PRRT1_MOUSE
ID PRRT1_MOUSE Reviewed; 306 AA.
AC O35449;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Proline-rich transmembrane protein 1;
DE AltName: Full=Dispanin subfamily D member 1;
DE Short=DSPD1;
DE AltName: Full=Synapse differentiation-induced protein 4 {ECO:0000303|PubMed:29490264};
DE Short=SynDIG4 {ECO:0000303|PubMed:29490264};
GN Name=Prrt1 {ECO:0000312|MGI:MGI:1932118};
GN Synonyms=Ng5 {ECO:0000250|UniProtKB:Q6MG82};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 GENE FAMILY.
RX PubMed=22363774; DOI=10.1371/journal.pone.0031961;
RA Sallman Almen M., Bringeland N., Fredriksson R., Schioth H.B.;
RT "The dispanins: a novel gene family of ancient origin that contains 14
RT human members.";
RL PLoS ONE 7:E31961-E31961(2012).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=29490264; DOI=10.1016/j.celrep.2018.02.026;
RA Matt L., Kirk L.M., Chenaux G., Speca D.J., Puhger K.R., Pride M.C.,
RA Qneibi M., Haham T., Plambeck K.E., Stern-Bach Y., Silverman J.L.,
RA Crawley J.N., Hell J.W., Diaz E.;
RT "SynDIG4/Prrt1 Is Required for Excitatory Synapse Development and
RT Plasticity Underlying Cognitive Function.";
RL Cell Rep. 22:2246-2253(2018).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31216424; DOI=10.1016/j.mcn.2019.06.008;
RA Troyano-Rodriguez E., Mann S., Ullah R., Ahmad M.;
RT "PRRT1 regulates basal and plasticity-induced AMPA receptor trafficking.";
RL Mol. Cell. Neurosci. 98:155-163(2019).
CC -!- FUNCTION: Required to maintain a pool of extrasynaptic AMPA-regulated
CC glutamate receptors (AMPAR) which is necessary for synapse development
CC and function (PubMed:29490264). Regulates AMPAR function and synaptic
CC transmission during development but is dispensable at mature
CC hippocampal synapses (PubMed:29490264, PubMed:31216424). Plays a role
CC in regulating basal phosphorylation levels of glutamate receptor GRIA1
CC and promotes GRIA1 and GRIA2 cell surface expression (PubMed:31216424).
CC {ECO:0000269|PubMed:29490264, ECO:0000269|PubMed:31216424}.
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 {ECO:0000269|PubMed:22632720}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:22632720};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6MG82}.
CC Synapse {ECO:0000305|PubMed:22632720}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level)
CC (PubMed:22632720). In brain, expressed throughout the hippocampus with
CC weak expression in the olfactory bulb and neocortex (at protein level)
CC (PubMed:29490264). {ECO:0000269|PubMed:22632720,
CC ECO:0000269|PubMed:29490264}.
CC -!- DISRUPTION PHENOTYPE: Decreased Gria1/GluA1 and Gria2/GluA2 density at
CC extrasynaptic sites and increased density of Gria1 at synapses
CC (PubMed:29490264). Reduced cell surface expression of Gria1 and Gria2
CC (PubMed:31216424). Reduced phosphorylation of Gria1 'Ser-863' and
CC increased phosphorylation of Gria1 'Ser-849' (PubMed:31216424). Reduced
CC synaptic transmission in immature hippocampal neurons
CC (PubMed:29490264). No change in basal synaptic transmission in mature
CC hippocampal neurons (PubMed:31216424). Shown to impair tetanus-induced
CC long-term potentiation (LTP) in 8-12 week old mice in one study
CC (PubMed:29490264). Another study shows no effect on LTP in young mature
CC mice at postnatal days 24-36 (PubMed:31216424). Severely impaired long-
CC term depression (PubMed:31216424). Deficiency in cognitive learning and
CC memory tasks (PubMed:29490264). {ECO:0000269|PubMed:29490264,
CC ECO:0000269|PubMed:31216424}.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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DR EMBL; AF030001; AAB82012.1; -; Genomic_DNA.
DR CCDS; CCDS28653.1; -.
DR PIR; T09067; T09067.
DR RefSeq; NP_112152.1; NM_030890.1.
DR AlphaFoldDB; O35449; -.
DR BioGRID; 234424; 2.
DR IntAct; O35449; 1.
DR STRING; 10090.ENSMUSP00000015620; -.
DR TCDB; 8.A.58.2.14; the dispanin (dispanin) family.
DR iPTMnet; O35449; -.
DR PhosphoSitePlus; O35449; -.
DR SwissPalm; O35449; -.
DR PaxDb; O35449; -.
DR PRIDE; O35449; -.
DR ProteomicsDB; 291568; -.
DR ABCD; O35449; 1 sequenced antibody.
DR Antibodypedia; 61533; 90 antibodies from 18 providers.
DR Ensembl; ENSMUST00000015620; ENSMUSP00000015620; ENSMUSG00000015476.
DR GeneID; 260297; -.
DR KEGG; mmu:260297; -.
DR UCSC; uc008cdf.1; mouse.
DR CTD; 80863; -.
DR MGI; MGI:1932118; Prrt1.
DR VEuPathDB; HostDB:ENSMUSG00000015476; -.
DR eggNOG; ENOG502QWCK; Eukaryota.
DR GeneTree; ENSGT00940000162382; -.
DR HOGENOM; CLU_096299_0_0_1; -.
DR InParanoid; O35449; -.
DR OMA; CHLSPYP; -.
DR OrthoDB; 1273993at2759; -.
DR PhylomeDB; O35449; -.
DR TreeFam; TF331357; -.
DR BioGRID-ORCS; 260297; 1 hit in 71 CRISPR screens.
DR PRO; PR:O35449; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O35449; protein.
DR Bgee; ENSMUSG00000015476; Expressed in primary visual cortex and 113 other tissues.
DR ExpressionAtlas; O35449; baseline and differential.
DR Genevisible; O35449; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030545; F:signaling receptor regulator activity; IDA:MGI.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0060292; P:long-term synaptic depression; IMP:UniProtKB.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IDA:MGI.
DR GO; GO:0050808; P:synapse organization; IMP:MGI.
DR InterPro; IPR007593; CD225/Dispanin_fam.
DR Pfam; PF04505; CD225; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Signal-anchor; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..306
FT /note="Proline-rich transmembrane protein 1"
FT /id="PRO_0000135698"
FT TOPO_DOM 1..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q6MG82"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..275
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q6MG82"
FT INTRAMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..306
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q6MG82"
FT REGION 1..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 306 AA; 31389 MW; D8875395737F3E6B CRC64;
MSSEKSGLPD SVPHTSPPPY NAPQPPAEPP IPPPQTAPSS HHHHHHHYHQ SGTATLPRLG
AGGLASAAAS AQRGPSSSAT LPRPPHHAPP GPAAGAPPPG CATLPRMPPD PYLQETRFEG
PLPPPPPAAA APPPPAPAPT AQAPGFVVPT HAGAVGTLPL GGYVAPGYPL QLQPCTAYVP
VYPVGTPYAG GTPGGPGVTS TLPPPPQGPG LALLEPRRPP HDYMPIAVLT TICCFWPTGI
IAIFKAVQVR TALARGDLVS AEIASREARN FSFISLAVGI AAMVLCTILT VVIIIAAQHH
ENYWDP
