PRR7_MOUSE
ID PRR7_MOUSE Reviewed; 269 AA.
AC Q3V0I2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Proline-rich protein 7;
DE AltName: Full=Synaptic proline-rich membrane protein;
GN Name=Prr7;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP 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 INTERACTION WITH JUN.
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).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27657535; DOI=10.1371/journal.pone.0162863;
RA Hrdinka M., Sudan K., Just S., Drobek A., Stepanek O., Schlueter D.,
RA Reinhold D., Jordan B.A., Gintschel P., Schraven B., Kreutz M.R.;
RT "Normal development and function of T cells in Proline rich 7 (Prr7)
RT deficient mice.";
RL PLoS ONE 11:E0162863-E0162863(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 (By similarity). Inhibits ubiquitination-mediated degradation and
CC promotes phosphorylation and transcriptional activity of transcription
CC factor JUN (By similarity). Might play a redundant role in the
CC regulation of T cell receptor signaling (PubMed:27657535). Might
CC promote apoptosis in T cells (By similarity).
CC {ECO:0000250|UniProtKB:P0C6T3, ECO:0000250|UniProtKB:Q8TB68,
CC ECO:0000269|PubMed:27657535}.
CC -!- SUBUNIT: Forms a complex with NMDA receptor zeta subunit GRIN1 and
CC epsilon subunit GRIN2B (By similarity). Interacts with GRIN2B (By
CC similarity). Interacts with GRIN1; the interaction is reduced upon NMDA
CC receptor activity (By similarity). Found in a postsynaptic membrane
CC complex with DLG4 and GRIN1 (By similarity). Interacts with DLG4 (via
CC PDZ3 domain and to lesser degree via PDZ2 domain) (By similarity).
CC Interacts with JUN (PubMed:27458189). Found in a complex with JUN and
CC FBXW7 (By similarity). Interacts with JUN and FBXW7; the interaction
CC inhibits ubiquitination-mediated JUN degradation promoting its
CC phosphorylation and transcriptional activity (By similarity). Interacts
CC with SRC (By similarity). {ECO:0000250|UniProtKB:P0C6T3,
CC ECO:0000250|UniProtKB:Q8TB68, 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:0000250|UniProtKB:P0C6T3}; Single-pass type III membrane
CC protein {ECO:0000305}. Postsynaptic density membrane
CC {ECO:0000250|UniProtKB:P0C6T3}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8TB68}. Synapse {ECO:0000250|UniProtKB:P0C6T3}.
CC Cell projection, dendrite {ECO:0000250|UniProtKB:P0C6T3}. Nucleus
CC {ECO:0000250|UniProtKB:P0C6T3}. Note=Enriched in postsynaptic plasma
CC membrane and postsynaptic densities (PSD). Accumulates in spines along
CC with synapse maturation and colocalizes with DLG4 in a punctate
CC pattern. Translocates from synapses to nuclei following NMDA receptor
CC activity (By similarity). {ECO:0000250|UniProtKB:P0C6T3}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, moderately expressed in
CC lymph nodes and T cells and low expression in thymus and spleen.
CC Expressed in single positive progenitor thymocytes, particularly in CD8
CC single positive thymocytes. {ECO:0000269|PubMed:27657535}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q8TB68}.
CC -!- PTM: Tyrosine phosphorylated, possibly by SRC.
CC {ECO:0000250|UniProtKB:Q8TB68}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are viable and
CC fertile. T-cell and B-cell development are normal. T cell receptor
CC signaling and activation induced cell death appear normal. Small
CC reduction of CD4 single positive thymocytes.
CC {ECO:0000269|PubMed:27657535}.
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DR EMBL; AK133129; BAE21522.1; -; mRNA.
DR CCDS; CCDS26546.1; -.
DR RefSeq; NP_001025467.1; NM_001030296.4.
DR RefSeq; XP_017171029.1; XM_017315540.1.
DR AlphaFoldDB; Q3V0I2; -.
DR BioGRID; 240804; 3.
DR IntAct; Q3V0I2; 1.
DR MINT; Q3V0I2; -.
DR STRING; 10090.ENSMUSP00000046776; -.
DR iPTMnet; Q3V0I2; -.
DR PhosphoSitePlus; Q3V0I2; -.
DR MaxQB; Q3V0I2; -.
DR PaxDb; Q3V0I2; -.
DR PRIDE; Q3V0I2; -.
DR ProteomicsDB; 291748; -.
DR Antibodypedia; 29296; 144 antibodies from 22 providers.
DR Ensembl; ENSMUST00000046533; ENSMUSP00000046776; ENSMUSG00000034686.
DR GeneID; 432763; -.
DR KEGG; mmu:432763; -.
DR UCSC; uc007qrb.2; mouse.
DR CTD; 80758; -.
DR MGI; MGI:3487246; Prr7.
DR VEuPathDB; HostDB:ENSMUSG00000034686; -.
DR eggNOG; ENOG502RA5T; Eukaryota.
DR GeneTree; ENSGT00950000183109; -.
DR HOGENOM; CLU_081607_0_0_1; -.
DR InParanoid; Q3V0I2; -.
DR OMA; FCSYLRR; -.
DR OrthoDB; 1388391at2759; -.
DR PhylomeDB; Q3V0I2; -.
DR TreeFam; TF332076; -.
DR BioGRID-ORCS; 432763; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q3V0I2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3V0I2; protein.
DR Bgee; ENSMUSG00000034686; Expressed in striatum and 53 other tissues.
DR ExpressionAtlas; Q3V0I2; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0036041; F:long-chain fatty acid binding; ISS:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; IMP:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Cell projection; Cytoplasm; Immunity;
KW Lipoprotein; Membrane; Nucleus; Palmitate; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Signal-anchor; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Proline-rich protein 7"
FT /id="PRO_0000328650"
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:0000250|UniProtKB:Q8TB68"
FT REGION 2..39
FT /note="Required for membrane localization"
FT /evidence="ECO:0000250|UniProtKB:Q8TB68"
FT REGION 63..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..121
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 /evidence="ECO:0000255"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 269 AA; 30354 MW; CBEDCF9596CC40B8 CRC64;
MVMSQGTYTF LTCFAGFWLI WGLIVLLCCF CSFLRRRLKR RQEERLREQN LRALELEPLE
LEGSLAGSPP GLAPPPPPHR SRLEAPVHAH SHVHVHPLLH HGPAPPHAHP HPHHHALPHP
PPPHLAVPPR PWSYPRQAES DMSKPPCYEE AVLMAEPPPP YSEVLTDTRG LYRKIVTPFL
SRRDSAEKQE QPPPSYKPLF LDRGYTSALH LPSAPRPAAP CPALCLQAER SRRVFPSWTD
SELSSREPLE HGAWRLPVSI PLFGRTTAV
