Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Proline-rich transmembrane protein 2

Gene

Prrt2

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

Functioni

As a component of the outer core of AMPAR complex, may be involved in synaptic transmission in the central nervous system. In hippocampal neurons, in presynaptic terminals, plays an important role in the final steps of neurotransmitter release, possibly by regulating Ca2+-sensing (PubMed:27052163). In the cerebellum, may inhibit SNARE complex formation and downregulate short-term facilitation (PubMed:29056747).2 Publications

GO - Molecular functioni

  • SH3 domain binding Source: MGI
  • syntaxin-1 binding Source: UniProtKB

GO - Biological processi

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1916267 Prrt2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 274CytoplasmicSequence analysis1 PublicationAdd BLAST274
Intramembranei275 – 295HelicalSequence analysis1 PublicationAdd BLAST21
Topological domaini296 – 323CytoplasmicSequence analysis1 PublicationAdd BLAST28
Transmembranei324 – 344HelicalSequence analysis1 PublicationAdd BLAST21
Topological domaini345 – 346ExtracellularSequence analysis1 Publication2

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

Mutant mice are normal at birth, but display paroxysmal movements at the onset of locomotion that persist in the adulthood. Adult animals present abnormal motor behaviors characterized by wild running and jumping in response to audiogenic stimuli that are ineffective in wild-type mice and an increased sensitivity to the convulsive effects of pentylentetrazol. Although the overall brain structure is not affected by the knockout, the thickness of the neocortex in young adult is significantly reduced in medial and caudal regions compared to their wild-type littermates. No significant differences are observed in the thickness of the CA1, CA3 and DG regions of the hippocampus, as well as for the molecular and granule layers of the cerebellum (PubMed:28007585). Mice with a conditional knockout in the central nervous system develop normally, but showed poor performance in motor coordination functions (PubMed:29056747).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004157351 – 346Proline-rich transmembrane protein 2Add BLAST346

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei28PhosphoserineCombined sources1
Modified residuei74PhosphothreonineCombined sources1
Modified residuei78PhosphothreonineCombined sources1
Modified residuei98PhosphoserineCombined sources1
Modified residuei102PhosphoserineCombined sources1
Modified residuei244PhosphoserineBy similarity1
Modified residuei246Omega-N-methylarginineCombined sources1
Modified residuei254PhosphoserineCombined sources1
Modified residuei255PhosphoserineCombined sources1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiE9PUL5
PaxDbiE9PUL5
PeptideAtlasiE9PUL5
PRIDEiE9PUL5

PTM databases

iPTMnetiE9PUL5
PhosphoSitePlusiE9PUL5
SwissPalmiE9PUL5

Expressioni

Tissue specificityi

Neuron-specific expression throughout the brain, with the highest levels in the cerebellum, basal ganglia, hippocampus, substantia nigra, and neocortex (at protein level) (PubMed:22101681, PubMed:22243967, PubMed:22832103, PubMed:22632720, PubMed:25915028, PubMed:27052163, PubMed:27172900, PubMed:28007585, PubMed:29056747). Highly expressed also in spinal cord (at protein level) (PubMed:22101681, PubMed:22832103). Detected at very low levels in the heart, lung, kidney and skin (PubMed:22101681).9 Publications

Developmental stagei

At the mRNA level, expressed at low levels in the developing brain before 16 dpc. 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. At the protein level, first detected at very low levels at 17.5 dpc. Expression increases at early postnatal stages in the cerebral cortex, hippocampus and cerebellum. Expression increases to reach a plateau around P14, a period of intense synapse formation and rearrangement, and starts to slightly decrease around P90 (at protein level) (PubMed:27052163, PubMed:29056747).3 Publications

Gene expression databases

BgeeiENSMUSG00000045114 Expressed in 27 organ(s), highest expression level in bone marrow
ExpressionAtlasiE9PUL5 baseline and differential
GenevisibleiE9PUL5 MM

Interactioni

Subunit structurei

Component of the outer core of AMPAR complex (PubMed:22632720, PubMed:25915028). 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 (PubMed:22632720). Interacts with intersectin 1/ITSN1 (PubMed:26797119). Interacts with SNARE complex components, including SNAP25, STX1A, SYT1 and SYT2; this interaction may inhibit SNARE complex formation (PubMed:22832103, PubMed:27052163, PubMed:29056747).6 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000124520

Structurei

3D structure databases

ProteinModelPortaliE9PUL5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi42 – 222Pro-richAdd BLAST181

Sequence similaritiesi

Belongs to the CD225/Dispanin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J12U Eukaryota
ENOG410YRJ7 LUCA
GeneTreeiENSGT00530000063980
InParanoidiE9PUL5
OMAiVEEDRMG
OrthoDBiEOG091G0JH3
PhylomeDBiE9PUL5
TreeFamiTF331357

Family and domain databases

InterProiView protein in InterPro
IPR007593 CD225/Dispanin_fam
PfamiView protein in Pfam
PF04505 CD225, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0J9YU72A0A0J9YU72_MOUSE
Proline-rich transmembrane protein ...
Prrt2
61Annotation score:
A0A0J9YV24A0A0J9YV24_MOUSE
Proline-rich transmembrane protein ...
Prrt2
61Annotation score:
A0A0J9YTS8A0A0J9YTS8_MOUSE
Proline-rich transmembrane protein ...
Prrt2
55Annotation score:

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

Similar proteinsi

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...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000124520

PTM databases

iPTMnetiE9PUL5
PhosphoSitePlusiE9PUL5
SwissPalmiE9PUL5

Proteomic databases

MaxQBiE9PUL5
PaxDbiE9PUL5
PeptideAtlasiE9PUL5
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

eggNOGiENOG410J12U Eukaryota
ENOG410YRJ7 LUCA
GeneTreeiENSGT00530000063980
InParanoidiE9PUL5
OMAiVEEDRMG
OrthoDBiEOG091G0JH3
PhylomeDBiE9PUL5
TreeFamiTF331357

Miscellaneous databases

ChiTaRSiPrrt2 mouse
PROiPR:E9PUL5
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000045114 Expressed in 27 organ(s), highest expression level in bone marrow
ExpressionAtlasiE9PUL5 baseline and differential
GenevisibleiE9PUL5 MM

Family and domain databases

InterProiView protein in InterPro
IPR007593 CD225/Dispanin_fam
PfamiView protein in Pfam
PF04505 CD225, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPRRT2_MOUSE
AccessioniPrimary (citable) accession number: E9PUL5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: April 5, 2011
Last modified: November 7, 2018
This is version 50 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again