PRRT1_RAT
ID PRRT1_RAT Reviewed; 306 AA.
AC Q6MG82;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
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:26660156};
DE Short=SynDIG4 {ECO:0000303|PubMed:26660156};
GN Name=Prrt1 {ECO:0000312|RGD:1359348};
GN Synonyms=Ng5 {ECO:0000312|EMBL:CAE83964.1};
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] {ECO:0000312|EMBL:CAE83964.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:CAE83964.1};
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [2]
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 [3]
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 [4]
RP TOPOLOGY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=26660156; DOI=10.1002/cne.23945;
RA Kirk L.M., Ti S.W., Bishop H.I., Orozco-Llamas M., Pham M., Trimmer J.S.,
RA Diaz E.;
RT "Distribution of the SynDIG4/proline-rich transmembrane protein 1 in rat
RT brain.";
RL J. Comp. Neurol. 524:2266-2280(2016).
CC -!- FUNCTION: Required to maintain a pool of extrasynaptic AMPA-regulated
CC glutamate receptors (AMPAR) which is necessary for synapse development
CC and function. Regulates basal AMPAR function and synaptic transmission
CC during development but is dispensable at mature hippocampal synapses.
CC Plays a role in regulating basal phosphorylation levels of glutamate
CC receptor GRIA1 and promotes GRIA1 and GRIA2 cell surface expression.
CC {ECO:0000250|UniProtKB:O35449}.
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:0000269|PubMed:26660156,
CC ECO:0000305|PubMed:22632720}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:26660156}. Synapse {ECO:0000305|PubMed:22632720}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level)
CC (PubMed:22632720, PubMed:26660156). In brain, expressed in the
CC neocortex and enriched in the hippocampus but only modestly expressed
CC in the cerebellum (PubMed:26660156). Expressed throughout the
CC hippocampus but is most highly expressed in the CA1 region and the
CC stratum lacunosum-moleculare of the CA2 region (PubMed:26660156).
CC {ECO:0000269|PubMed:22632720, ECO:0000269|PubMed:26660156}.
CC -!- DEVELOPMENTAL STAGE: Expression is low at postnatal day 0, increases at
CC postnatal day 7, peaks at postnatal days 14 and 21 and decreases at 2
CC months of age. {ECO:0000269|PubMed:26660156}.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE83964.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX883044; CAE83964.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001027456.1; NM_001032285.1.
DR AlphaFoldDB; Q6MG82; -.
DR BioGRID; 268233; 1.
DR CORUM; Q6MG82; -.
DR IntAct; Q6MG82; 1.
DR MINT; Q6MG82; -.
DR STRING; 10116.ENSRNOP00000000495; -.
DR PhosphoSitePlus; Q6MG82; -.
DR SwissPalm; Q6MG82; -.
DR PaxDb; Q6MG82; -.
DR PRIDE; Q6MG82; -.
DR ABCD; Q6MG82; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000000495; ENSRNOP00000000495; ENSRNOG00000000433.
DR GeneID; 406167; -.
DR KEGG; rno:406167; -.
DR UCSC; RGD:1359348; rat.
DR CTD; 80863; -.
DR RGD; 1359348; Prrt1.
DR eggNOG; ENOG502QWCK; Eukaryota.
DR GeneTree; ENSGT00940000162382; -.
DR HOGENOM; CLU_096299_0_0_1; -.
DR InParanoid; Q6MG82; -.
DR OMA; CHLSPYP; -.
DR OrthoDB; 1273993at2759; -.
DR PhylomeDB; Q6MG82; -.
DR TreeFam; TF331357; -.
DR PRO; PR:Q6MG82; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000433; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q6MG82; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:RGD.
DR GO; GO:0030545; F:signaling receptor regulator activity; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0060292; P:long-term synaptic depression; ISS:UniProtKB.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:UniProtKB.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
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_0000299077"
FT TOPO_DOM 1..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26660156"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..275
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:26660156"
FT INTRAMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..306
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:26660156"
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; 4A5C2A23A33E2116 CRC64;
MSSEKSGLPD SVPHTSPPPY NAPQPPAEPP IPPPQTAPSS HHHHHHHYHQ SGTATLPRLG
AGGLASAAAG AQRGPSSSAT LPRPPHHAPP GPAAGAPPPG CATLPRMPPD PYLQETRFEG
PLPPPPPAAA APPPPAPAPT AQAPGFVVPT HAGAVGTLPL GGYVAPGYPL QLQPCTAYVP
VYPVGTPYAS GTPGGPGVTS TLPPPPQGPG LALLEPRRPP HDYMPIAVLT TICCFWPTGI
IAIFKAVQVR TALARGDLVS AEIASREARN FSFISLAVGI AAMVLCTILT VVIIIAAQHH
ENYWDP
