LOCUS NDEL1_RAT 345 aa linear ROD 29-MAY-2024
DEFINITION RecName: Full=Nuclear distribution protein nudE-like 1;
Short=Protein Nudel.
ACCESSION Q78PB6
VERSION Q78PB6.1
DBSOURCE UniProtKB: locus NDEL1_RAT, accession Q78PB6;
class: standard.
extra accessions:Q6IRI4
created: Jun 13, 2006.
sequence updated: Jul 5, 2004.
annotation updated: May 29, 2024.
xrefs: AY008298.1, AAG21830.1, BC070909.1, AAH70909.1, NP_579854.1,
XP_006246640.1, 2V71_A, 2V71_B
xrefs (non-sequence databases): PDBsum:2V71, AlphaFoldDB:Q78PB6,
SMR:Q78PB6, IntAct:Q78PB6, MINT:Q78PB6,
STRING:10116.ENSRNOP00000005574, iPTMnet:Q78PB6,
PhosphoSitePlus:Q78PB6, jPOST:Q78PB6,
PaxDb:10116-ENSRNOP00000005574, Ensembl:ENSRNOT00000005574.8,
Ensembl:ENSRNOP00000005574.6, Ensembl:ENSRNOG00000004139.9,
GeneID:170845, KEGG:rno:170845, UCSC:RGD:621235, AGR:RGD:621235,
CTD:81565, RGD:621235, VEuPathDB:HostDB:ENSRNOG00000004139,
eggNOG:KOG1853, GeneTree:ENSGT00390000000111,
HOGENOM:CLU_057872_0_0_1, InParanoid:Q78PB6, OrthoDB:2910907at2759,
PhylomeDB:Q78PB6, TreeFam:TF325693, Reactome:R-RNO-141444,
Reactome:R-RNO-2467813, Reactome:R-RNO-2500257,
Reactome:R-RNO-5663220, Reactome:R-RNO-68877,
Reactome:R-RNO-9648025, EvolutionaryTrace:Q78PB6, PRO:PR:Q78PB6,
Proteomes:UP000002494, Bgee:ENSRNOG00000004139, GO:0030424,
GO:1904115, GO:0043203, GO:0044297, GO:0031252, GO:0090724,
GO:0005813, GO:0005871, GO:0000776, GO:0005874, GO:0005875,
GO:0005815, GO:0060053, GO:0005635, GO:0005819, GO:0008021,
GO:0043014, GO:0048487, GO:0042802, GO:0008017, GO:0070012,
GO:0044877, GO:0016477, GO:0021955, GO:0051642, GO:0021799,
GO:0007059, GO:0051303, GO:0000132, GO:0001833, GO:0008286,
GO:0032418, GO:0000226, GO:0007020, GO:0007100, GO:0060052,
GO:0001764, GO:0031175, GO:1990138, GO:0051081, GO:0045773,
GO:0048680, GO:1900029, GO:0140650, GO:0033157, GO:0010975,
GO:0008090, GO:0047496, Gene3D:6.10.250.1080, InterPro:IPR033494,
InterPro:IPR006964, PANTHER:PTHR10921, PANTHER:PTHR10921:SF0,
Pfam:PF04880
KEYWORDS 3D-structure; Alternative splicing; Centromere; Chromosome; Coiled
coil; Cytoplasm; Cytoskeleton; Developmental protein;
Differentiation; Kinetochore; Lipoprotein; Microtubule;
Neurogenesis; Palmitate; Phosphoprotein; Reference proteome;
Transport.
SOURCE Rattus norvegicus (Norway rat)
ORGANISM Rattus norvegicus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
REFERENCE 1 (residues 1 to 345)
AUTHORS Umezu,M., Kitagawa,M., Aoki,J. and Arai,H.
TITLE Direct Submission
JOURNAL Submitted (??-SEP-2000) to the EMBL/GenBank/DDBJ databases
REMARK NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).;
STRAIN=Sprague-Dawley; TISSUE=Liver
REFERENCE 2 (residues 1 to 345)
AUTHORS Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
Makowski,K.A., Bosak,S. and Malek,J.
CONSRTM MGC Project Team
TITLE The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC)
JOURNAL Genome Res 14 (10B), 2121-2127 (2004)
PUBMED 15489334
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).;
TISSUE=Heart
Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
Morin, Ryan]]
REFERENCE 3 (residues 1 to 345)
AUTHORS Niethammer,M., Smith,D.S., Ayala,R., Peng,J., Ko,J., Lee,M.S.,
Morabito,M. and Tsai,L.H.
