NCDN_BOVIN
ID NCDN_BOVIN Reviewed; 729 AA.
AC Q2KJ97; A1L535;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Neurochondrin;
GN Name=NCDN;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MCHR1 (By similarity). Interacts with SEMA4C.
CC Interacts with DIAPH1 (via FH3 domain) (By similarity). Interacts with
CC GRM5. {ECO:0000250|UniProtKB:O35095, ECO:0000250|UniProtKB:Q9UBB6,
CC ECO:0000250|UniProtKB:Q9Z0E0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O35095}. Endosome membrane
CC {ECO:0000250|UniProtKB:O35095}; Lipid-anchor
CC {ECO:0000250|UniProtKB:O35095}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:O35095}. Postsynapse
CC {ECO:0000250|UniProtKB:O35095}. Note=Localizes to somatic regions of
CC neurons. Localization to endosome membrane requires palmitoylation.
CC {ECO:0000250|UniProtKB:O35095}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2KJ97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2KJ97-2; Sequence=VSP_032314;
CC -!- PTM: Palmitoylated. Palmitoylation by ZDHHC1, ZDHHC3 and ZDHHC11
CC regulates the association of NCDN with endosome membranes. May also be
CC palmitoylated by ZDHHC7. {ECO:0000250|UniProtKB:O35095}.
CC -!- SIMILARITY: Belongs to the neurochondrin family. {ECO:0000305}.
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DR EMBL; BT029822; ABM06085.1; -; mRNA.
DR EMBL; BC105450; AAI05451.1; -; mRNA.
DR RefSeq; NP_001039396.1; NM_001045931.1. [Q2KJ97-1]
DR AlphaFoldDB; Q2KJ97; -.
DR SMR; Q2KJ97; -.
DR STRING; 9913.ENSBTAP00000033145; -.
DR PaxDb; Q2KJ97; -.
DR PRIDE; Q2KJ97; -.
DR Ensembl; ENSBTAT00000033225; ENSBTAP00000033145; ENSBTAG00000016696. [Q2KJ97-1]
DR GeneID; 505994; -.
DR KEGG; bta:505994; -.
DR CTD; 23154; -.
DR VEuPathDB; HostDB:ENSBTAG00000016696; -.
DR eggNOG; KOG2611; Eukaryota.
DR GeneTree; ENSGT00390000013601; -.
DR HOGENOM; CLU_012443_0_0_1; -.
DR InParanoid; Q2KJ97; -.
DR OMA; DRKYELC; -.
DR OrthoDB; 311670at2759; -.
DR TreeFam; TF323752; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000016696; Expressed in prefrontal cortex and 104 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0045453; P:bone resorption; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Cell projection; Cytoplasm; Endosome;
KW Lipoprotein; Membrane; Methylation; Palmitate; Phosphoprotein;
KW 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_0000324616"
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:0000250|UniProtKB:O35095"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O35095"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O35095"
FT VAR_SEQ 1..340
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_032314"
SQ SEQUENCE 729 AA; 78799 MW; D2397C69662B2B7E CRC64;
MSCCDLAAAG QLGKAGIMAS DCEPALNQAE SRNPTLERYL GALREAKNDS EQFAALLLVT
KAVKAGDIDA KTRRRIFDAV GFTFPNRLLT TKEAPDGCPD HVLRALGVAL LACFCSDPEL
AAHPQVLNKI PILSTFLTAR GDPDDAARRS MVDDTYQCLT AVAGTPRGPR HLIAGGTVSA
LCQAYLGHGY GFDQALALLV GLLAAAETQC WKEAEPDLLA VLRGLSEDFQ KAEDASKFEL
CQLLPLFLPP TTVPSECLRD LQAGLARILG SKLSSWQRNP ALKLAARLAH ACGSDWIPAG
NSGSKFLALL VNLACVEVRL ALEETGTEVK EDVVTACYAL MELGIQECTR CEQSLLKEPQ
KVQLVSIMKE AIGAVIHYLQ QVGPEKQKEP FVFASVRILG AWLAEETSSL RKEVCQLLPF
LVRYAKTLYE EAEEANDLSQ QVATLAISPT TPGPTWPGDA LRLLLPGWCH LTVEDGPREI
LIKEGAPSLL CKYFLQQWEL TSPGHDTSVL PDSVEIGLQT CCHIFLNLVV TAPGLIKRDA
CFTSLMNTLM ASLPSLVQQQ GRLLLAANVA TLGLLMARLL STSPALQGTP ASRGFFAAAI
LFLSQSHVAR ATPGSEQAVL ALSPDYEGVW ADLQELWFLG MQAFTGCVPL LPWLAPAALR
SRWPQELLQL LGSVSPNSVK PEMVAAYQGV LVELARANRL CREAMRLQAG EETASHYRMA
ALEQCLAEP
