NRN1_MOUSE
ID NRN1_MOUSE Reviewed; 142 AA.
AC Q8CFV4; Q7TSR9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Neuritin;
DE AltName: Full=Candidate plasticity gene 15 protein;
DE Flags: Precursor;
GN Name=Nrn1; Synonyms=Cpg15;
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=Medulla oblongata;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18, AND INDUCTION.
RC STRAIN=C57BL/6J;
RX PubMed=14664806; DOI=10.1016/s1044-7431(03)00230-6;
RA Fujino T., Lee W.-C.A., Nedivi E.;
RT "Regulation of cpg15 by signaling pathways that mediate synaptic
RT plasticity.";
RL Mol. Cell. Neurosci. 24:538-554(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
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 [6]
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).
CC -!- FUNCTION: Promotes neurite outgrowth and especially branching of
CC neuritic processes in primary hippocampal and cortical cells.
CC {ECO:0000250}.
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}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}. Synapse {ECO:0000305|PubMed:22632720}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
CC {ECO:0000269|PubMed:22632720}.
CC -!- INDUCTION: By synaptic activity through NMDA receptors and L-type
CC voltage-sensitive calcium channels. By cAMP in active neurons.
CC {ECO:0000269|PubMed:14664806}.
CC -!- SIMILARITY: Belongs to the neuritin family. {ECO:0000305}.
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DR EMBL; AK161859; BAE36610.1; -; mRNA.
DR EMBL; BC035531; AAH35531.1; -; mRNA.
DR EMBL; AY150584; AAN84528.1; -; Genomic_DNA.
DR CCDS; CCDS26455.1; -.
DR RefSeq; NP_705757.1; NM_153529.2.
DR AlphaFoldDB; Q8CFV4; -.
DR IntAct; Q8CFV4; 2.
DR MINT; Q8CFV4; -.
DR STRING; 10090.ENSMUSP00000040900; -.
DR iPTMnet; Q8CFV4; -.
DR PhosphoSitePlus; Q8CFV4; -.
DR SwissPalm; Q8CFV4; -.
DR MaxQB; Q8CFV4; -.
DR PaxDb; Q8CFV4; -.
DR PRIDE; Q8CFV4; -.
DR ProteomicsDB; 293738; -.
DR Antibodypedia; 24561; 195 antibodies from 31 providers.
DR DNASU; 68404; -.
DR Ensembl; ENSMUST00000037623; ENSMUSP00000040900; ENSMUSG00000039114.
DR GeneID; 68404; -.
DR KEGG; mmu:68404; -.
DR UCSC; uc007qcm.3; mouse.
DR CTD; 51299; -.
DR MGI; MGI:1915654; Nrn1.
DR VEuPathDB; HostDB:ENSMUSG00000039114; -.
DR eggNOG; ENOG502RZNR; Eukaryota.
DR GeneTree; ENSGT00530000063853; -.
DR HOGENOM; CLU_135101_0_0_1; -.
DR InParanoid; Q8CFV4; -.
DR OMA; KCDAVFR; -.
DR PhylomeDB; Q8CFV4; -.
DR TreeFam; TF332589; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 68404; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Nrn1; mouse.
DR PRO; PR:Q8CFV4; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8CFV4; protein.
DR Bgee; ENSMUSG00000039114; Expressed in habenula and 178 other tissues.
DR ExpressionAtlas; Q8CFV4; baseline and differential.
DR Genevisible; Q8CFV4; MM.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0007409; P:axonogenesis; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:1990138; P:neuron projection extension; IDA:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR InterPro; IPR026144; Neuritin_fam.
DR PANTHER; PTHR15902; PTHR15902; 1.
DR Pfam; PF15056; NRN1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Signal; Synapse.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..116
FT /note="Neuritin"
FT /id="PRO_0000262514"
FT PROPEP 117..142
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000262515"
FT LIPID 116
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 142 AA; 15353 MW; 6E5CCE2C9822C6E6 CRC64;
MGLKLNGRYI SLILAVQIAY LVQAVRAAGK CDAVFKGFSD CLLKLGDSMA NYPQGLDDKT
NIKTVCTYWE DFHSCTVTAL TDCQEGAKDM WDKLRKESKN LNIQGSLFEL CGSSNGAAGS
LLPALSVLLV SLSAALATWF SF