TITLE NUDEL is a novel Cdk5 substrate that associates with LIS1 and
cytoplasmic dynein
JOURNAL Neuron 28 (3), 697-711 (2000)
PUBMED 11163260
REMARK INTERACTION WITH PAFAH1B1 AND DYNEIN, AND SUBCELLULAR LOCATION.;
TISSUE=Brain
REFERENCE 4 (residues 1 to 345)
AUTHORS Hayashi,M.A., Portaro,F.C., Bastos,M.F., Guerreiro,J.R.,
Oliveira,V., Gorrao,S.S., Tambourgi,D.V., Sant'Anna,O.A.,
Whiting,P.J., Camargo,L.M., Konno,K., Brandon,N.J. and Camargo,A.C.
TITLE Inhibition of NUDEL (nuclear distribution
element-like)-oligopeptidase activity by disrupted-in-schizophrenia
1
JOURNAL Proc Natl Acad Sci U S A 102 (10), 3828-3833 (2005)
PUBMED 15728732
REMARK PUTATIVE FUNCTION AS AN OLIGOPEPTIDASE.
REFERENCE 5 (residues 1 to 345)
AUTHORS Kamiya,A., Tomoda,T., Chang,J., Takaki,M., Zhan,C., Morita,M.,
Cascio,M.B., Elashvili,S., Koizumi,H., Takanezawa,Y., Dickerson,F.,
Yolken,R., Arai,H. and Sawa,A.
TITLE DISC1-NDEL1/NUDEL protein interaction, an essential component for
neurite outgrowth, is modulated by genetic variations of DISC1
JOURNAL Hum Mol Genet 15 (22), 3313-3323 (2006)
PUBMED 17035248
REMARK FUNCTION, INTERACTION WITH DISC1, INDUCTION, AND SUBCELLULAR
LOCATION.
REFERENCE 6 (residues 1 to 345)
AUTHORS Lundby,A., Secher,A., Lage,K., Nordsborg,N.B., Dmytriyev,A.,
Lundby,C. and Olsen,J.V.
TITLE Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues
JOURNAL Nat Commun 3, 876 (2012)
PUBMED 22673903
REMARK PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Publication Status: Online-Only
COMMENT On Jun 13, 2006 this sequence version replaced gi:81884834.
[FUNCTION] Required for organization of the cellular microtubule
array and microtubule anchoring at the centrosome. May regulate
microtubule organization at least in part by targeting the
microtubule severing protein KATNA1 to the centrosome. Also
positively regulates the activity of the minus-end directed
microtubule motor protein dynein. May enhance dynein-mediated
microtubule sliding by targeting dynein to the microtubule plus
ends. Required for several dynein- and microtubule-dependent
processes such as the maintenance of Golgi integrity, the
centripetal motion of secretory vesicles and the coupling of the
nucleus and centrosome. Also required during brain development for
the migration of newly formed neurons from the
ventricular/subventricular zone toward the cortical plate. Required
for mitosis in some cell types but appears to be dispensible for
mitosis in cortical neuronal progenitors, which instead requires
NDE1. Facilitates the polymerization of neurofilaments from the
individual subunits NEFH and NEFL. Positively regulates lysosome
peripheral distribution and ruffled border formation in osteoclasts
(By similarity). Plays a role, together with DISC1, in the
regulation of neurite outgrowth. {ECO:0000250,
ECO:0000250|UniProtKB:Q9ERR1, ECO:0000269|PubMed:17035248}.
[SUBUNIT] Self-associates. Interacts with dynactin, tubulin gamma,
KATNA1, KATNB1, microtubules, PCM1, PCNT, and YWHAE. Interacts
directly with NEFL and indirectly with NEFH. Interacts (via
C-terminus) with CENPF. Interacts with DISC1, dynein and PAFAH1B1.
Interacts with ZNF365. Interacts with PLEKHM1 (via N- and
C-terminus). {ECO:0000250, ECO:0000250|UniProtKB:Q9ERR1}.
[SUBCELLULAR LOCATION] Cytoplasm, cytoskeleton. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome.
Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton,
spindle. Note=Localizes to the mitotic spindle and to the
microtubules of the manchette in elongated spermatids (By
similarity). Localizes to the interphase centrosome. Localizes to
the cell body of the motor neurons and colocalizes with assembled
neurofilaments within axonal processes. Colocalizes with DISC1 in
the perinuclear region, including the centrosome. {ECO:0000250}.
[ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
isoforms=2; Name=1; IsoId=Q78PB6-1; Sequence=Displayed; Name=2;
IsoId=Q78PB6-2; Sequence=VSP_019312, VSP_019313.
[INDUCTION] Up-regulated during neurite outgrowth upon
differentiation with NGF. {ECO:0000269|PubMed:17035248}.
[PTM] Phosphorylated in mitosis. Can be phosphorylated by CDK1,
CDK5 and MAPK1. Phosphorylation by CDK5 promotes interaction with
KATNA1 and YWHAE (By similarity). {ECO:0000250}.
