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Protein

Proline-rich transmembrane protein 2

Gene

Prrt2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Proline-rich transmembrane protein 2
Alternative name(s):
Dispanin subfamily B member 3
Short name:
DSPB3
Gene namesi
Name:Prrt2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1916267. Prrt2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 274274ExtracellularSequence AnalysisAdd
BLAST
Transmembranei275 – 29521HelicalSequence AnalysisAdd
BLAST
Topological domaini296 – 32328CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei324 – 34421HelicalSequence AnalysisAdd
BLAST
Topological domaini345 – 3462ExtracellularSequence Analysis

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
  • synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 346346Proline-rich transmembrane protein 2PRO_0000415735Add
BLAST

Proteomic databases

MaxQBiE9PUL5.
PRIDEiE9PUL5.

Expressioni

Tissue specificityi

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

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiE9PUL5.

Interactioni

Subunit structurei

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.1 Publication

Structurei

3D structure databases

ProteinModelPortaliE9PUL5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi42 – 222181Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the CD225/Dispanin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000063980.
InParanoidiE9PUL5.
OMAiTQKPRDY.
OrthoDBiEOG7NSB45.
PhylomeDBiE9PUL5.
TreeFamiTF331357.

Family and domain databases

InterProiIPR007593. CD225/Dispanin_fam.
[Graphical view]
PfamiPF04505. Dispanin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E9PUL5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASSSQVSE MKGVEDSSKT QTEGPRHSEE GLGPVQVVAE IPDQPEALQP
60 70 80 90 100
GPGITAAPVD SGPKAELAPE TTETPVETPE TVQATDLSLN PEEGSKASPS
110 120 130 140 150
PSPSEARQEP ASKPDVNRET AAEEGSEPQS TAPPEPTSEP AFQINTQSDP
160 170 180 190 200
QPTSQPPPKP PLQAEPPTQE DPTTEVLTES TGEKQENGAV VPLQAGDGEE
210 220 230 240 250
GPAPQPHSPP STKTPPANGA PPRVLQKLVE EDRIGRAHGG HPGSPRGSLS
260 270 280 290 300
RHPSSQLAGP GVEGGEGTQK PRDYIILAIL SCFCPMWPVN IVAFAYAVMS
310 320 330 340
RNSLQQGDVD GAQRLGRVAK LLSIVALVGG VLIIIASCVI NLGVYK
Length:346
Mass (Da):35,924
Last modified:April 5, 2011 - v1
Checksum:iE7C3AF4159F4995F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC122863 Genomic DNA. No translation available.
CCDSiCCDS52405.1.
RefSeqiNP_001096033.1. NM_001102563.1.
UniGeneiMm.392047.

Genome annotation databases

EnsembliENSMUST00000159916; ENSMUSP00000124520; ENSMUSG00000045114.
GeneIDi69017.
KEGGimmu:69017.
UCSCiuc009jty.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC122863 Genomic DNA. No translation available.
CCDSiCCDS52405.1.
RefSeqiNP_001096033.1. NM_001102563.1.
UniGeneiMm.392047.

3D structure databases

ProteinModelPortaliE9PUL5.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

MaxQBiE9PUL5.
PRIDEiE9PUL5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000159916; ENSMUSP00000124520; ENSMUSG00000045114.
GeneIDi69017.
KEGGimmu:69017.
UCSCiuc009jty.1. mouse.

Organism-specific databases

CTDi112476.
MGIiMGI:1916267. Prrt2.

Phylogenomic databases

GeneTreeiENSGT00530000063980.
InParanoidiE9PUL5.
OMAiTQKPRDY.
OrthoDBiEOG7NSB45.
PhylomeDBiE9PUL5.
TreeFamiTF331357.

Miscellaneous databases

ChiTaRSiPrrt2. mouse.
NextBioi328399.
PROiE9PUL5.
SOURCEiSearch...

Gene expression databases

BgeeiE9PUL5.

Family and domain databases

InterProiIPR007593. CD225/Dispanin_fam.
[Graphical view]
PfamiPF04505. Dispanin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiPRRT2_MOUSE
AccessioniPrimary (citable) accession number: E9PUL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: April 5, 2011
Last modified: February 4, 2015
This is version 29 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.