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E9PUL5 (PRRT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proline-rich transmembrane protein 2
Alternative name(s):
Dispanin subfamily B member 3
Short name=DSPB3
Gene names
Name:Prrt2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Component of the outer core of AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing. Ref.3

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Cell junctionsynapse Probable Ref.3.

Tissue specificity

Expressed in the brain (at protein level). Also highly expressed in spinal cord. Detected at low levels in the heart, lung, kidney and skin. Ref.2 Ref.3

Developmental stage

Before 16 dpc, low levels in the developing brain. Expression markedly increases during early postnatal stages with a peak at P14. At this stage, expressed throughout the brain, with high levels in the cerebral cortex (cortical layers), hippocampus and cerebellum (granule cells and Purkinje cell layers). Progressively declines to relatively low levels in adulthood. Ref.2

Sequence similarities

Belongs to the CD225/Dispanin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346Proline-rich transmembrane protein 2
PRO_0000415735

Regions

Topological domain1 – 274274Extracellular Potential
Transmembrane275 – 29521Helical; Potential
Topological domain296 – 32328Cytoplasmic Potential
Transmembrane324 – 34421Helical; Potential
Topological domain345 – 3462Extracellular Potential
Compositional bias42 – 222181Pro-rich

Sequences

Sequence LengthMass (Da)Tools
E9PUL5 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: E7C3AF4159F4995F

FASTA34635,924
        10         20         30         40         50         60 
MAASSSQVSE MKGVEDSSKT QTEGPRHSEE GLGPVQVVAE IPDQPEALQP GPGITAAPVD 

        70         80         90        100        110        120 
SGPKAELAPE TTETPVETPE TVQATDLSLN PEEGSKASPS PSPSEARQEP ASKPDVNRET 

       130        140        150        160        170        180 
AAEEGSEPQS TAPPEPTSEP AFQINTQSDP QPTSQPPPKP PLQAEPPTQE DPTTEVLTES 

       190        200        210        220        230        240 
TGEKQENGAV VPLQAGDGEE GPAPQPHSPP STKTPPANGA PPRVLQKLVE EDRIGRAHGG 

       250        260        270        280        290        300 
HPGSPRGSLS RHPSSQLAGP GVEGGEGTQK PRDYIILAIL SCFCPMWPVN IVAFAYAVMS 

       310        320        330        340 
RNSLQQGDVD GAQRLGRVAK LLSIVALVGG VLIIIASCVI NLGVYK 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"Exome sequencing identifies truncating mutations in PRRT2 that cause paroxysmal kinesigenic dyskinesia."
Chen W.J., Lin Y., Xiong Z.Q., Wei W., Ni W., Tan G.H., Guo S.L., He J., Chen Y.F., Zhang Q.J., Li H.F., Lin Y., Murong S.X., Xu J., Wang N., Wu Z.Y.
Nat. Genet. 43:1252-1255(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[3]"High-resolution proteomics unravel architecture and molecular diversity of native AMPA receptor complexes."
Schwenk J., Harmel N., Brechet A., Zolles G., Berkefeld H., Muller C.S., Bildl W., Baehrens D., Huber B., Kulik A., Klocker N., Schulte U., Fakler B.
Neuron 74:621-633(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AMPAR COMPLEX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"The dispanins: a novel gene family of ancient origin that contains 14 human members."
Sallman Almen M., Bringeland N., Fredriksson R., Schioth H.B.
PLoS ONE 7:E31961-E31961(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC122863 Genomic DNA. No translation available.
CCDSCCDS52405.1.
RefSeqNP_001096033.1. NM_001102563.1.
UniGeneMm.392047.

3D structure databases

ProteinModelPortalE9PUL5.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

MaxQBE9PUL5.
PRIDEE9PUL5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000159916; ENSMUSP00000124520; ENSMUSG00000045114.
GeneID69017.
KEGGmmu:69017.
UCSCuc009jty.1. mouse.

Organism-specific databases

CTD112476.
MGIMGI:1916267. Prrt2.

Phylogenomic databases

GeneTreeENSGT00530000063980.
OMATQKPRDY.
OrthoDBEOG7NSB45.
PhylomeDBE9PUL5.
TreeFamTF331357.

Gene expression databases

BgeeE9PUL5.

Family and domain databases

InterProIPR007593. CD225/Dispanin_fam.
[Graphical view]
PfamPF04505. Dispanin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio328399.
PROE9PUL5.
SOURCESearch...

Entry information

Entry namePRRT2_MOUSE
AccessionPrimary (citable) accession number: E9PUL5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: April 5, 2011
Last modified: July 9, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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