NEUG_BOVIN
ID NEUG_BOVIN Reviewed; 78 AA.
AC P35722; Q2KI68;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Neurogranin;
DE Short=NG;
DE AltName: Full=B-50 immunoreactive C-kinase substrate;
DE Short=BICKS;
DE AltName: Full=p17;
DE Contains:
DE RecName: Full=NEUG(55-78);
GN Name=NRGN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-36, ACETYLATION AT MET-1, AND MASS
RP SPECTROMETRY.
RX PubMed=1824695; DOI=10.1016/s0021-9258(18)52425-x;
RA Baudier J., Deloulme J.C., van Dorsselaer A., Black D., Matthes H.W.D.;
RT "Purification and characterization of a brain-specific protein kinase C
RT substrate, neurogranin (p17). Identification of a consensus amino acid
RT sequence between neurogranin and neuromodulin (GAP43) that corresponds to
RT the protein kinase C phosphorylation site and the calmodulin-binding
RT domain.";
RL J. Biol. Chem. 266:229-237(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION AT SER-36 BY PHK.
RX PubMed=8454596; DOI=10.1016/s0021-9258(18)53240-3;
RA Paudel H.K., Zwiers H., Wang J.H.;
RT "Phosphorylase kinase phosphorylates the calmodulin-binding regulatory
RT regions of neuronal tissue-specific proteins B-50 (GAP-43) and
RT neurogranin.";
RL J. Biol. Chem. 268:6207-6213(1993).
RN [4]
RP CITRULLINATION AT ARG-68.
RX PubMed=23828821; DOI=10.1002/pmic.201300064;
RA Jin Z., Fu Z., Yang J., Troncosco J., Everett A.D., Van Eyk J.E.;
RT "Identification and Characterization of citrulline-modified brain proteins
RT by combining HCD and CID fragmentation.";
RL Proteomics 13:2682-2691(2013).
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.
CC -!- TISSUE SPECIFICITY: Is highly enriched in brain. Accumulates
CC postsynaptically in dendritic spines of neostriatal neurons.
CC -!- DOMAIN: Neurogranin is intrinsically unstructured; however, upon
CC binding with CaM, The IQ domain adopts a helical conformation.
CC {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
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 (By similarity). {ECO:0000250}.
CC -!- MASS SPECTROMETRY: [Neurogranin]: Mass=7837.1; Mass_error=0.5;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:1824695};
CC -!- SIMILARITY: Belongs to the neurogranin family. {ECO:0000305}.
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DR EMBL; BC112751; AAI12752.1; -; mRNA.
DR PIR; A39034; A39034.
DR RefSeq; NP_001106784.1; NM_001113313.2.
DR AlphaFoldDB; P35722; -.
DR BMRB; P35722; -.
DR SMR; P35722; -.
DR STRING; 9913.ENSBTAP00000001930; -.
DR iPTMnet; P35722; -.
DR PaxDb; P35722; -.
DR Ensembl; ENSBTAT00000001930; ENSBTAP00000001930; ENSBTAG00000001474.
DR GeneID; 616955; -.
DR KEGG; bta:616955; -.
DR CTD; 4900; -.
DR VEuPathDB; HostDB:ENSBTAG00000001474; -.
DR VGNC; VGNC:32262; NRGN.
DR eggNOG; ENOG502S6YP; Eukaryota.
DR GeneTree; ENSGT00440000039324; -.
DR HOGENOM; CLU_129609_1_0_1; -.
DR InParanoid; P35722; -.
DR OMA; KSKDPEC; -.
DR TreeFam; TF342962; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000001474; Expressed in Ammon's horn and 99 other tissues.
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 1: Evidence at protein level;
KW Acetylation; Calmodulin-binding; Citrullination; Direct protein sequencing;
KW Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..78
FT /note="Neurogranin"
FT /id="PRO_0000159589"
FT PEPTIDE 55..78
FT /note="NEUG(55-78)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000377700"
FT DOMAIN 26..49
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 50..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:0000269|PubMed:1824695"
FT MOD_RES 36
FT /note="Phosphoserine; by PHK and PKC"
FT /evidence="ECO:0000269|PubMed:1824695,
FT ECO:0000269|PubMed:8454596"
FT MOD_RES 68
FT /note="Citrulline; partial"
FT /evidence="ECO:0000269|PubMed:23828821"
FT MOD_RES 68
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q92686"
FT CONFLICT 11
FT /note="K -> C (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="D -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 78 AA; 7549 MW; 8E47CDA39F085794 CRC64;
MDCCTESACS KPDDDILDIP LDDPGANAAA AKIQASFRGH MARKKIKSGE RGRKGPGPGG
PGGAGGARGG AGGGPSGD
