NCDN_HUMAN
ID NCDN_HUMAN Reviewed; 729 AA.
AC Q9UBB6; D3DPR9; Q9UBY2; Q9Y4A6; Q9Y4D9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Neurochondrin {ECO:0000305};
GN Name=NCDN {ECO:0000312|HGNC:HGNC:17597}; Synonyms=KIAA0607;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10524216; DOI=10.1016/s0167-4781(99)00120-7;
RA Mochizuki R., Ishizuka Y., Yanai K., Murakami K., Koga Y., Fukamizu A.;
RT "Molecular cloning and expression of human neurochondrin-1 and -2.";
RL Biochim. Biophys. Acta 1446:397-402(1999).
RN [2]
RP ERRATUM OF PUBMED:10524216.
RX PubMed=10684983; DOI=10.1016/s0167-4781(99)00236-5;
RA Mochizuki R., Ishizuka Y., Yanai K., Murakami K., Koga Y., Fukamizu A.;
RL Biochim. Biophys. Acta 1490:367-368(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [7]
RP FUNCTION, AND INTERACTION WITH MCHR1.
RX PubMed=16945926; DOI=10.1074/jbc.m602889200;
RA Francke F., Ward R.J., Jenkins L., Kellett E., Richter D., Milligan G.,
RA Baechner D.;
RT "Interaction of neurochondrin with the melanin-concentrating hormone
RT receptor 1 interferes with G protein-coupled signal transduction but not
RT agonist-mediated internalization.";
RL J. Biol. Chem. 281:32496-32507(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, ACETYLATION [LARGE SCALE
RP ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]
RP (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
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).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-392 AND LEU-392.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [14]
RP INVOLVEMENT IN NEDIES, FUNCTION, VARIANTS NEDIES GLN-433; GLN-478; ARG-498
RP AND LEU-652, AND CHARACTERIZATION OF VARIANTS NEDIES GLN-433; GLU-478;
RP ARG-498 AND LEU-652.
RX PubMed=33711248; DOI=10.1016/j.ajhg.2021.02.015;
RA Fatima A., Hoeber J., Schuster J., Koshimizu E., Maya-Gonzalez C.,
RA Keren B., Mignot C., Akram T., Ali Z., Miyatake S., Tanigawa J., Koike T.,
RA Kato M., Murakami Y., Abdullah U., Ali M.A., Fadoul R., Laan L.,
RA Castillejo-Lopez C., Liik M., Jin Z., Birnir B., Matsumoto N., Baig S.M.,
RA Klar J., Dahl N.;
RT "Monoallelic and bi-allelic variants in NCDN cause neurodevelopmental
RT delay, intellectual disability, and epilepsy.";
RL Am. J. Hum. Genet. 108:739-748(2021).
CC -!- FUNCTION: Probably involved in signal transduction in the nervous
CC system, via increasing cell surface localization of GRM5/mGluR5 and
CC positively regulating its signaling (PubMed:33711248). Required for the
CC spatial learning process. Acts as a negative regulator of Ca(2+)-
CC calmodulin-dependent protein kinase 2 (CaMK2) phosphorylation. May play
CC a role in modulating melanin-concentrating hormone-mediated functions
CC via its interaction with MCHR1 that interferes with G protein-coupled
CC signal transduction. May be involved in bone metabolism. May also be
CC involved in neurite outgrowth (Probable). {ECO:0000269|PubMed:16945926,
CC ECO:0000269|PubMed:33711248, ECO:0000305|PubMed:33711248}.
CC -!- SUBUNIT: Interacts with MCHR1 (PubMed:16945926). Interacts with SEMA4C
CC (By similarity). Interacts with DIAPH1 (via FH3 domain) (By
CC similarity). Interacts with GRM5 (By similarity).
CC {ECO:0000250|UniProtKB:O35095, ECO:0000250|UniProtKB:Q9Z0E0,
CC ECO:0000269|PubMed:16945926}.
CC -!- INTERACTION:
CC Q9UBB6; Q5JST6: EFHC2; NbExp=6; IntAct=EBI-1053490, EBI-2349927;
CC Q9UBB6; O95678: KRT75; NbExp=3; IntAct=EBI-1053490, EBI-2949715;
CC Q9UBB6; P26367: PAX6; NbExp=3; IntAct=EBI-1053490, EBI-747278;
CC Q9UBB6; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-1053490, EBI-717399;
CC Q9UBB6; Q08117: TLE5; NbExp=3; IntAct=EBI-1053490, EBI-717810;
CC Q9UBB6; O96006: ZBED1; NbExp=3; IntAct=EBI-1053490, EBI-740037;
CC Q9UBB6; Q8TD17: ZNF398; NbExp=3; IntAct=EBI-1053490, EBI-8643207;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23687301}.
