NRN1_RAT
ID NRN1_RAT Reviewed; 142 AA.
AC O08957;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Neuritin;
DE Flags: Precursor;
GN Name=Nrn1;
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 [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Hippocampus;
RX PubMed=9122250; DOI=10.1073/pnas.94.6.2648;
RA Naeve G.S., Ramakrishnan M., Kramer R., Hevroni D., Citri Y., Theill L.E.;
RT "Neuritin: a gene induced by neural activity and neurotrophins that
RT promotes neuritogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2648-2653(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PROTEIN SEQUENCE OF 37-59, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
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:0000269|PubMed:9122250}.
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 predominantly in brain (at protein
CC level). Highest expression in the dentate gyrus and lowest expression
CC in the striatum. Concentrated on neuronal cell bodies and unevenly
CC dispersed along neuritic projections in the nonmyelinated regions of
CC the brain. Expressed in postmitotic-differentiating neurons of the
CC developmental nervous system and neuronal structures associated with
CC plasticity in the adult. {ECO:0000269|PubMed:22632720,
CC ECO:0000269|PubMed:9122250}.
CC -!- DEVELOPMENTAL STAGE: Expression first detected in developing brain at
CC embryonic day 15; the level of expression increases throughout
CC embryonic development and postnatally into adulthood.
CC {ECO:0000269|PubMed:9122250}.
CC -!- INDUCTION: Induced by neural activity and by the activity-regulated
CC neurotrophins BDNF and NTF3. {ECO:0000269|PubMed:9122250}.
CC -!- SIMILARITY: Belongs to the neuritin family. {ECO:0000305}.
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DR EMBL; U88958; AAB53415.1; -; mRNA.
DR EMBL; BC087582; AAH87582.1; -; mRNA.
DR PIR; JC6305; JC6305.
DR RefSeq; NP_445798.1; NM_053346.1.
DR AlphaFoldDB; O08957; -.
DR CORUM; O08957; -.
DR STRING; 10116.ENSRNOP00000066878; -.
DR jPOST; O08957; -.
DR PaxDb; O08957; -.
DR PRIDE; O08957; -.
DR Ensembl; ENSRNOT00000116839; ENSRNOP00000082569; ENSRNOG00000050767.
DR GeneID; 83834; -.
DR KEGG; rno:83834; -.
DR CTD; 51299; -.
DR RGD; 621586; Nrn1.
DR eggNOG; ENOG502RZNR; Eukaryota.
DR GeneTree; ENSGT00530000063853; -.
DR InParanoid; O08957; -.
DR OrthoDB; 1469106at2759; -.
DR PhylomeDB; O08957; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:O08957; -.
DR Proteomes; UP000002494; Chromosome 17.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; ISO:RGD.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IDA:RGD.
DR GO; GO:1990138; P:neuron projection extension; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR InterPro; IPR026144; Neuritin_fam.
DR PANTHER; PTHR15902; PTHR15902; 1.
DR Pfam; PF15056; NRN1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Signal; Synapse.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..116
FT /note="Neuritin"
FT /id="PRO_0000262516"
FT PROPEP 117..142
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000262517"
FT LIPID 116
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 142 AA; 15289 MW; 6E5CC0CC8D6392E6 CRC64;
MGLKLNGRYI SLILAVQIAY LVQAVRAAGK CDAVFKGFSD CLLKLGDSMA NYPQGLDDKT
NIKTVCTYWE DFHSCTVTAL TDCQEGAKDM WDKLRKESKN LNIQGSLFEL CGSGNGAAGS
LLPALSVLLV SLSAALATWL SF
