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Neurochondrin (Neurite outgrowth-related protein from the rat brain) (Norbin)

 NCDN_RAT                Reviewed;         729 AA.
O35095; Q5PQW2;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 2.
12-SEP-2018, entry version 101.
RecName: Full=Neurochondrin;
AltName: Full=Neurite outgrowth-related protein from the rat brain;
AltName: Full=Norbin;
Name=Ncdn;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
INDUCTION.
STRAIN=Wistar; TISSUE=Brain;
PubMed=9398642; DOI=10.1006/bbrc.1997.7660;
Shinozaki K., Maruyama K., Kume H., Kuzume H., Obata K.;
"A novel brain gene, norbin, induced by treatment of
tetraethylammonium in rat hippocampal slice and accompanied with
neurite-outgrowth in neuro 2a cells.";
Biochem. Biophys. Res. Commun. 240:766-771(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10521593; DOI=10.1016/S0169-328X(99)00181-3;
Shinozaki K., Kume H., Kuzume H., Obata K., Maruyama K.;
"Norbin, a neurite-outgrowth-related protein, is a cytosolic protein
localized in the somatodendritic region of neurons and distributed
prominently in dendritic outgrowth in Purkinje cells.";
Brain Res. Mol. Brain Res. 71:364-368(1999).
[4]
TISSUE SPECIFICITY.
PubMed=18572016; DOI=10.1016/j.bbrc.2008.06.042;
Schwaibold E.M., Brandt D.T.;
"Identification of Neurochondrin as a new interaction partner of the
FH3 domain of the Diaphanous-related formin Dia1.";
Biochem. Biophys. Res. Commun. 373:366-372(2008).
[5]
INTERACTION WITH GRM5.
PubMed=20007903; DOI=10.1126/science.1178496;
Wang H., Westin L., Nong Y., Birnbaum S., Bendor J., Brismar H.,
Nestler E., Aperia A., Flajolet M., Greengard P.;
"Norbin is an endogenous regulator of metabotropic glutamate receptor
5 signaling.";
Science 326:1554-1557(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Probably involved in signal transduction, in the nervous
system, via increasing cell surface localization of GRM5 and
positively regulating its signaling. Required for the spatial
learning process. Acts as a negative regulator of Ca(2+)-
calmodulin-dependent protein kinase 2 (CaMK2) phosphorylation. May
play a role in modulating melanin-concentrating hormone-mediated
functions via its interaction with MCHR1 that interferes with G
protein-coupled signal transduction. May be involved in bone
metabolism. May also be involved in neurite outgrowth.
{ECO:0000269|PubMed:9398642}.
-!- SUBUNIT: Interacts with MCHR1 and SEMA4C (By similarity).
Interacts with DIAPH1 (via FH3 domain) (By similarity). Interacts
with GRM5. {ECO:0000250, ECO:0000269|PubMed:20007903}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:10521593}. Cell projection, dendrite
{ECO:0000269|PubMed:10521593}. Note=Localizes to somatic regions
of neurons.
-!- TISSUE SPECIFICITY: Expressed in brain and in peripheral nervous
system (at protein level). Weakly expressed in neurites.
{ECO:0000269|PubMed:10521593, ECO:0000269|PubMed:18572016,
ECO:0000269|PubMed:9398642}.
-!- INDUCTION: Upon tetraethylammonium (TEA) treatment.
{ECO:0000269|PubMed:9398642}.
-!- SIMILARITY: Belongs to the neurochondrin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB006461; BAA22938.1; -; mRNA.
EMBL; BC087000; AAH87000.1; -; mRNA.
PIR; JC5812; JC5812.
RefSeq; NP_445995.2; NM_053543.2.
RefSeq; XP_017449158.1; XM_017593669.1.
UniGene; Rn.5653; -.
BioGrid; 250125; 1.
IntAct; O35095; 1.
iPTMnet; O35095; -.
PhosphoSitePlus; O35095; -.
SwissPalm; O35095; -.
PaxDb; O35095; -.
PRIDE; O35095; -.
Ensembl; ENSRNOT00000016230; ENSRNOP00000016229; ENSRNOG00000011751.
GeneID; 89791; -.
KEGG; rno:89791; -.
UCSC; RGD:621734; rat.
CTD; 23154; -.
RGD; 621734; Ncdn.
eggNOG; KOG2611; Eukaryota.
eggNOG; ENOG410XRYT; LUCA.
GeneTree; ENSGT00390000013601; -.
HOGENOM; HOG000113742; -.
HOVERGEN; HBG097452; -.
InParanoid; O35095; -.
OMA; YIQATIR; -.
OrthoDB; EOG091G04JK; -.
PhylomeDB; O35095; -.
TreeFam; TF323752; -.
PRO; PR:O35095; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000011751; Expressed in 9 organ(s), highest expression level in Ammon's horn.
Genevisible; O35095; RN.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0045453; P:bone resorption; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; IEP:UniProtKB.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IDA:RGD.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR008709; Neurochondrin.
PANTHER; PTHR13109; PTHR13109; 1.
Pfam; PF05536; Neurochondrin; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
Acetylation; Cell projection; Complete proteome; Cytoplasm;
Methylation; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9UBB6}.
CHAIN 2 729 Neurochondrin.
/FTId=PRO_0000324619.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q9UBB6}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBB6}.
MOD_RES 75 75 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q9Z0E0}.
MOD_RES 448 448 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CONFLICT 381 381 R -> Q (in Ref. 1; BAA22938).
{ECO:0000305}.
SEQUENCE 729 AA; 78923 MW; EDED4B921A6B85CD CRC64;
MSCCDLAAAG QLGKAGIMAS DCEPALNQAE SRNPTLERYL GALREAKNDS EQFAALLLVT
KAVKAGDIDA KTRRRIFDAV GFTFPNRLLT TKEAPDGCPD HVLRALGVAL LACFCSDPEL
ASHPQVLNKI PILCTFLTAR GDPDDAARRS MIDDTYQCLT AVAGTPRGPR HLIAGGTVSA
LCQAYLGHGY GFDQALALLV GLLAAAETQC WKEAEPDLLA VLRGLSEDFQ RAEDASKFEL
CQLLPLFLPP TTVPPECHRD LQAGLARILG SKLSSWQRNP ALKLAARLAH ACGSDWIPVG
SSGSKFLALL VNLACVEVRL ALEETGTEVK EDVVTACYAL MELGIQECTR CEQSLLKEPQ
KVQLVSIMKE AIGAVIHYLL RVGPEKQKEP FVFASVRILG AWLAEETSSL RKEVCQLLPF
LVRYAKTLYE EAEEASDISQ QVANLAISPT TPGPAWPGDA LRLLLPGWCH LTVEDGPREI
LIKEGAPSLL CKYFLQQWEL TSPGHDTSVL PDSVEIGLQT CCHIFLNLVV TAPGLIKRDA
CFTSLMNTLM TSLPSLVQQQ GRLLLAANVA TLGLLMARLL STSPALQGTP ASRGFFAAAI
LFLSQSHVAR ATPGSDQAVL ALSPDYEGIW ADLQELWFLG MQAFTGCVPL LPWLAPAALR
SRWPQELLQL LGSVSPNSVK PEMVAAYQGV LVELARANRL CREAMRLQAG EETASHYRMA
ALEQCLSEP


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