CC Endosome membrane {ECO:0000250|UniProtKB:O35095}; Lipid-anchor
CC {ECO:0000305|PubMed:23687301}. 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; Synonyms=NCDN1, Neurochondrin-1;
CC IsoId=Q9UBB6-1; Sequence=Displayed;
CC Name=2; Synonyms=NCDN2, Neurochondrin-2;
CC IsoId=Q9UBB6-2; Sequence=VSP_032315;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in whole adult brain and in
CC all individual brain regions examined, including spinal cord. Weakly
CC expressed in ovary, testis, fetal brain and small intestine.
CC {ECO:0000269|PubMed:10524216, ECO:0000269|PubMed:9628581}.
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 -!- DISEASE: Neurodevelopmental disorder with infantile epileptic spasms
CC (NEDIES) [MIM:619373]: An autosomal dominant neurodevelopmental
CC disorder characterized by onset of severe and frequent epileptic spasms
CC within the first year of life. Affected individuals have global
CC developmental delay with delayed walking and poor or absent speech.
CC More variable features may include poor overall growth, high-arched
CC palate, and delayed myelination on brain imaging.
CC {ECO:0000269|PubMed:33711248}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the neurochondrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD05029.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA25533.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB018739; BAA85384.2; -; mRNA.
DR EMBL; AB018740; BAA85385.2; -; mRNA.
DR EMBL; AB027514; BAA77830.1; -; Genomic_DNA.
DR EMBL; AB027514; BAA77831.1; -; Genomic_DNA.
DR EMBL; AB011179; BAA25533.1; ALT_INIT; mRNA.
DR EMBL; AC004865; AAD05029.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471059; EAX07410.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07411.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07412.1; -; Genomic_DNA.
DR EMBL; BC024592; AAH24592.1; -; mRNA.
DR CCDS; CCDS30672.1; -. [Q9UBB6-2]
DR CCDS; CCDS392.1; -. [Q9UBB6-1]
DR RefSeq; NP_001014839.1; NM_001014839.1. [Q9UBB6-1]
DR RefSeq; NP_001014841.1; NM_001014841.1. [Q9UBB6-2]
DR RefSeq; NP_055099.1; NM_014284.2. [Q9UBB6-1]
DR AlphaFoldDB; Q9UBB6; -.
DR SMR; Q9UBB6; -.
DR BioGRID; 116768; 103.
DR IntAct; Q9UBB6; 18.
DR STRING; 9606.ENSP00000362340; -.
DR GlyGen; Q9UBB6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UBB6; -.
DR PhosphoSitePlus; Q9UBB6; -.
DR BioMuta; NCDN; -.
DR EPD; Q9UBB6; -.
DR jPOST; Q9UBB6; -.
DR MassIVE; Q9UBB6; -.
DR MaxQB; Q9UBB6; -.
DR PaxDb; Q9UBB6; -.
DR PeptideAtlas; Q9UBB6; -.
DR PRIDE; Q9UBB6; -.
DR ProteomicsDB; 83925; -. [Q9UBB6-1]
DR ProteomicsDB; 83926; -. [Q9UBB6-2]
DR Antibodypedia; 17311; 215 antibodies from 28 providers.
DR DNASU; 23154; -.
DR Ensembl; ENST00000356090.8; ENSP00000348394.4; ENSG00000020129.16. [Q9UBB6-1]
DR Ensembl; ENST00000373243.7; ENSP00000362340.2; ENSG00000020129.16. [Q9UBB6-1]
DR Ensembl; ENST00000373253.7; ENSP00000362350.3; ENSG00000020129.16. [Q9UBB6-2]
DR GeneID; 23154; -.
DR KEGG; hsa:23154; -.
DR MANE-Select; ENST00000373243.7; ENSP00000362340.2; NM_014284.3; NP_055099.1.
DR UCSC; uc001bza.3; human. [Q9UBB6-1]
DR CTD; 23154; -.
DR DisGeNET; 23154; -.
DR GeneCards; NCDN; -.
DR HGNC; HGNC:17597; NCDN.
DR HPA; ENSG00000020129; Tissue enriched (brain).
DR MIM; 608458; gene.
DR MIM; 619373; phenotype.
DR neXtProt; NX_Q9UBB6; -.
DR OpenTargets; ENSG00000020129; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA134963729; -.
DR VEuPathDB; HostDB:ENSG00000020129; -.
DR eggNOG; KOG2611; Eukaryota.
DR GeneTree; ENSGT00390000013601; -.
DR HOGENOM; CLU_012443_0_0_1; -.
DR InParanoid; Q9UBB6; -.
DR OMA; DRKYELC; -.
DR OrthoDB; 311670at2759; -.
DR PhylomeDB; Q9UBB6; -.
DR TreeFam; TF323752; -.
DR PathwayCommons; Q9UBB6; -.
DR SignaLink; Q9UBB6; -.
