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Protein

Neurogranin

Gene

Nrgn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates the affinity of calmodulin for calcium. Involved in synaptic plasticity and spatial learning (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei38 – 381Crucial for interaction with calmodulinBy similarity

GO - Molecular functioni

  • calmodulin binding Source: RGD
  • phosphatidic acid binding Source: RGD
  • phosphatidylinositol-3,4,5-trisphosphate binding Source: RGD

GO - Biological processi

  • associative learning Source: RGD
  • positive regulation of long-term synaptic potentiation Source: RGD
  • telencephalon development Source: RGD
Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogranin
Short name:
Ng
Alternative name(s):
Protein kinase C substrate 7.5 kDa protein
RC3
Cleaved into the following chain:
Gene namesi
Name:Nrgn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi61833. Nrgn.

Subcellular locationi

GO - Cellular componenti

  • axon Source: RGD
  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • dendritic spine head Source: RGD
  • mitochondrial membrane Source: RGD
  • neuronal cell body Source: RGD
  • nucleus Source: RGD
  • postsynaptic density Source: RGD
  • synapse Source: RGD
  • trans-Golgi network transport vesicle membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi3 – 31C → S: No effect on oxidant-mediated disulfide bond formation nor on in vitro PKC-mediated phosphorylation. No effect on oxidant-mediated disulfide bond formation; when associated with G-4 or S-9. 1 Publication
Mutagenesisi4 – 41C → G: No effect on oxidant-mediated disulfide bond formation nor on in vitro PKC-mediated phosphorylation. No effect on oxidant-mediated disulfide bond formation; when associated with S-3 or S-9. 1 Publication
Mutagenesisi9 – 91C → S: No effect on oxidant-mediated disulfide bond formation nor on in vitro PKC-mediated phosphorylation. No effect on oxidant-mediated disulfide bond formation; when associated with S-3 or G-4. 1 Publication
Mutagenesisi51 – 511C → G: No oxidant-mediated disulfide bond formation. No effect on in vitro PKC-mediated phosphorylation. No oxidant-mediated disulfide bond formation; when associated with S-3; G-4 and S-9. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7878NeurograninPRO_0000159593Add
BLAST
Peptidei55 – 7824NEUG(55-78)PRO_0000375992Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCurated
Disulfide bondi3 ↔ 51Or C-51 with C-4 or C-91 Publication
Modified residuei36 – 361Phosphoserine; by PHK and PKC2 Publications
Modified residuei68 – 681Citrulline; partialBy similarity

Post-translational modificationi

Phosphorylated at Ser-36 by PHK and PKC. Phosphorylation prevents interaction with Calmodulin and interrupts several learning- and memory-associated functions (By similarity).By similarity
Phosphorylation is activated by calcium, phospholipids, and diacylglycerol. Phosphorylation inhibits binding to calmodulin both in the presence and absence of calcium.2 Publications
Disulfide bond formation is redox-sensitive. The cysteine residues are readily oxidized by several nitric acid (NO) donors and other oxidants to form intramolecular disulfide. Cys-51 can form a disulfide with any other of the cysteine residues with an order of reactivity Cys-9 > Cys-4 > Cys-3.

Keywords - PTMi

Acetylation, Citrullination, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ04940.
PRIDEiQ04940.

PTM databases

iPTMnetiQ04940.

Expressioni

Tissue specificityi

Highly enriched in brain with restricted expression in neuronal subsets primarily in the cortex, striatum, and hippocampus as well as certain nuclei within the thalamus, hypothalamus and olfactory bulb. Accumulates postsynaptically in dendritic spines of neostriatal neurons.2 Publications

Gene expression databases

GenevisibleiQ04940. RN.

Interactioni

Subunit structurei

Interacts with apo-calmodulin; this interaction decreases the affinity of calmodulin for calcium ions.2 Publications

GO - Molecular functioni

  • calmodulin binding Source: RGD

Protein-protein interaction databases

BioGridi249041. 3 interactions.
STRINGi10116.ENSRNOP00000014404.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 4722IQPROSITE-ProRule annotationAdd
BLAST
Domaini48 – 7831Collagen-likeAdd
BLAST

Domaini

Neurogranin is intrinsically unstructured; however, upon binding with CaM, The IQ domain adopts a helical conformation.By similarity

Sequence similaritiesi

Belongs to the neurogranin family.Curated
Contains 1 collagen-like domain.Curated
Contains 1 IQ domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410JNUP. Eukaryota.
ENOG41118RJ. LUCA.
GeneTreeiENSGT00440000039324.
HOGENOMiHOG000113769.
HOVERGENiHBG000470.
InParanoidiQ04940.
OMAiPQESACS.
OrthoDBiEOG7BCNFV.
PhylomeDBiQ04940.
TreeFamiTF342962.

