ID   NEUG_CAPHI              Reviewed;          78 AA.
AC   P54877;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Neurogranin;
DE            Short=NG;
DE   AltName: Full=Protein kinase C substrate 7.5 kDa protein;
DE   AltName: Full=RC3;
DE   Contains:
DE     RecName: Full=NEUG(55-78);
GN   Name=NRGN;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7539519; DOI=10.1016/0169-328x(94)00237-9;
RA   Piosik P.A., van Groenigen M., Ponne N.J., Bolhuis P.A., Baas F.;
RT   "RC3/neurogranin structure and expression in the caprine brain in relation
RT   to congenital hypothyroidism.";
RL   Brain Res. Mol. Brain Res. 29:119-130(1995).
CC   -!- FUNCTION: Acts as a 'third messenger' substrate of protein kinase C-
CC       mediated molecular cascades during synaptic development and remodeling.
CC       Binds to calmodulin in the absence of calcium (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: Neurogranin is intrinsically unstructured; however, upon
CC       binding with CaM, The IQ domain adopts a helical conformation.
CC       {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:0000250}.
CC   -!- SIMILARITY: Belongs to the neurogranin family. {ECO:0000305}.
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DR   EMBL; S78295; AAB34481.1; -; mRNA.
DR   PIR; I47043; I47043.
DR   AlphaFoldDB; P54877; -.
DR   BMRB; P54877; -.
DR   SMR; P54877; -.
DR   STRING; 9925.ENSCHIP00000027053; -.
DR   Ensembl; ENSCHIT00010026624; ENSCHIP00010018980; ENSCHIG00010013897.
DR   Proteomes; UP000291000; Unplaced.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   Pfam; PF00612; IQ; 1.
DR   SMART; SM00015; IQ; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   3: Inferred from homology;
KW   Acetylation; Calmodulin-binding; Citrullination; Methylation;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..78
FT                   /note="Neurogranin"
FT                   /id="PRO_0000159590"
FT   PEPTIDE         55..78
FT                   /note="NEUG(55-78)"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000377701"
FT   DOMAIN          26..47
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          48..78
FT                   /note="Collagen-like"
FT   REGION          38..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            38
FT                   /note="Crucial for interaction with calmodulin"
FT                   /evidence="ECO:0000250"
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:0000250|UniProtKB:P35722"
FT   MOD_RES         68
FT                   /note="Citrulline; partial"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         68
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92686"
SQ   SEQUENCE   78 AA;  7549 MW;  8E47CDA39F085794 CRC64;
     MDCCTESACS KPDDDILDIP LDDPGANAAA AKIQASFRGH MARKKIKSGE RGRKGPGPGG
     PGGAGGARGG AGGGPSGD