DR BioGRID-ORCS; 23154; 27 hits in 1089 CRISPR screens.
DR ChiTaRS; NCDN; human.
DR GeneWiki; NCDN; -.
DR GenomeRNAi; 23154; -.
DR Pharos; Q9UBB6; Tbio.
DR PRO; PR:Q9UBB6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UBB6; protein.
DR Bgee; ENSG00000020129; Expressed in middle frontal gyrus and 131 other tissues.
DR ExpressionAtlas; Q9UBB6; baseline and differential.
DR Genevisible; Q9UBB6; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Cytoplasm;
KW Disease variant; Endosome; Epilepsy; Intellectual disability; Lipoprotein;
KW Membrane; Methylation; Palmitate; Phosphoprotein; Reference proteome;
KW Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..729
FT /note="Neurochondrin"
FT /id="PRO_0000324617"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
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..17
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032315"
FT VARIANT 392
FT /note="V -> E (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs753974779)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_039849"
FT VARIANT 392
FT /note="V -> L (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_039850"
FT VARIANT 433
FT /note="E -> Q (in NEDIES; unknown pathological
FT significance; in the neuroblastoma cell line SH-SY5Y, in
FT which NCDN has been knocked out, does not rescue impaired
FT neurite formation following retinoic acid treatment,
FT contrary to wild-type; no effect on phosphorylation of
FT ERK1/ERK2)"
FT /evidence="ECO:0000269|PubMed:33711248"
FT /id="VAR_085876"
FT VARIANT 478
FT /note="R -> Q (in NEDIES; in the neuroblastoma cell line
FT SH-SY5Y, in which NCDN has been knocked out, does not
FT rescue impaired neurite formation following retinoic acid
FT treatment, contrary to wild-type; no effect on
FT phosphorylation of ERK1/ERK2)"
FT /evidence="ECO:0000269|PubMed:33711248"
FT /id="VAR_085877"
FT VARIANT 498
FT /note="W -> R (in NEDIES; in the neuroblastoma cell line
FT SH-SY5Y, in which NCDN has been knocked out, does not
FT rescue impaired neurite formation following retinoic acid
FT treatment, contrary to wild-type; in these cells,
FT associated with markedly decreased phosphorylation of ERK1/
FT ERK2, compared to wild-type, suggesting impaired GRM5
FT activation)"
FT /evidence="ECO:0000269|PubMed:33711248"
FT /id="VAR_085878"
FT VARIANT 652
FT /note="P -> L (in NEDIES; in the neuroblastoma cell line
FT SH-SY5Y, in which NCDN has been knocked out, does not
FT rescue impaired neurite formation following retinoic acid
FT treatment, contrary to wild-type; in these cells,
FT associated with markedly decreased phosphorylation of ERK1/
FT ERK2, compared to wild-type, suggesting impaired GRM5
FT activation)"
FT /evidence="ECO:0000269|PubMed:33711248"
FT /id="VAR_085879"
FT INIT_MET Q9UBB6-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q9UBB6-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 729 AA; 78864 MW; FA8D46B06CE1F5AB CRC64;
MSCCDLAAAG QLGKASIMAS DCEPALNQAE GRNPTLERYL GALREAKNDS EQFAALLLVT
KAVKAGDIDA KTRRRIFDAV GFTFPNRLLT TKEAPDGCPD HVLRALGVAL LACFCSDPEL
AAHPQVLNKI PILSTFLTAR GDPDDAARRS MIDDTYQCLT AVAGTPRGPR HLIAGGTVSA
LCQAYLGHGY GFDQALALLV GLLAAAETQC WKEAEPDLLA VLRGLSEDFQ KAEDASKFEL
CQLLPLFLPP TTVPPECYRD LQAGLARILG SKLSSWQRNP ALKLAARLAH ACGSDWIPAG
SSGSKFLALL VNLACVEVRL ALEETGTEVK EDVVTACYAL MELGIQECTR CEQSLLKEPQ
KVQLVSVMKE AIGAVIHYLL QVGSEKQKEP FVFASVRILG AWLAEETSSL RKEVCQLLPF
LVRYAKTLYE EAEEANDLSQ QVANLAISPT TPGPTWPGDA LRLLLPGWCH LTVEDGPREI
LIKEGAPSLL CKYFLQQWEL TSPGHDTSVL PDSVEIGLQT CCHIFLNLVV TAPGLIKRDA
CFTSLMNTLM TSLPALVQQQ GRLLLAANVA TLGLLMARLL STSPALQGTP ASRGFFAAAI
LFLSQSHVAR ATPGSDQAVL ALSPEYEGIW ADLQELWFLG MQAFTGCVPL LPWLAPAALR
SRWPQELLQL LGSVSPNSVK PEMVAAYQGV LVELARANRL CREAMRLQAG EETASHYRMA
ALEQCLSEP