Family and domain databases

InterProiIPR000048. IQ_motif_EF-hand-BS.
[Graphical view]
PfamiPF00612. IQ. 1 hit.
[Graphical view]
SMARTiSM00015. IQ. 1 hit.
[Graphical view]
PROSITEiPS50096. IQ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q04940-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDCCTESACS KPDDDILDIP LDDPGANAAA AKIQASFRGH MARKKIKSGE
60 70
CGRKGPGPGG PGGAGGARGG AGGGPSGD
Length:78
Mass (Da):7,496
Last modified:June 1, 1994 - v1
Checksum:i8E47CDB38E095794
GO

Mass spectrometryi

Molecular mass is 1775.78 Da from positions 55 - 78. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09119 mRNA. Translation: AAA42023.1.
U22062 Genomic RNA. Translation: AAA80223.1.
PIRiA57288.
RefSeqiNP_077054.1. NM_024140.2.
UniGeneiRn.11236.

Genome annotation databases

EnsembliENSRNOT00000014404; ENSRNOP00000014404; ENSRNOG00000010688.
GeneIDi64356.
KEGGirno:64356.
UCSCiRGD:61833. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09119 mRNA. Translation: AAA42023.1.
U22062 Genomic RNA. Translation: AAA80223.1.
PIRiA57288.
RefSeqiNP_077054.1. NM_024140.2.
UniGeneiRn.11236.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249041. 3 interactions.
STRINGi10116.ENSRNOP00000014404.

PTM databases

iPTMnetiQ04940.

Proteomic databases

PaxDbiQ04940.
PRIDEiQ04940.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014404; ENSRNOP00000014404; ENSRNOG00000010688.
GeneIDi64356.
KEGGirno:64356.
UCSCiRGD:61833. rat.

Organism-specific databases

CTDi4900.
RGDi61833. Nrgn.

Phylogenomic databases

eggNOGiENOG410JNUP. Eukaryota.
ENOG41118RJ. LUCA.
GeneTreeiENSGT00440000039324.
HOGENOMiHOG000113769.
HOVERGENiHBG000470.
InParanoidiQ04940.
OMAiPQESACS.
OrthoDBiEOG7BCNFV.
PhylomeDBiQ04940.
TreeFamiTF342962.

Miscellaneous databases

PROiQ04940.

Gene expression databases

GenevisibleiQ04940. RN.

Family and domain databases

InterProiIPR000048. IQ_motif_EF-hand-BS.
[Graphical view]
PfamiPF00612. IQ. 1 hit.
[Graphical view]
SMARTiSM00015. IQ. 1 hit.
[Graphical view]
PROSITEiPS50096. IQ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Subtractive cDNA cloning of RC3, a rodent cortex-enriched mRNA encoding a novel 78 residue protein."
    Watson J.B., Battenberg E.F., Wong K.K., Bloom F.E., Sutcliffe J.G.
    J. Neurosci. Res. 26:397-408(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Characterization of a 7.5-kDa protein kinase C substrate (RC3 protein, neurogranin) from rat brain."
    Huang K.-P., Huang F.L., Chen H.-C.
    Arch. Biochem. Biophys. 305:570-580(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-36, INTERACTION WITH CALM1.
    Tissue: Brain.
  3. "Structure and regulation of the gene encoding the neuron-specific protein kinase C substrate neurogranin (RC3 protein)."
    Sato T., Xiao D.M., Li H., Huang F.L., Huang K.P.
    J. Biol. Chem. 270:10314-10322(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
    Tissue: Testis.
  4. "Discovering new bioactive neuropeptides in the striatum secretome using in vivo microdialysis and versatile proteomics."
    Bernay B., Gaillard M.-C., Guryca V., Emadali A., Kuhn L., Bertrand A., Detraz I., Carcenac C., Savasta M., Brouillet E., Garin J., Elalouf J.-M.
    Mol. Cell. Proteomics 8:946-958(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 55-78, MASS SPECTROMETRY.
    Strain: Wistar.
    Tissue: Corpus striatum.
  5. "Localization of the protein kinase C phosphorylation/calmodulin-binding substrate RC3 in dendritic spines of neostriatal neurons."
    Watson J.B., Sutcliffe J.G., Fisher R.S.
    Proc. Natl. Acad. Sci. U.S.A. 89:8581-8585(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  6. "Phosphorylase kinase phosphorylates the calmodulin-binding regulatory regions of neuronal tissue-specific proteins B-50 (GAP-43) and neurogranin."
    Paudel H.K., Zwiers H., Wang J.H.
    J. Biol. Chem. 268:6207-6213(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-36 BY PHK.
  7. "Nitric oxide modification of rat brain neurogranin. Identification of the cysteine residues involved in intramolecular disulfide bridge formation using site-directed mutagenesis."
    Mahoney C.W., Pak J.H., Huang K.-P.
    J. Biol. Chem. 271:28798-28804(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS, INTERACTION WITH CALM1, MUTAGENESIS OF CYS-3; CYS-4; CYS-9 AND CYS-51.
  8. "RC3/neurogranin and Ca2+/calmodulin-dependent protein kinase II produce opposing effects on the affinity of calmodulin for calcium."
    Gaertner T.R., Putkey J.A., Waxham M.N.
    J. Biol. Chem. 279:39374-39382(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiNEUG_RAT
AccessioniPrimary (citable) accession number: Q04940
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 8, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.