NDEL1_MACFA
ID NDEL1_MACFA Reviewed; 347 AA.
AC Q4R4S6;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Nuclear distribution protein nudE-like 1;
DE Short=Protein Nudel;
GN Name=NDEL1; Synonyms=NUDEL; ORFNames=QflA-10529;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for organization of the cellular microtubule array
CC and microtubule anchoring at the centrosome. May regulate microtubule
CC organization at least in part by targeting the microtubule severing
CC protein KATNA1 to the centrosome. Also positively regulates the
CC activity of the minus-end directed microtubule motor protein dynein.
CC May enhance dynein-mediated microtubule sliding by targeting dynein to
CC the microtubule plus ends. Required for several dynein- and
CC microtubule-dependent processes such as the maintenance of Golgi
CC integrity, the centripetal motion of secretory vesicles and the
CC coupling of the nucleus and centrosome. Also required during brain
CC development for the migration of newly formed neurons from the
CC ventricular/subventricular zone toward the cortical plate. Required for
CC mitosis in some cell types but appears to be dispensible for mitosis in
CC cortical neuronal progenitors, which instead requires NDE1. Facilitates
CC the polymerization of neurofilaments from the individual subunits NEFH
CC and NEFL. Positively regulates lysosome peripheral distribution and
CC ruffled border formation in osteoclasts (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9ERR1}.
CC -!- SUBUNIT: Self-associates. Interacts with DISC1, dynein, dynactin,
CC tubulin gamma, KATNA1, KATNB1, microtubules, PAFAH1B1, PCM1, PCNT, and
CC YWHAE. Interacts directly with NEFL and indirectly with NEFH. Interacts
CC (via C-terminus) with CENPF. Interacts with ZNF365. Interacts with
CC PLEKHM1 (via N- and C-terminus). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9ERR1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Note=Localizes to the interphase
CC centrosome and the mitotic spindle. Localizes to the cell body of the
CC motor neurons and colocalizes with assembled neurofilaments within
CC axonal processes. Localizes to the microtubules of the manchette in
CC elongated spermatids. Localizes to the kinetochore in a CENPF-dependent
CC manner (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated in mitosis. Can be phosphorylated by CDK1, CDK5 and
CC MAPK1. Phosphorylation by CDK5 promotes interaction with KATNA1 and
CC YWHAE (By similarity). {ECO:0000250}.
CC -!- PTM: Palmitoylation at Cys-273 reduces affinity for dynein.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE01899.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB169818; BAE01899.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q4R4S6; -.
DR SMR; Q4R4S6; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0007100; P:mitotic centrosome separation; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IEA:InterPro.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISS:UniProtKB.
DR InterPro; IPR033493; NDEL1.
DR InterPro; IPR033494; NUDE.
DR InterPro; IPR006964; NUDE_dom.
DR PANTHER; PTHR10921; PTHR10921; 1.
DR PANTHER; PTHR10921:SF0; PTHR10921:SF0; 1.
DR Pfam; PF04880; NUDE_C; 1.
PE 2: Evidence at transcript level;
KW Centromere; Chromosome; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Kinetochore; Lipoprotein;
KW Microtubule; Neurogenesis; Palmitate; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..347
FT /note="Nuclear distribution protein nudE-like 1"
FT /id="PRO_0000240211"
FT REGION 56..166
FT /note="Self-association"
FT /evidence="ECO:0000250"
FT REGION 64..189
FT /note="Interaction with KATNB1"
FT /evidence="ECO:0000250"
FT REGION 114..133
FT /note="Required for interaction with PAFAH1B1"
FT /evidence="ECO:0000250"
FT REGION 175..347
FT /note="Interaction with CENPF"
FT /evidence="ECO:0000250"
FT REGION 189..256
FT /note="Interaction with YWHAE"
FT /evidence="ECO:0000250"
FT REGION 191..347
FT /note="Interaction with NEFL"
FT /evidence="ECO:0000250"
FT REGION 195..256
FT /note="Interaction with KATNA1"
FT /evidence="ECO:0000250"
FT REGION 241..280
FT /note="Interaction with DISC1"
FT /evidence="ECO:0000250"
FT REGION 256..291
FT /note="Required for localization to the centrosome and
FT interaction with dynein, dynactin, tubulin gamma, PCM1 and
FT PCNT"
FT /evidence="ECO:0000250"
FT REGION 314..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..190
FT /evidence="ECO:0000255"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZM8"
FT MOD_RES 219
FT /note="Phosphothreonine; by CDK1 and MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q9GZM8"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZM8"
FT MOD_RES 242
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9GZM8"
FT MOD_RES 245
FT /note="Phosphothreonine; by CDK1 and MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q9GZM8"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q78PB6"
FT LIPID 273
FT /note="S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7"
FT /evidence="ECO:0000250"
SQ SEQUENCE 347 AA; 38587 MW; 8C3F21269394CDB6 CRC64;
MDGEDIPDFS SLKEETAYWK ELSLKYKQSF QEARDELVEF QEGSRELEAE LEAQLVQAEQ
RNRDLQADNQ RLKYEVEALK EKLEHQYAQS YKQVSVLEDD LSQTRAIKEQ LHKYVRELEQ
ANDDLERAKR ATIVSLEDFE QRLNQAIERN AFLESELDEK ESLLVSVQRL KDEARDLRQE
LAVRERQQEV TRKSAPSSPT LDCEKMDSAV QASLSLPATP VGKGTENTFP SPKAIPNGFG
TSPLTPSARI SALNIVGDLL RKVGALESKL AACRNFAKDQ ASRKSYISGN VNCGVLNGNG
TKFSRSGHTS FFDKGAVNGF DPAPPPPDPG LGSSRPSSAP GMLPLSV
