NEUG_MOUSE
ID NEUG_MOUSE Reviewed; 78 AA.
AC P60761; B2RRN7; Q3TYH4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Neurogranin;
DE Short=Ng;
DE AltName: Full=RC3;
DE Contains:
DE RecName: Full=NEUG(55-78);
GN Name=Nrgn;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=129/SvJ;
RX PubMed=11016969; DOI=10.1073/pnas.210184697;
RA Pak J.H., Huang F.L., Li J., Balschun D., Reymann K.G., Chiang C.,
RA Westphal H., Huang K.P.;
RT "Involvement of neurogranin in the modulation of calcium/calmodulin-
RT dependent protein kinase II, synaptic plasticity, and spatial learning: a
RT study with knockout mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:11232-11237(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Visual cortex;
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 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 [4]
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 [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-68, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 27-50 IN COMPLEX WITH CALMODULIN,
RP SUBUNIT, IQ DOMAIN, PHOSPHORYLATION AT SER-36, AND MUTAGENESIS OF ARG-38.
RX PubMed=23462742; DOI=10.1038/srep01392;
RA Kumar V., Chichili V.P., Zhong L., Tang X., Velazquez-Campoy A., Sheu F.S.,
RA Seetharaman J., Gerges N.Z., Sivaraman J.;
RT "Structural basis for the interaction of unstructured neuron specific
RT substrates neuromodulin and neurogranin with Calmodulin.";
RL Sci. Rep. 3:1392-1392(2013).
CC -!- FUNCTION: Regulates the affinity of calmodulin for calcium. Involved in
CC synaptic plasticity and spatial learning.
CC {ECO:0000269|PubMed:11016969}.
CC -!- SUBUNIT: Interacts with apo-calmodulin; this interaction decreases the
CC affinity of calmodulin for calcium ions. {ECO:0000269|PubMed:23462742}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Synapse. Cell projection, dendritic
CC spine. Note=Restricted to dendritic spines of a subset of neurons.
CC {ECO:0000250}.
CC -!- DOMAIN: Neurogranin is intrinsically unstructured; however, upon
CC binding with CaM, The IQ domain adopts a helical conformation.
CC -!- PTM: Disulfide bond formation is redox-sensitive. The cysteine residues
CC are readily oxidized by several nitric acid (NO) donors and other
CC oxidants to form intramolecular disulfide. Cys-51 can form a disulfide
CC with any other of the cysteine residues with an order of reactivity
CC Cys-9 > Cys-4 > Cys-3 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-36 by PHK and PKC, phosphorylation prevents
CC interaction with Calmodulin and interrupts several learning- and
CC memory-associated functions. {ECO:0000269|PubMed:23462742}.
CC -!- SIMILARITY: Belongs to the neurogranin family. {ECO:0000305}.
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DR EMBL; AF230869; AAG27519.1; -; Genomic_DNA.
DR EMBL; AK002933; BAB22466.1; -; mRNA.
DR EMBL; AK158630; BAE34589.1; -; mRNA.
DR EMBL; BC061102; AAH61102.1; -; mRNA.
DR EMBL; BC138511; AAI38512.1; -; mRNA.
DR EMBL; BC138513; AAI38514.1; -; mRNA.
DR CCDS; CCDS40585.1; -.
DR RefSeq; NP_071312.1; NM_022029.2.
DR PDB; 4E50; X-ray; 2.70 A; A=25-50.
DR PDBsum; 4E50; -.
DR AlphaFoldDB; P60761; -.
DR BMRB; P60761; -.
DR SMR; P60761; -.
DR BioGRID; 211017; 5.
DR IntAct; P60761; 2.
DR STRING; 10090.ENSMUSP00000070113; -.
DR iPTMnet; P60761; -.
DR PhosphoSitePlus; P60761; -.
DR MaxQB; P60761; -.
DR PaxDb; P60761; -.
DR PeptideAtlas; P60761; -.
DR PRIDE; P60761; -.
DR ProteomicsDB; 287483; -.
DR Antibodypedia; 45991; 190 antibodies from 36 providers.
DR DNASU; 64011; -.
DR Ensembl; ENSMUST00000065668; ENSMUSP00000070113; ENSMUSG00000053310.
DR GeneID; 64011; -.
DR KEGG; mmu:64011; -.
DR UCSC; uc009ovc.1; mouse.
DR CTD; 4900; -.
DR MGI; MGI:1927184; Nrgn.
DR VEuPathDB; HostDB:ENSMUSG00000053310; -.
DR eggNOG; ENOG502S6YP; Eukaryota.
DR GeneTree; ENSGT00440000039324; -.
DR HOGENOM; CLU_129609_1_0_1; -.
DR InParanoid; P60761; -.
DR OMA; KSKDPEC; -.
DR PhylomeDB; P60761; -.
DR TreeFam; TF342962; -.
DR BioGRID-ORCS; 64011; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Nrgn; mouse.
DR PRO; PR:P60761; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P60761; protein.
DR Bgee; ENSMUSG00000053310; Expressed in superior frontal gyrus and 98 other tissues.
DR Genevisible; P60761; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0044327; C:dendritic spine head; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0012510; C:trans-Golgi network transport vesicle membrane; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IDA:MGI.
DR GO; GO:0070300; F:phosphatidic acid binding; ISO:MGI.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:MGI.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:MGI.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0021537; P:telencephalon development; IEA:Ensembl.
DR DisProt; DP02296; -.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR Pfam; PF00612; IQ; 1.
DR SMART; SM00015; IQ; 1.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calmodulin-binding; Cell projection;
KW Citrullination; Cytoplasm; Disulfide bond; Methylation; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..78
FT /note="Neurogranin"
FT /id="PRO_0000159592"
FT PEPTIDE 55..78
FT /note="NEUG(55-78)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000377702"
FT DOMAIN 26..47
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 48..78
FT /note="Collagen-like"
FT REGION 39..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 38
FT /note="Crucial for interaction with calmodulin"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P35722"
FT MOD_RES 36
FT /note="Phosphoserine; by PHK and PKC"
FT /evidence="ECO:0000269|PubMed:23462742"
FT MOD_RES 68
FT /note="Citrulline; partial"
FT /evidence="ECO:0000250"
FT MOD_RES 68
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT DISULFID 3..51
FT /note="Or C-51 with C-4 or C-9"
FT MUTAGEN 38
FT /note="R->A: Abolishes calmodulin binding, unable to
FT potentiate synaptic transmission."
FT /evidence="ECO:0000269|PubMed:23462742"
FT HELIX 28..45
FT /evidence="ECO:0007829|PDB:4E50"
SQ SEQUENCE 78 AA; 7496 MW; 8E47CDB38E095794 CRC64;
MDCCTESACS KPDDDILDIP LDDPGANAAA AKIQASFRGH MARKKIKSGE CGRKGPGPGG
PGGAGGARGG AGGGPSGD
