NGRN_MOUSE
ID NGRN_MOUSE Reviewed; 293 AA.
AC Q99KS2; Q8C401; Q99PU9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Neugrin;
DE AltName: Full=FI58Gm;
DE AltName: Full=Neurite outgrowth-associated protein;
DE Short=m-Neugrin;
DE Flags: Precursor;
GN Name=Ngrn; Synonyms=Fi58g;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=11118320; DOI=10.1006/bbrc.2000.3971;
RA Ishigaki S., Niwa J., Yoshihara T., Mitsuma N., Doyu M., Sobue G.;
RT "Two novel genes, human neugrin and mouse m-neugrin, are upregulated with
RT neuronal differentiation in neuroblastoma cells.";
RL Biochem. Biophys. Res. Commun. 279:526-533(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Lung, Placenta, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: Plays an essential role in mitochondrial ribosome biogenesis.
CC As a component of a functional protein-RNA module, consisting of RCC1L,
CC NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal
CC RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and is required for
CC intra-mitochondrial translation of core subunits of the oxidative
CC phosphorylation system. {ECO:0000250|UniProtKB:Q9NPE2}.
CC -!- SUBUNIT: Forms a regulatory protein-RNA complex, consisting of RCC1L,
CC NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA. Interacts with
CC 16S mt-rRNA; this interaction is direct.
CC {ECO:0000250|UniProtKB:Q9NPE2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NPE2}. Secreted
CC {ECO:0000250|UniProtKB:Q9NPE2}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q9NPE2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99KS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99KS2-2; Sequence=VSP_039712, VSP_039713;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, liver and kidney. In
CC brain, mainly expressed in neurons rather than glial cells.
CC {ECO:0000269|PubMed:11118320}.
CC -!- DEVELOPMENTAL STAGE: Level of expression increases with embryonal
CC development. {ECO:0000269|PubMed:11118320}.
CC -!- INDUCTION: Highly up-regulated in neuroblastostoma cells by RA and
CC MG132 treatment inducing neurite outgrowth.
CC {ECO:0000269|PubMed:11118320}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the neugrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04034.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB21528.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB21528.1; Type=Miscellaneous discrepancy; Note=The N-terminus contains a duplicated region of sequence.; Evidence={ECO:0000305};
CC Sequence=BAC38868.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAE26050.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE26868.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB047544; BAB21528.1; ALT_SEQ; mRNA.
DR EMBL; AK083330; BAC38868.1; ALT_SEQ; mRNA.
DR EMBL; AK144756; BAE26050.1; ALT_INIT; mRNA.
DR EMBL; AK146059; BAE26868.1; ALT_SEQ; mRNA.
DR EMBL; AC109232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004034; AAH04034.1; ALT_INIT; mRNA.
DR CCDS; CCDS21393.2; -. [Q99KS2-1]
DR PIR; JC7564; JC7564.
DR RefSeq; NP_113552.3; NM_031375.4. [Q99KS2-1]
DR AlphaFoldDB; Q99KS2; -.
DR STRING; 10090.ENSMUSP00000113444; -.
DR GlyGen; Q99KS2; 1 site.
DR iPTMnet; Q99KS2; -.
DR PhosphoSitePlus; Q99KS2; -.
DR EPD; Q99KS2; -.
DR MaxQB; Q99KS2; -.
DR PaxDb; Q99KS2; -.
DR PeptideAtlas; Q99KS2; -.
DR PRIDE; Q99KS2; -.
DR ProteomicsDB; 252889; -. [Q99KS2-1]
DR Antibodypedia; 28784; 140 antibodies from 25 providers.
DR DNASU; 83485; -.
DR Ensembl; ENSMUST00000117989; ENSMUSP00000113444; ENSMUSG00000047084. [Q99KS2-1]
DR GeneID; 83485; -.
DR KEGG; mmu:83485; -.
DR UCSC; uc009hzz.2; mouse. [Q99KS2-1]
DR CTD; 51335; -.
DR MGI; MGI:1933212; Ngrn.
DR VEuPathDB; HostDB:ENSMUSG00000047084; -.
DR eggNOG; ENOG502S5A6; Eukaryota.
DR GeneTree; ENSGT00390000014472; -.
DR HOGENOM; CLU_076903_1_0_1; -.
DR InParanoid; Q99KS2; -.
DR OMA; AMDQIRY; -.
DR OrthoDB; 734251at2759; -.
DR PhylomeDB; Q99KS2; -.
DR TreeFam; TF324463; -.
DR BioGRID-ORCS; 83485; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Ngrn; mouse.
DR PRO; PR:Q99KS2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q99KS2; protein.
DR Bgee; ENSMUSG00000047084; Expressed in olfactory epithelium and 254 other tissues.
DR Genevisible; Q99KS2; MM.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0061668; P:mitochondrial ribosome assembly; ISS:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR InterPro; IPR010487; NGRN/Rrg9.
DR PANTHER; PTHR13475; PTHR13475; 1.
DR Pfam; PF06413; Neugrin; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; Differentiation; Glycoprotein;
KW Membrane; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..293
FT /note="Neugrin"
FT /id="PRO_0000294484"
FT REGION 177..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPE2"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 55..66
FT /note="SALKRQKKAMRF -> RYLLRGEPSAWS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039712"
FT VAR_SEQ 67..293
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039713"
FT CONFLICT 121
FT /note="V -> L (in Ref. 1; BAB21528)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="H -> Y (in Ref. 1; BAB21528)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="S -> A (in Ref. 4; AAH04034)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="P -> A (in Ref. 4; AAH04034)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="P -> L (in Ref. 4; AAH04034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 32447 MW; 2E1BD7C94829322C CRC64;
MALSLSLFLG GRVRTSLARC GFASQVMAGP GSVSCEPDPD SDWEPEEREL QEVESALKRQ
KKAMRFQKIR RQMEAPGAPP RTLTWEAMEQ IRYLHKEFAE SWSVPRLAEG FDVSTDVIRR
VLKSKFVPTL EQKLRQDQKV LKKAGFTREI GQLPVSEDTL KALSAGRSVS GLLMAGDEVS
SKSQNHSTAL KVAKSHPHST DAQKKREGRD KRIQVLEESL VPATTALGHQ RELQKSATSD
SEATGRAGSD TLPSAVLLEE LKPGEPGDQS FSSKVVQRGH DFFDSNGNFL YRI
