Potential
Transmembrane61 – 8121Helical; Potential
Topological domain82 – 10120Lumenal Potential

Sequences

Sequence LengthMass (Da)Tools
Q9CQR7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 6596CA2984FBCC59

FASTA10111,999
        10         20         30         40         50         60 
MNLERVSNEE KLNLCRKYYL GGFAFLPFLW LVNIFWFFRE AFLAPAYTEQ SQIKGYVWRS 

        70         80         90        100 
AVGFLFWVII LATWITIFQI YRPRWGALGD YLSFTIPLGT P

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney, Pancreas and Testis.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain and Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK002440 mRNA. Translation: BAB22102.1.
AK006284 mRNA. Translation: BAB24503.1.
AK007621 mRNA. Translation: BAB25141.1.
BC024347 mRNA. Translation: AAH24347.1.
BC081443 mRNA. Translation: AAH81443.1.
IPIIPI00132969.
RefSeqNP_079774.1. NM_025498.2.
UniGeneMm.86557.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP-36333N.
IntActQ9CQR7. 2 interactions.
STRING10090.ENSMUSP00000044682.

PTM databases

PhosphoSiteQ9CQR7.

Proteomic databases

PaxDbQ9CQR7.
PRIDEQ9CQR7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000043898; ENSMUSP00000044682; ENSMUSG00000036835.
GeneID66340.
KEGGmmu:66340.
UCSCuc009gez.1. mouse.

Organism-specific databases

CTD55851.
MGIMGI:1913590. Psenen.

Phylogenomic databases

eggNOGNOG279333.
GeneTreeENSGT00390000016319.
HOGENOMHOG000006914.
HOVERGENHBG045628.
InParanoidQ9CQR7.
KOK06170.
OMAWGATADY.
OrthoDBEOG483D63.

Enzyme and pathway databases

ReactomeREACT_115202. Signal Transduction.
REACT_99130. A third proteolytic cleavage releases NICD.

Gene expression databases

BgeeQ9CQR7.
CleanExMM_PSENEN.
GenevestigatorQ9CQR7.
GermOnlineENSMUSG00000036835. Mus musculus.
ENSMUSG00000056412. Mus musculus.

Family and domain databases

InterProIPR019379. Gamma_Secretase_Asp_P_PEN2.
[Graphical view]
PfamPF10251. PEN-2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ9CQR7.
ChEMBLCHEMBL4539.
NextBio321375.
SOURCESearch...

Entry information

Entry namePEN2_MOUSE
AccessionPrimary (citable) accession number: Q9CQR7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 2001
Last modified: May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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