NUD2_CAEEL
ID NUD2_CAEEL Reviewed; 293 AA.
AC O45717;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein nud-2 {ECO:0000305};
GN Name=nud-2 {ECO:0000303|PubMed:16996038, ECO:0000312|WormBase:R11A5.2};
GN ORFNames=R11A5.2 {ECO:0000312|WormBase:R11A5.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH LIS-1, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16996038; DOI=10.1016/j.brainres.2006.08.067;
RA Locke C.J., Williams S.N., Schwarz E.M., Caldwell G.A., Caldwell K.A.;
RT "Genetic interactions among cortical malformation genes that influence
RT susceptibility to convulsions in C. elegans.";
RL Brain Res. 1120:23-34(2006).
RN [3] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH LIS-1, INTERACTION WITH UNC-83,
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 239-LYS--ALA-293.
RX PubMed=20005871; DOI=10.1016/j.ydbio.2009.12.004;
RA Fridolfsson H.N., Ly N., Meyerzon M., Starr D.A.;
RT "UNC-83 coordinates kinesin-1 and dynein activities at the nuclear envelope
RT during nuclear migration.";
RL Dev. Biol. 338:237-250(2010).
RN [4]
RP FUNCTION.
RX PubMed=27697906; DOI=10.1242/dev.141192;
RA Bone C.R., Chang Y.T., Cain N.E., Murphy S.P., Starr D.A.;
RT "Nuclei migrate through constricted spaces using microtubule motors and
RT actin networks in C. elegans hypodermal cells.";
RL Development 143:4193-4202(2016).
CC -!- FUNCTION: Part of a complex with lis-1, which is recruited to the
CC nuclear envelope by unc-83, where, in turn, it recruits dynein to the
CC nuclear surface and regulates nuclear migration in hypodermal precursor
CC cells (PubMed:20005871, PubMed:27697906). Plays a role in GABAergic
CC synaptic vesicle localization in the ventral nerve cord
CC (PubMed:16996038). {ECO:0000269|PubMed:16996038,
CC ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:27697906}.
CC -!- SUBUNIT: Component of a dynein-regulating complex composed of at least
CC lis-1 and nud-2 (PubMed:20005871). Interacts with lis-1; the
CC interaction is direct (PubMed:16996038). Interacts (via C-terminus)
CC with unc-83; the interaction is direct, and is required for recruitment
CC of nud-2 to the nuclear envelope (PubMed:20005871).
CC {ECO:0000269|PubMed:16996038, ECO:0000269|PubMed:20005871}.
CC -!- INTERACTION:
CC O45717; Q20398: magu-4; NbExp=4; IntAct=EBI-326083, EBI-322716;
CC O45717; Q23064-3: unc-83; NbExp=5; IntAct=EBI-326083, EBI-2902257;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:20005871}.
CC Note=Recruited to the nuclear envelope by unc-83.
CC {ECO:0000269|PubMed:20005871}.
CC -!- TISSUE SPECIFICITY: Expressed in ventral cord neurons, the pharynx,
CC seam cells of the hypodermis and in vulval muscle cells.
CC {ECO:0000269|PubMed:16996038}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in viable
CC animals, but a small, but significant number of animals have nuclear
CC migration defects in hyp7 hypodermal precursor cells (PubMed:20005871).
CC RNAi-mediated knockdown results in an abnormal distribution of
CC GABAergic synaptic vesicles at synaptic termini of the ventral nerve
CC cord (PubMed:16996038). RNAi-mediated knockdown in combination with
CC exposure to pentylenetetrazole, a GABA antagonist that induces
CC seizures, results in impaired locomotion, stiffened appearance and an
CC increased convulsion incidence as compared to wild-type animals
CC (PubMed:16996038). {ECO:0000269|PubMed:16996038,
CC ECO:0000269|PubMed:20005871}.
CC -!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}.
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DR EMBL; BX284601; CAB05597.1; -; Genomic_DNA.
DR PIR; T24165; T24165.
DR RefSeq; NP_492172.1; NM_059771.4.
DR AlphaFoldDB; O45717; -.
DR SMR; O45717; -.
DR ComplexPortal; CPX-1389; lis-1-nud-2 microtubule-associated dynein motor complex.
DR IntAct; O45717; 6.
DR STRING; 6239.R11A5.2; -.
DR EPD; O45717; -.
DR PaxDb; O45717; -.
DR PeptideAtlas; O45717; -.
DR EnsemblMetazoa; R11A5.2.1; R11A5.2.1; WBGene00011230.
DR GeneID; 172554; -.
DR KEGG; cel:CELE_R11A5.2; -.
DR UCSC; R11A5.2; c. elegans.
DR CTD; 172554; -.
DR WormBase; R11A5.2; CE12724; WBGene00011230; nud-2.
DR eggNOG; KOG1853; Eukaryota.
DR GeneTree; ENSGT00390000000111; -.
DR HOGENOM; CLU_918979_0_0_1; -.
DR InParanoid; O45717; -.
DR OMA; SCVNRIV; -.
DR OrthoDB; 1300183at2759; -.
DR PhylomeDB; O45717; -.
DR PRO; PR:O45717; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00011230; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; IC:ComplexPortal.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0051642; P:centrosome localization; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051303; P:establishment of chromosome localization; IBA:GO_Central.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0007100; P:mitotic centrosome separation; IBA:GO_Central.
DR GO; GO:0007097; P:nuclear migration; IMP:WormBase.
DR GO; GO:0031022; P:nuclear migration along microfilament; IMP:ComplexPortal.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IMP:WormBase.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:WormBase.
DR GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
DR InterPro; IPR033494; NUDE.
DR PANTHER; PTHR10921; PTHR10921; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Reference proteome.
FT CHAIN 1..293
FT /note="Protein nud-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000443516"
FT REGION 239..293
FT /note="Required for interaction with unc-83 isoform c"
FT /evidence="ECO:0000269|PubMed:20005871"
FT COILED 36..147
FT /evidence="ECO:0000255"
FT MUTAGEN 239..293
FT /note="Missing: Abolishes interaction with unc-83 isoform
FT c."
FT /evidence="ECO:0000269|PubMed:20005871"
SQ SEQUENCE 293 AA; 34265 MW; 84E075C3DC96C3D9 CRC64;
MDLSEDQIRG LPHHELLGHF LQMREEFNEF QTSSAEIEKM MDSELDDLKT QLKKAETRVQ
QMTTEQIRNK DRQDDSRVQF AQVEEQLRRE NSHLHEQCES QRERIRKLEQ RNDVLETSER
NKEYLASDLG SKLDHAIEKI AMLESELYER QVAAEEMHRL REEQLRTTER PRLIVEPLRN
DPEILPDEPS PGPSKEEFKM SSEDVFMEDV QHHEDVRMEE TIAKIDEVRI DDNKNIQEKS
QRVSTGTGAG ACINRIVKDL MTKVERLDSI LSTIRVSNNS SNNNSSHLTT TRA
