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Neuritin (Candidate plasticity gene 15 protein)

 NRN1_MOUSE              Reviewed;         142 AA.
Q8CFV4; Q7TSR9;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
12-SEP-2018, entry version 95.
RecName: Full=Neuritin;
AltName: Full=Candidate plasticity gene 15 protein;
Flags: Precursor;
Name=Nrn1; Synonyms=Cpg15;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18, AND INDUCTION.
STRAIN=C57BL/6J;
PubMed=14664806; DOI=10.1016/S1044-7431(03)00230-6;
Fujino T., Lee W.-C.A., Nedivi E.;
"Regulation of cpg15 by signaling pathways that mediate synaptic
plasticity.";
Mol. Cell. Neurosci. 24:538-554(2003).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
IDENTIFICATION IN AMPAR COMPLEX, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=22632720; DOI=10.1016/j.neuron.2012.03.034;
Schwenk J., Harmel N., Brechet A., Zolles G., Berkefeld H.,
Muller C.S., Bildl W., Baehrens D., Huber B., Kulik A., Klocker N.,
Schulte U., Fakler B.;
"High-resolution proteomics unravel architecture and molecular
diversity of native AMPA receptor complexes.";
Neuron 74:621-633(2012).
-!- FUNCTION: Promotes neurite outgrowth and especially branching of
neuritic processes in primary hippocampal and cortical cells.
{ECO:0000250}.
-!- SUBUNIT: Component of the outer core of AMPAR complex. AMPAR
complex consists of an inner core made of 4 pore-forming GluA/GRIA
proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary
subunits arranged in a twofold symmetry. One of the two pairs of
distinct binding sites is occupied either by CNIH2, CNIH3 or
CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8
or GSG1L. This inner core of AMPAR complex is complemented by
outer core constituents binding directly to the GluA/GRIA proteins
at sites distinct from the interaction sites of the inner core
constituents. Outer core constituents include at least PRRT1,
PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner
and outer core serve as a platform for other, more peripherally
associated AMPAR constituents. Alone or in combination, these
auxiliary subunits control the gating and pharmacology of the
AMPAR complex and profoundly impact their biogenesis and protein
processing. {ECO:0000269|PubMed:22632720}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor,
GPI-anchor {ECO:0000305}. Cell junction, synapse
{ECO:0000305|PubMed:22632720}.
-!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
{ECO:0000269|PubMed:22632720}.
-!- INDUCTION: By synaptic activity through NMDA receptors and L-type
voltage-sensitive calcium channels. By cAMP in active neurons.
{ECO:0000269|PubMed:14664806}.
-!- SIMILARITY: Belongs to the neuritin family. {ECO:0000305}.
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EMBL; AK161859; BAE36610.1; -; mRNA.
EMBL; BC035531; AAH35531.1; -; mRNA.
EMBL; AY150584; AAN84528.1; -; Genomic_DNA.
CCDS; CCDS26455.1; -.
RefSeq; NP_705757.1; NM_153529.2.
UniGene; Mm.232930; -.
SMR; Q8CFV4; -.
IntAct; Q8CFV4; 1.
STRING; 10090.ENSMUSP00000040900; -.
iPTMnet; Q8CFV4; -.
PhosphoSitePlus; Q8CFV4; -.
SwissPalm; Q8CFV4; -.
MaxQB; Q8CFV4; -.
PaxDb; Q8CFV4; -.
PRIDE; Q8CFV4; -.
Ensembl; ENSMUST00000037623; ENSMUSP00000040900; ENSMUSG00000039114.
GeneID; 68404; -.
KEGG; mmu:68404; -.
UCSC; uc007qcm.3; mouse.
CTD; 51299; -.
MGI; MGI:1915654; Nrn1.
eggNOG; ENOG410IXWR; Eukaryota.
eggNOG; ENOG410YHS3; LUCA.
GeneTree; ENSGT00530000063853; -.
HOGENOM; HOG000059601; -.
HOVERGEN; HBG052772; -.
InParanoid; Q8CFV4; -.
OMA; FHSCATT; -.
PhylomeDB; Q8CFV4; -.
TreeFam; TF332589; -.
Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
PRO; PR:Q8CFV4; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000039114; Expressed in 199 organ(s), highest expression level in liver.
CleanEx; MM_NRN1; -.
ExpressionAtlas; Q8CFV4; baseline and differential.
Genevisible; Q8CFV4; MM.
GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
GO; GO:0046658; C:anchored component of plasma membrane; IDA:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
GO; GO:0007409; P:axonogenesis; ISO:MGI.
GO; GO:0007399; P:nervous system development; ISO:MGI.
GO; GO:1990138; P:neuron projection extension; IDA:MGI.
InterPro; IPR026144; Neuritin_fam.
PANTHER; PTHR15902; PTHR15902; 1.
Pfam; PF15056; NRN1; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Complete proteome; Glycoprotein;
GPI-anchor; Lipoprotein; Membrane; Reference proteome; Signal;
Synapse.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 116 Neuritin.
/FTId=PRO_0000262514.
PROPEP 117 142 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000262515.
LIPID 116 116 GPI-anchor amidated glycine.
{ECO:0000255}.
SEQUENCE 142 AA; 15353 MW; 6E5CCE2C9822C6E6 CRC64;
MGLKLNGRYI SLILAVQIAY LVQAVRAAGK CDAVFKGFSD CLLKLGDSMA NYPQGLDDKT
NIKTVCTYWE DFHSCTVTAL TDCQEGAKDM WDKLRKESKN LNIQGSLFEL CGSSNGAAGS
LLPALSVLLV SLSAALATWF SF


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