PRR7_RAT
ID PRR7_RAT Reviewed; 269 AA.
AC P0C6T3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Proline-rich protein 7;
DE AltName: Full=Synaptic proline-rich membrane protein;
GN Name=Prr7;
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 PROTEIN SEQUENCE OF 174-182; 189-203 AND 234-265, IDENTIFICATION IN A
RP POSTSYNAPTIC MEMBRANE COMPLEX WITH DLG4 AND GRIN1, INTERACTION WITH DLG4,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=15629447; DOI=10.1016/j.bbrc.2004.11.154;
RA Murata Y., Doi T., Taniguchi H., Fujiyoshi Y.;
RT "Proteomic analysis revealed a novel synaptic proline-rich membrane protein
RT (PRR7) associated with PSD-95 and NMDA receptor.";
RL Biochem. Biophys. Res. Commun. 327:183-191(2005).
RN [3]
RP FUNCTION, IDENTIFICATION IN COMPLEX WITH DLG4 AND GRIN1, IDENTIFICATION IN
RP A COMPLEX WITH GRIN1 AND GRIN2B, INTERACTION WITH DLG4; GRIN1; GRIN2B AND
RP FBXW7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF 39-LYS--ARG-47.
RX PubMed=27458189; DOI=10.15252/embj.201593070;
RA Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S.,
RA Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.;
RT "Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and regulates
RT NMDA-mediated excitotoxicity.";
RL EMBO J. 35:1923-1934(2016).
CC -!- FUNCTION: Acts as a synapse-to-nucleus messenger to promote NMDA
CC receptor-mediated excitotoxicity in neurons in a JUN-dependent manner
CC (PubMed:27458189). Inhibits ubiquitination-mediated degradation and
CC promotes phosphorylation and transcriptional activity of transcription
CC factor JUN (PubMed:27458189). Might play a redundant role in the
CC regulation of T cell receptor signaling (By similarity). Might promote
CC apoptosis in T cells (By similarity). {ECO:0000250|UniProtKB:Q8TB68,
CC ECO:0000269|PubMed:27458189}.
CC -!- SUBUNIT: Forms a complex with NMDA receptor zeta subunit GRIN1 and
CC epsilon subunit GRIN2B (PubMed:27458189). Interacts with GRIN2B
CC (PubMed:27458189). Interacts with GRIN1; the interaction is reduced
CC upon NMDA receptor activity (PubMed:27458189). Found in a postsynaptic
CC membrane complex with DLG4 and GRIN1 (PubMed:15629447,
CC PubMed:27458189). Interacts with DLG4 (via PDZ3 domain and to lesser
CC degree via PDZ2 domain) (PubMed:15629447, PubMed:27458189). Interacts
CC with FBXW7 (PubMed:27458189). Found in a complex with JUN and FBXW7 (By
CC similarity). Interacts with JUN and FBXW7; the interaction inhibits
CC ubiquitination-mediated JUN degradation promoting its phosphorylation
CC and transcriptional activity (By similarity). Interacts with SRC (By
CC similarity). {ECO:0000250|UniProtKB:Q8TB68,
CC ECO:0000269|PubMed:15629447, ECO:0000269|PubMed:27458189}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8TB68};
CC Single-pass type III membrane protein {ECO:0000305}. Postsynaptic cell
CC membrane {ECO:0000269|PubMed:15629447}; Single-pass type III membrane
CC protein {ECO:0000305}. Postsynaptic density membrane
CC {ECO:0000269|PubMed:15629447, ECO:0000269|PubMed:27458189}. Cytoplasm,
CC perinuclear region {ECO:0000250|UniProtKB:Q8TB68}. Synapse
CC {ECO:0000269|PubMed:27458189}. Cell projection, dendrite
CC {ECO:0000269|PubMed:27458189}. Nucleus {ECO:0000269|PubMed:27458189}.
CC Note=Enriched in postsynaptic plasma membrane and postsynaptic
CC densities (PSD) (PubMed:15629447, PubMed:27458189). Accumulates in
CC spines along with synapse maturation and colocalizes with DLG4 in a
CC punctate pattern (PubMed:15629447). Translocates from synapses to
CC nuclei following NMDA receptor activity (PubMed:27458189).
