PRRT2_RAT
ID PRRT2_RAT Reviewed; 344 AA.
AC D3ZFB6;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Proline-rich transmembrane protein 2;
DE AltName: Full=Dispanin subfamily B member 3;
DE Short=DSPB3;
GN Name=Prrt2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; THR-78 AND SER-242, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP IDENTIFICATION IN AMPAR COMPLEX, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22632720; DOI=10.1016/j.neuron.2012.03.034;
RA Schwenk J., Harmel N., Brechet A., Zolles G., Berkefeld H., Muller C.S.,
RA Bildl W., Baehrens D., Huber B., Kulik A., Klocker N., Schulte U.,
RA Fakler B.;
RT "High-resolution proteomics unravel architecture and molecular diversity of
RT native AMPA receptor complexes.";
RL Neuron 74:621-633(2012).
RN [4]
RP INTERACTION WITH ITSN1.
RX PubMed=26797119; DOI=10.1074/jbc.m115.683888;
RA Rossi P., Sterlini B., Castroflorio E., Marte A., Onofri F., Valtorta F.,
RA Maragliano L., Corradi A., Benfenati F.;
RT "A Novel Topology of Proline-rich Transmembrane Protein 2 (PRRT2): hints
RT for an intracellular function at the synapse.";
RL J. Biol. Chem. 291:6111-6123(2016).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27172900; DOI=10.18632/oncotarget.9258;
RA Liu Y.T., Nian F.S., Chou W.J., Tai C.Y., Kwan S.Y., Chen C., Kuo P.W.,
RA Lin P.H., Chen C.Y., Huang C.W., Lee Y.C., Soong B.W., Tsai J.W.;
RT "PRRT2 mutations lead to neuronal dysfunction and neurodevelopmental
RT defects.";
RL Oncotarget 7:39184-39196(2016).
CC -!- FUNCTION: As a component of the outer core of AMPAR complex, may be
CC involved in synaptic transmission in the central nervous system. In
CC hippocampal neurons, in presynaptic terminals, plays an important role
CC in the final steps of neurotransmitter release, possibly by regulating
CC Ca(2+)-sensing. In the cerebellum, may inhibit SNARE complex formation
CC and down-regulate short-term facilitation.
CC {ECO:0000250|UniProtKB:E9PUL5}.
CC -!- SUBUNIT: Component of the outer core of AMPAR complex. AMPAR complex
CC consists of an inner core made of 4 pore-forming GluA/GRIA proteins
CC (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged
CC in a twofold symmetry. One of the two pairs of distinct binding sites
CC is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors
CC CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR
CC complex is complemented by outer core constituents binding directly to
CC the GluA/GRIA proteins at sites distinct from the interaction sites of
CC the inner core constituents. Outer core constituents include at least
CC PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the
CC inner and outer core serve as a platform for other, more peripherally
CC associated AMPAR constituents. Alone or in combination, these auxiliary
CC subunits control the gating and pharmacology of the AMPAR complex and
CC profoundly impact their biogenesis and protein processing
CC (PubMed:22632720). Interacts with intersectin 1/ITSN1
CC (PubMed:26797119). Interacts with SNARE complex components, including
CC SNAP25, STX1A, SYT1 and SYT2; this interaction may inhibit SNARE
CC complex formation (By similarity). {ECO:0000250|UniProtKB:Q7Z6L0,
CC ECO:0000269|PubMed:22632720, ECO:0000269|PubMed:26797119}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27172900};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:E9PUL5}.
CC Presynaptic cell membrane {ECO:0000250|UniProtKB:E9PUL5}; Single-pass
CC membrane protein {ECO:0000250|UniProtKB:E9PUL5}. Synapse
CC {ECO:0000250|UniProtKB:E9PUL5}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q7Z6L0}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000269|PubMed:27172900}. Postsynaptic
CC density membrane {ECO:0000269|PubMed:27172900}. Cell projection,
CC dendritic spine {ECO:0000269|PubMed:27172900}.
CC -!- TISSUE SPECIFICITY: Neuron-specific expression throughout the brain,
CC including hippocampus (at protein level). {ECO:0000269|PubMed:22632720,
CC ECO:0000269|PubMed:27172900}.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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DR RefSeq; NP_001263399.1; NM_001276470.1.
DR AlphaFoldDB; D3ZFB6; -.
DR CORUM; D3ZFB6; -.
DR STRING; 10116.ENSRNOP00000050996; -.
DR iPTMnet; D3ZFB6; -.
DR PhosphoSitePlus; D3ZFB6; -.
DR PaxDb; D3ZFB6; -.
DR PRIDE; D3ZFB6; -.
DR Ensembl; ENSRNOT00000049044; ENSRNOP00000050996; ENSRNOG00000029366.
DR GeneID; 361651; -.
DR KEGG; rno:361651; -.
DR UCSC; RGD:1564195; rat.
DR CTD; 112476; -.
DR RGD; 1564195; Prrt2.
DR eggNOG; ENOG502S2U1; Eukaryota.
DR GeneTree; ENSGT00940000161103; -.
DR HOGENOM; CLU_070349_0_0_1; -.
DR InParanoid; D3ZFB6; -.
DR OMA; DPQPDCQ; -.
DR OrthoDB; 1101977at2759; -.
DR PhylomeDB; D3ZFB6; -.
DR TreeFam; TF331357; -.
DR PRO; PR:D3ZFB6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000029366; Expressed in cerebellum and 17 other tissues.
DR Genevisible; D3ZFB6; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IDA:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; ISS:UniProtKB.
DR GO; GO:0099502; P:calcium-dependent activation of synaptic vesicle fusion; ISO:RGD.
DR GO; GO:1905513; P:negative regulation of short-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0035544; P:negative regulation of SNARE complex assembly; ISS:UniProtKB.
DR GO; GO:0050884; P:neuromuscular process controlling posture; ISO:RGD.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; ISS:UniProtKB.
DR InterPro; IPR007593; CD225/Dispanin_fam.
DR Pfam; PF04505; CD225; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasmic vesicle; Membrane; Methylation;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..344
FT /note="Proline-rich transmembrane protein 2"
FT /id="PRO_0000420687"
FT TOPO_DOM 1..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT INTRAMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT TOPO_DOM 294..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT TOPO_DOM 343..344
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT REGION 1..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 244
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
SQ SEQUENCE 344 AA; 35821 MW; 58B7852F54537C53 CRC64;
MAASSSEVSE MKGVEDSSNT HSEGPRHSEE GMGPVQVVAE NLDQPEALQS GPDTTAAPVD
SGPKAELAPE TTETPVETPE TVQATDLSVN PGEDSKTCPS PKEACQEPAS RPEVNREATA
EQGAEQQSAA PPEPTSEQAL QLNTQSDPQP TSQPPPKPPL QAEPPTQENP TTEVLTESTG
EKQENGAVVP LQAGDGEEGP APQPHSPPST KTPPANGAPP RVLQKLVEED RIGRAHGGHP
GSPRGSLSRH PSSQLAGPGV EGGEGTQKPR DYIILAILSC FCPMWPVNIV AFAYAVMSRN
SLQQGDVDGA QRLGRVAKLL SIVALVGGVL IIIASCVINL GVYK
