NCDN_RAT
ID NCDN_RAT Reviewed; 729 AA.
AC O35095; Q5PQW2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Neurochondrin;
DE AltName: Full=Neurite outgrowth-related protein from the rat brain;
DE AltName: Full=Norbin;
GN Name=Ncdn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=9398642; DOI=10.1006/bbrc.1997.7660;
RA Shinozaki K., Maruyama K., Kume H., Kuzume H., Obata K.;
RT "A novel brain gene, norbin, induced by treatment of tetraethylammonium in
RT rat hippocampal slice and accompanied with neurite-outgrowth in neuro 2a
RT cells.";
RL Biochem. Biophys. Res. Commun. 240:766-771(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10521593; DOI=10.1016/s0169-328x(99)00181-3;
RA Shinozaki K., Kume H., Kuzume H., Obata K., Maruyama K.;
RT "Norbin, a neurite-outgrowth-related protein, is a cytosolic protein
RT localized in the somatodendritic region of neurons and distributed
RT prominently in dendritic outgrowth in Purkinje cells.";
RL Brain Res. Mol. Brain Res. 71:364-368(1999).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=18572016; DOI=10.1016/j.bbrc.2008.06.042;
RA Schwaibold E.M., Brandt D.T.;
RT "Identification of Neurochondrin as a new interaction partner of the FH3
RT domain of the Diaphanous-related formin Dia1.";
RL Biochem. Biophys. Res. Commun. 373:366-372(2008).
RN [5]
RP INTERACTION WITH GRM5.
RX PubMed=20007903; DOI=10.1126/science.1178496;
RA Wang H., Westin L., Nong Y., Birnbaum S., Bendor J., Brismar H.,
RA Nestler E., Aperia A., Flajolet M., Greengard P.;
RT "Norbin is an endogenous regulator of metabotropic glutamate receptor 5
RT signaling.";
RL Science 326:1554-1557(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7]
RP SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-3 AND CYS-4, AND MUTAGENESIS OF
RP CYS-3 AND CYS-4.
RX PubMed=23687301; DOI=10.1074/jbc.m112.431676;
RA Oku S., Takahashi N., Fukata Y., Fukata M.;
RT "In silico screening for palmitoyl substrates reveals a role for DHHC1/3/10
RT (zDHHC1/3/11)-mediated neurochondrin palmitoylation in its targeting to
RT Rab5-positive endosomes.";
RL J. Biol. Chem. 288:19816-19829(2013).
CC -!- FUNCTION: Probably involved in signal transduction, in the nervous
CC system, via increasing cell surface localization of GRM5 and positively
CC regulating its signaling. Required for the spatial learning process.
CC Acts as a negative regulator of Ca(2+)-calmodulin-dependent protein
CC kinase 2 (CaMK2) phosphorylation. May play a role in modulating
CC melanin-concentrating hormone-mediated functions via its interaction
CC with MCHR1 that interferes with G protein-coupled signal transduction.
CC May be involved in bone metabolism. May also be involved in neurite
CC outgrowth. {ECO:0000269|PubMed:9398642}.
CC -!- SUBUNIT: Interacts with MCHR1 (By similarity). Interacts with SEMA4C.
CC Interacts with DIAPH1 (via FH3 domain) (By similarity). Interacts with
CC GRM5 (PubMed:20007903). {ECO:0000250|UniProtKB:Q9UBB6,
CC ECO:0000250|UniProtKB:Q9Z0E0, ECO:0000269|PubMed:20007903}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10521593}.
CC Endosome membrane {ECO:0000269|PubMed:23687301}; Lipid-anchor
CC {ECO:0000305|PubMed:23687301}. Cell projection, dendrite
CC {ECO:0000269|PubMed:10521593, ECO:0000269|PubMed:23687301}. Postsynapse
CC {ECO:0000269|PubMed:23687301}. Note=Localizes to somatic regions of
CC neurons (PubMed:10521593, PubMed:23687301). Localization to endosome
CC membrane requires palmitoylation (PubMed:23687301).
CC {ECO:0000269|PubMed:10521593, ECO:0000269|PubMed:23687301}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and in peripheral nervous system
CC (at protein level). Weakly expressed in neurites.
CC {ECO:0000269|PubMed:10521593, ECO:0000269|PubMed:18572016,
CC ECO:0000269|PubMed:9398642}.
CC -!- INDUCTION: Upon tetraethylammonium (TEA) treatment.
CC {ECO:0000269|PubMed:9398642}.
CC -!- PTM: Palmitoylated (PubMed:23687301). Palmitoylation by ZDHHC1, ZDHHC3
CC and ZDHHC11 regulates the association of NCDN with endosome membranes
CC (PubMed:23687301). May also be palmitoylated by ZDHHC7
CC (PubMed:23687301). {ECO:0000269|PubMed:23687301}.
CC -!- SIMILARITY: Belongs to the neurochondrin family. {ECO:0000305}.
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DR EMBL; AB006461; BAA22938.1; -; mRNA.
DR EMBL; BC087000; AAH87000.1; -; mRNA.
DR PIR; JC5812; JC5812.
DR RefSeq; NP_445995.2; NM_053543.2.
DR RefSeq; XP_017449158.1; XM_017593669.1.
DR AlphaFoldDB; O35095; -.
DR SMR; O35095; -.
DR BioGRID; 250125; 3.
DR IntAct; O35095; 3.
DR MINT; O35095; -.
DR STRING; 10116.ENSRNOP00000016229; -.
DR iPTMnet; O35095; -.
DR PhosphoSitePlus; O35095; -.
DR SwissPalm; O35095; -.
DR jPOST; O35095; -.
DR PaxDb; O35095; -.
DR PRIDE; O35095; -.
DR Ensembl; ENSRNOT00000016230; ENSRNOP00000016229; ENSRNOG00000011751.
DR GeneID; 89791; -.
DR KEGG; rno:89791; -.
DR UCSC; RGD:621734; rat.
DR CTD; 23154; -.
DR RGD; 621734; Ncdn.
DR eggNOG; KOG2611; Eukaryota.
DR GeneTree; ENSGT00390000013601; -.
DR HOGENOM; CLU_012443_0_0_1; -.
DR InParanoid; O35095; -.
DR OMA; DRKYELC; -.
DR OrthoDB; 311670at2759; -.
DR PhylomeDB; O35095; -.
DR TreeFam; TF323752; -.
DR PRO; PR:O35095; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000011751; Expressed in Ammon's horn and 19 other tissues.
DR Genevisible; O35095; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:UniProtKB.
DR GO; GO:0045453; P:bone resorption; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IEP:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IDA:RGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR008709; Neurochondrin.
DR PANTHER; PTHR13109; PTHR13109; 1.
DR Pfam; PF05536; Neurochondrin; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Cytoplasm; Endosome; Lipoprotein; Membrane;
KW Methylation; Palmitate; Phosphoprotein; Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB6"
FT CHAIN 2..729
FT /note="Neurochondrin"
FT /id="PRO_0000324619"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB6"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB6"
FT MOD_RES 75
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0E0"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:23687301"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:23687301"
FT MUTAGEN 3
FT /note="C->S: Loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:23687301"
FT MUTAGEN 4
FT /note="C->S: Loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:23687301"
FT CONFLICT 381
FT /note="R -> Q (in Ref. 1; BAA22938)"
FT /evidence="ECO:0000305"
SQ 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