CC {ECO:0000269|PubMed:15629447, ECO:0000269|PubMed:27458189}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (PubMed:15629447,
CC PubMed:27458189). Expressed in the cerebral cortex and especially in
CC hippocampal neural cells (at protein level) (PubMed:15629447,
CC PubMed:27458189). {ECO:0000269|PubMed:15629447,
CC ECO:0000269|PubMed:27458189}.
CC -!- DEVELOPMENTAL STAGE: Expression detected at postnatal day 7 and
CC expression increases until 4 weeks after birth.
CC {ECO:0000269|PubMed:27458189}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q8TB68}.
CC -!- PTM: Tyrosine phosphorylated, possibly by SRC.
CC {ECO:0000250|UniProtKB:Q8TB68}.
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DR EMBL; AABR03104952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001102586.1; NM_001109116.1.
DR RefSeq; XP_006253714.1; XM_006253652.3.
DR RefSeq; XP_017456132.1; XM_017600643.1.
DR AlphaFoldDB; P0C6T3; -.
DR BioGRID; 270014; 2.
DR CORUM; P0C6T3; -.
DR STRING; 10116.ENSRNOP00000038274; -.
DR PaxDb; P0C6T3; -.
DR PRIDE; P0C6T3; -.
DR Ensembl; ENSRNOT00000036162; ENSRNOP00000038274; ENSRNOG00000021447.
DR GeneID; 498704; -.
DR KEGG; rno:498704; -.
DR UCSC; RGD:1561898; rat.
DR CTD; 80758; -.
DR RGD; 1561898; Prr7.
DR eggNOG; ENOG502RA5T; Eukaryota.
DR GeneTree; ENSGT00950000183109; -.
DR HOGENOM; CLU_081607_0_0_1; -.
DR InParanoid; P0C6T3; -.
DR OMA; FCSYLRR; -.
DR OrthoDB; 1388391at2759; -.
DR PhylomeDB; P0C6T3; -.
DR TreeFam; TF332076; -.
DR PRO; PR:P0C6T3; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000021447; Expressed in frontal cortex and 17 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0036041; F:long-chain fatty acid binding; ISS:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:RGD.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; ISO:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
DR GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IDA:SynGO.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Cell projection; Cytoplasm;
KW Direct protein sequencing; Immunity; Lipoprotein; Membrane; Nucleus;
KW Palmitate; Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
KW Signal-anchor; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Proline-rich protein 7"
FT /id="PRO_0000328651"
FT TOPO_DOM 1..9
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..44
FT /note="Required for interaction with NMDA receptors"
FT /evidence="ECO:0000269|PubMed:27458189"
FT REGION 2..39
FT /note="Required for membrane localization"
FT /evidence="ECO:0000250|UniProtKB:Q8TB68"
FT REGION 64..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..269
FT /note="Required for apoptosis induction"
FT /evidence="ECO:0000250|UniProtKB:Q8TB68"
FT REGION 146..166
FT /note="Required for internalization"
FT /evidence="ECO:0000250|UniProtKB:Q8TB68"
FT MOTIF 267..269
FT /note="PDZ-binding"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V0I2"
FT MUTAGEN 39..47
FT /note="KRRQEERLR->AAAQEEALA: Loss of nuclear localization
FT and loss of apoptosis induction."
FT /evidence="ECO:0000269|PubMed:27458189"
SQ SEQUENCE 269 AA; 30377 MW; 7C55B86C72508F5E CRC64;
MVMSQGTYTF LTCFAGFWLI WGLIVLLCCF CSFLRRRLKR RQEERLREQN LRALELEPLE
LEGSLAGSPP GLAPPPPPHR SRLEAPVHAH SHVHVHPLLH HGPAQPHAHP HPHHHALPHP
PPSHLSVPPR PWSYPRQAES DMSKPPCYEE AVLMAEPPPP YSEVLTDTRG LYRKIVTPFL
SRRDSAEKQE QPPPSYKPLF LDRGYTSALH LPSAPRPAAP CPALCLQADR SRRVFPSWTD
SELSSREPLE HGAWRLPVSI PLFGRTTAV