[PTM] Palmitoylation at Cys-273 reduces affinity for dynein.
{ECO:0000250}.
[SIMILARITY] Belongs to the nudE family. {ECO:0000305}.
[CAUTION] Was originally thought to function as an oligopeptidase
(NUDEL-oligopeptidase or endooligopeptidase A) which could regulate
peptide levels relevant to brain function.
{ECO:0000305|PubMed:15728732}.
FEATURES Location/Qualifiers
source 1..345
/organism="Rattus norvegicus"
/db_xref="taxon:10116"
gene 1..345
/gene="Ndel1"
/gene_synonym="Nude2"
/gene_synonym="Nudel"
Protein 1..345
/product="Nuclear distribution protein nudE-like 1"
/note="Protein Nudel"
/UniProtKB_evidence="Evidence at protein level"
Region 1..345
/region_name="Mature chain"
/note="Nuclear distribution protein nudE-like 1.
/id=PRO_0000240215."
Region 12..164
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:2V71."
Region <27..>195
/region_name="Smc"
/note="Chromosome segregation ATPase Smc [Cell cycle
control, cell division, chromosome partitioning]; COG1196"
/db_xref="CDD:440809"
Region 28..190
/region_name="Coiled-coil region"
/note="/evidence=ECO:0000255."
Region 42
/region_name="Conflict"
/note="E -> Q (in Ref. 2; AAH70909).
/evidence=ECO:0000305."
Region 56..166
/region_name="Region of interest in the sequence"
/note="Self-association. /evidence=ECO:0000250."
Region 64..189
/region_name="Region of interest in the sequence"
/note="Interaction with KATNB1. /evidence=ECO:0000250."
Region 114..133
/region_name="Region of interest in the sequence"
/note="Required for interaction with PAFAH1B1.
/evidence=ECO:0000250."
Region 135..309
/region_name="NUDE_C"
/note="NUDE protein, C-terminal conserved region;
pfam04880"
/db_xref="CDD:461464"
Region 175..345
/region_name="Region of interest in the sequence"
/note="Interaction with CENPF. /evidence=ECO:0000250."
Region 189..256
/region_name="Region of interest in the sequence"
/note="Interaction with YWHAE. /evidence=ECO:0000250."
Region 191..345
/region_name="Region of interest in the sequence"
/note="Interaction with NEFL. /evidence=ECO:0000250."
Region 195..256
/region_name="Region of interest in the sequence"
/note="Interaction with KATNA1. /evidence=ECO:0000250."
Site 215
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q9GZM8."
Region 217..240
/region_name="Region of interest in the sequence"
/note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
Site 219
/site_type="phosphorylation"
/note="Phosphothreonine; by CDK1 and MAPK1.
/evidence=ECO:0000250|UniProtKB:Q9GZM8."
Region 227..278
/region_name="Region of interest in the sequence"
/note="Interaction with DISC1. /evidence=ECO:0000250."
Site 231
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q9GZM8."
Site 242
/site_type="phosphorylation"
/note="Phosphoserine; by CDK1.
/evidence=ECO:0000250|UniProtKB:Q9GZM8."
Site 245
/site_type="phosphorylation"
/note="Phosphothreonine; by CDK1 and MAPK1.
/evidence=ECO:0000250|UniProtKB:Q9GZM8."
Region 256..291
/region_name="Region of interest in the sequence"
/note="Required for localization to the centrosome and
interaction with dynein, dynactin, tubulin gamma, PCM1 and
PCNT. /evidence=ECO:0000250."
Site 273
/site_type="lipid-binding"
/note="S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7.
/evidence=ECO:0000250."
Region 314..345
/region_name="Region of interest in the sequence"
/note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
Region 316..328
/region_name="Splicing variant"
/note="AVNGFDPAPPPPG -> QEKVIFPTLFMGQ (in isoform 2).
/evidence=ECO:0000303|PubMed:15489334. /id=VSP_019312."
Region 329..345
/region_name="Splicing variant"
/note="Missing (in isoform 2).
/evidence=ECO:0000303|PubMed:15489334. /id=VSP_019313."
Site 344
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:22673903."
ORIGIN
1 mdgedipdfs slkeetaywk elslkykqsf qeardelvef qegsreleae leaqlvqaeq
61 rnrdlqadnq rlkyevealk eklehqyaqs ykqvsvledd lsqtraikeq lhkyvreleq
121 anddlerakr ativsledfe qrlnqaiern afleseldek esllvsvqrl kdeardlrqe
181 lavrerqqev trksapsspt ldcekmdsav qaslslpatp vgkgtensfp spkaipngfg
241 tspltpsari salnivgdll rkvgaleskl aacrnfakdq asrksyvpgs vncgvmnsng
301 pecprsgrat ffhkgavngf dpappppglg ssrpssapgm lplsv
//