NDEL1_RABIT
ID NDEL1_RABIT Reviewed; 345 AA.
AC O46480;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 3.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Nuclear distribution protein nudE-like 1;
DE Short=Protein Nudel;
GN Name=NDEL1; Synonyms=EOPA;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PUTATIVE FUNCTION AS AN OLIGOPEPTIDASE, AND
RP TISSUE SPECIFICITY.
RX PubMed=10694468; DOI=10.1006/bbrc.2000.2243;
RA Hayashi M.A.F., Portaro F.C.V., Tambourgi D.V., Sucupira M., Yamane T.,
RA Fernandes B.L., Ferro E.S., Reboucas N.A., de Camargo A.C.M.;
RT "Molecular and immunochemical evidences demonstrate that endooligopeptidase
RT A is the predominant cytosolic oligopeptidase of rabbit brain.";
RL Biochem. Biophys. Res. Commun. 269:7-13(2000).
RN [2]
RP ERRATUM OF PUBMED:10694468.
RA Hayashi M.A.F., Portaro F.C.V., Tambourgi D.V., Sucupira M., Yamane T.,
RA Fernandes B.L., Ferro E.S., Reboucas N.A., de Camargo A.C.M.;
RL Biochem. Biophys. Res. Commun. 272:309-309(2000).
RN [3]
RP SEQUENCE REVISION.
RA Hayashi M.A.F., Reboucas N.A., Tambourgi D.V., Ferro E.S., Fernandes B.L.,
RA Sucupira M., de Camargo A.C.M.;
RL Submitted (APR-2001) 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. Plays a
CC role, together with DISC1, in the regulation of neurite outgrowth.
CC Required for mitosis in some cell types but appears to be dispensible
CC for mitosis in cortical neuronal progenitors, which instead requires
CC NDE1. Facilitates the polymerization of neurofilaments from the
CC individual subunits NEFH and NEFL. Positively regulates lysosome
CC peripheral distribution and ruffled border formation in osteoclasts (By
CC similarity). {ECO:0000250, 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. Colocalizes with DISC1 in the perinuclear region,
CC including the centrosome. Localizes to the kinetochore in a CENPF-
CC dependent manner (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in heart, hypothalamus,
CC liver, lung, spleen and stomach. Expressed at higher levels in testis
CC and brain. Within the brain, expressed in cerebellum, cerebral stem,
CC cortex and striatum. {ECO:0000269|PubMed:10694468}.
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 -!- CAUTION: Was originally thought to function as an oligopeptidase
CC (NUDEL-oligopeptidase or endooligopeptidase A) which could regulate
CC peptide levels relevant to brain function.
CC {ECO:0000305|PubMed:10694468}.
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DR EMBL; AF015037; AAB99905.3; -; mRNA.
DR PIR; PC7064; PC7064.
DR RefSeq; NP_001075489.1; NM_001082020.1.
DR AlphaFoldDB; O46480; -.
DR SMR; O46480; -.
DR STRING; 9986.ENSOCUP00000014285; -.
DR PRIDE; O46480; -.
DR GeneID; 100008657; -.
DR KEGG; ocu:100008657; -.
DR CTD; 81565; -.
DR eggNOG; KOG1853; Eukaryota.
DR InParanoid; O46480; -.
DR OrthoDB; 1082224at2759; -.
DR Proteomes; UP000001811; 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 1: Evidence at protein 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..345
FT /note="Nuclear distribution protein nudE-like 1"
FT /id="PRO_0000240214"
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..345
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..345
FT /note="Interaction with NEFL"
FT /evidence="ECO:0000250"
FT REGION 195..256
FT /note="Interaction with KATNA1"
FT /evidence="ECO:0000250"
FT REGION 217..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..278
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 316..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 27..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 344
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 345 AA; 38449 MW; 3C4D93EE58C09B96 CRC64;
MDGEDIPDFS SLKEETAYWK ELSLKYKQTF QEARDELVEF QEGSRELEAE LEAQLVQAEQ
RNRDLQADNQ RLKYEVEALK EKLEHQYAQS YKQVSVLEDD LSQTRAIKEQ LHKYVRELEQ
ANDDLERAKR ATIVSLEDFE QRLNQAIERN AFLESELDEK ESLLVSVQRL KDEARDLRQE
LAVRERQQEV TRKSAPSSPT LDCEKMDSAV QASLSLPATP VGKGTENSFP SPKAIPNGFG
TSPLTPSARI SALNIVGDLL RKVGALESKL AACRNFAKDQ ASRKSYISGN VNCGVMNSNG
TKFSRSGHTS FFDKGAVNGF DPAPPPPGLG SSRPLSAPGM LPLSV
