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Protein

Proline-rich transmembrane protein 2

Gene

Prrt2

Organism
Rattus norvegicus (Rat)
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1564195. Prrt2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 272272ExtracellularSequence analysisAdd
BLAST
Transmembranei273 – 29321HelicalSequence analysisAdd
BLAST
Topological domaini294 – 32128CytoplasmicSequence analysisAdd
BLAST
Transmembranei322 – 34221HelicalSequence analysisAdd
BLAST
Topological domaini343 – 3442ExtracellularSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344Proline-rich transmembrane protein 2PRO_0000420687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281PhosphoserineBy similarity
Modified residuei74 – 741PhosphothreonineCombined sources
Modified residuei78 – 781PhosphothreonineCombined sources
Modified residuei242 – 2421PhosphoserineCombined sources
Modified residuei252 – 2521PhosphoserineBy similarity
Modified residuei253 – 2531PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiD3ZFB6.
PRIDEiD3ZFB6.

PTM databases

iPTMnetiD3ZFB6.

Expressioni

Tissue specificityi

Expressed in the brain (at protein level).1 Publication

Gene expression databases

GenevisibleiD3ZFB6. RN.

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000050996.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi131 – 22090Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the CD225/Dispanin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J12U. Eukaryota.
ENOG410YRJ7. LUCA.
GeneTreeiENSGT00530000063980.
InParanoidiD3ZFB6.
OMAiTQKPRDY.
OrthoDBiEOG7NSB45.
PhylomeDBiD3ZFB6.
TreeFamiTF331357.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

D3ZFB6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASSSEVSE MKGVEDSSNT HSEGPRHSEE GMGPVQVVAE NLDQPEALQS
60 70 80 90 100
GPDTTAAPVD SGPKAELAPE TTETPVETPE TVQATDLSVN PGEDSKTCPS
110 120 130 140 150
PKEACQEPAS RPEVNREATA EQGAEQQSAA PPEPTSEQAL QLNTQSDPQP
160 170 180 190 200
TSQPPPKPPL QAEPPTQENP TTEVLTESTG EKQENGAVVP LQAGDGEEGP
210 220 230 240 250
APQPHSPPST KTPPANGAPP RVLQKLVEED RIGRAHGGHP GSPRGSLSRH
260 270 280 290 300
PSSQLAGPGV EGGEGTQKPR DYIILAILSC FCPMWPVNIV AFAYAVMSRN
310 320 330 340
SLQQGDVDGA QRLGRVAKLL SIVALVGGVL IIIASCVINL GVYK
Length:344
Mass (Da):35,821
Last modified:April 20, 2010 - v1
Checksum:i58B7852F54537C53
GO

Sequence databases

RefSeqiNP_001263399.1. NM_001276470.1.
UniGeneiRn.51543.

Genome annotation databases

EnsembliENSRNOT00000049044; ENSRNOP00000050996; ENSRNOG00000029366.
GeneIDi361651.
KEGGirno:361651.
UCSCiRGD:1564195. rat.

Cross-referencesi

Sequence databases

RefSeqiNP_001263399.1. NM_001276470.1.
UniGeneiRn.51543.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000050996.

PTM databases

iPTMnetiD3ZFB6.

Proteomic databases

PaxDbiD3ZFB6.
PRIDEiD3ZFB6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000049044; ENSRNOP00000050996; ENSRNOG00000029366.
GeneIDi361651.
KEGGirno:361651.
UCSCiRGD:1564195. rat.

Organism-specific databases

CTDi112476.
RGDi1564195. Prrt2.

Phylogenomic databases

eggNOGiENOG410J12U. Eukaryota.
ENOG410YRJ7. LUCA.
GeneTreeiENSGT00530000063980.
InParanoidiD3ZFB6.
OMAiTQKPRDY.
OrthoDBiEOG7NSB45.
PhylomeDBiD3ZFB6.
TreeFamiTF331357.

Miscellaneous databases

PROiD3ZFB6.

Gene expression databases

GenevisibleiD3ZFB6. RN.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; THR-78 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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.

Entry informationi

Entry nameiPRRT2_RAT
AccessioniPrimary (citable) accession number: D3ZFB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2013
Last sequence update: April 20, 2010
Last modified: June 8, 2016
This is version 44 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.