E9PUL5 (PRRT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proline-rich transmembrane protein 2

Alternative name(s):
Dispanin subfamily B member 3
Short name=DSPB3

Gene names

Name:

Prrt2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Protein existence	Evidence 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 junction › synapse 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.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane Synapse
Domain	Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to biotic stimulus Inferred from electronic annotation. Source: InterPro
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 346	346	Proline-rich transmembrane protein 2		PRO_0000415735
Regions
	Topological domain	1 – 274	274	Extracellular Potential
	Transmembrane	275 – 295	21	Helical; Potential
	Topological domain	296 – 323	28	Cytoplasmic Potential
	Transmembrane	324 – 344	21	Helical; Potential
	Topological domain	345 – 346	2	Extracellular Potential
	Compositional bias	42 – 222	181	Pro-rich

Sequences

	Sequence		Length	Mass (Da)
	E9PUL5 [UniParc]. Last modified April 5, 2011. Version 1. Checksum: E7C3AF4159F4995F	FASTA	346	35,924
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00281761.
RefSeq	NP_001096033.1. NM_001102563.1.
UniGene	Mm.392047.
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	E9PUL5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000159916; ENSMUSP00000124520; ENSMUSG00000045114.
GeneID	69017.
KEGG	mmu:69017.
Organism-specific databases
CTD	112476.
MGI	MGI:1916267. Prrt2.
Phylogenomic databases
GeneTree	ENSGT00530000063980.
OMA	TQKPRDY.
Gene expression databases
Bgee	E9PUL5.
Family and domain databases
InterPro	IPR007593. Interferon-induced_TM_protein. [Graphical view]
Pfam	PF04505. CD225. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	328399.
SOURCE	Search...

Entry information

Entry name

PRRT2_MOUSE

Accession

Primary (citable) accession number: E9PUL5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 22, 2012
Last sequence update:	April 5, 2011
Last modified:	May 1, 2013
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program