NEDD1_ARATH
ID NEDD1_ARATH Reviewed; 782 AA.
AC B3H5K9; B6EUA6; Q9FI89;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Protein NEDD1 {ECO:0000303|PubMed:19383896};
DE AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 1 homolog {ECO:0000303|PubMed:19383896};
DE AltName: Full=Protein GCP-WD {ECO:0000303|PubMed:25438942};
GN Name=NEDD1 {ECO:0000303|PubMed:19383896};
GN Synonyms=GCP-WD {ECO:0000303|PubMed:25438942};
GN OrderedLocusNames=At5g05970 {ECO:0000312|Araport:AT5G05970};
GN ORFNames=K18J17.16 {ECO:0000312|EMBL:BAB10802.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19383896; DOI=10.1105/tpc.109.065953;
RA Zeng C.J., Lee Y.R., Liu B.;
RT "The WD40 repeat protein NEDD1 functions in microtubule organization during
RT cell division in Arabidopsis thaliana.";
RL Plant Cell 21:1129-1140(2009).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25438942; DOI=10.1016/j.cub.2014.09.013;
RA Walia A., Nakamura M., Moss D., Kirik V., Hashimoto T., Ehrhardt D.W.;
RT "GCP-WD mediates gamma-TuRC recruitment and the geometry of microtubule
RT nucleation in interphase arrays of Arabidopsis.";
RL Curr. Biol. 24:2548-2555(2014).
CC -!- FUNCTION: Regulates microtubules organization in a centrosome-
CC independent manner. Required for the spindle to be positioned correctly
CC and for the function of gamma-tubulin in organizing phragmoplast
CC microtubules (PubMed:19383896). Component of active gamma-tubulin ring
CC complexes (gamma-TuRCs) associated with cortical microtubules in
CC interphase cells (PubMed:25438942). Mediates gamma-TuRC recruitment to
CC the nucleation sites and is important for determining the ratio of
CC branched to parallel nucleation (PubMed:25438942). May mediate the
CC localization of GCP2 and GCP3 to the nuclear envelope
CC (PubMed:19383896). {ECO:0000269|PubMed:19383896,
CC ECO:0000269|PubMed:25438942}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:19383896,
CC ECO:0000269|PubMed:25438942}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:19383896}. Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:19383896}. Cytoplasm, cytoskeleton, microtubule
CC organizing center {ECO:0000269|PubMed:25438942}. Note=First detected in
CC prophase on the nuclear envelope, where it appeared to cap the future
CC spindle poles. Later detected along kinetochore microtubules (MTs) of
CC the metaphase spindle, with more prominent signals toward the poles. In
CC anaphase, detected with the shortening kinetochore fibers. In the
CC developing phragmoplast, localized mainly toward the minus end of MTs.
CC {ECO:0000269|PubMed:19383896}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B3H5K9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B3H5K9-2; Sequence=VSP_057697;
CC -!- TISSUE SPECIFICITY: Expressed in root meristematic cells.
CC {ECO:0000269|PubMed:19383896}.
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous. Compromised asymmetric
CC mitotic division in dividing microspores resulting in abortion of
CC gametogenesis. {ECO:0000269|PubMed:19383896}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AY093770; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB10802.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB017060; BAB10802.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90947.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90948.1; -; Genomic_DNA.
DR EMBL; AY093770; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001119176.1; NM_001125704.1. [B3H5K9-1]
DR RefSeq; NP_196216.2; NM_120679.3. [B3H5K9-2]
DR AlphaFoldDB; B3H5K9; -.
DR SMR; B3H5K9; -.
DR STRING; 3702.AT5G05970.2; -.
DR iPTMnet; B3H5K9; -.
DR PaxDb; B3H5K9; -.
DR PRIDE; B3H5K9; -.
DR ProteomicsDB; 238517; -. [B3H5K9-1]
DR EnsemblPlants; AT5G05970.1; AT5G05970.1; AT5G05970. [B3H5K9-2]
DR EnsemblPlants; AT5G05970.2; AT5G05970.2; AT5G05970. [B3H5K9-1]
DR GeneID; 830483; -.
DR Gramene; AT5G05970.1; AT5G05970.1; AT5G05970. [B3H5K9-2]
DR Gramene; AT5G05970.2; AT5G05970.2; AT5G05970. [B3H5K9-1]
DR KEGG; ath:AT5G05970; -.
DR Araport; AT5G05970; -.
DR TAIR; locus:2153629; AT5G05970.
DR eggNOG; KOG4378; Eukaryota.
DR InParanoid; B3H5K9; -.
DR OMA; RHLKYSS; -.
DR OrthoDB; 234690at2759; -.
DR PhylomeDB; B3H5K9; -.
DR PRO; PR:B3H5K9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B3H5K9; baseline and differential.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005828; C:kinetochore microtubule; IDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0140496; F:gamma-tubulin complex binding; IEA:InterPro.
DR GO; GO:0000919; P:cell plate assembly; IMP:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:TAIR.
DR GO; GO:0010968; P:regulation of microtubule nucleation; IEA:InterPro.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:TAIR.
DR GO; GO:2000694; P:regulation of phragmoplast microtubule organization; IMP:TAIR.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR044621; NEDD1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR45096; PTHR45096; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; Kinetochore; Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..782
FT /note="Protein NEDD1"
FT /id="PRO_0000433252"
FT REPEAT 1..34
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 41..80
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 90..130
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 133..172
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 176..216
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 220..260
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 262..301
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 307..358
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REGION 350..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 753..782
FT /evidence="ECO:0000255"
FT COMPBIAS 350..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 689
FT /note="Missing (in isoform 2)"
FT /id="VSP_057697"
SQ SEQUENCE 782 AA; 84757 MW; 384F0F6A5DC5EFCD CRC64;
MMSNLVEPSW RLLAASGGDT VKLFDVSADS GDPCVLSYTP SPGCAVNSVK WNHTNLVVAS
TGEDKKISLW RKNGQSLGTV PVTGKDGGDS AEECLSAISF SKKGSRYICS GGTGQIVKIW
DLQRKLCIKK LKGHTSTITG VMYNCKDEHL ASVSVGGDLI VHNLASGARA TELKDPNGQV
LRLLDYSRSS RHLLVTAGDD GTVHLWDTTG RSPKMSWLKQ HSAPTAGVCF SPSNEKIIAS
VGMDKKLYTY DSGSRRSSSC IAYEAPFSSL AFGDNGYILV AGTSNGRVVF YDIRGKPQPV
TVLHAFSNSE DVTSLSWQTS KPVIVNEKNY TSEMALLGST VEDSVVIPDP LPSTTPSASQ
SAMAPGSRGV SASTVNASSV EQTPNRNHLW PSGPLGRLHA LRANDSYNDD MGVFSPIIDV
SSVEKWADSE GYNNKDHLVV DNKPSSLLFP SSSKGYSFGD NGSKEHPIFD WKPSSTSKQD
DPRAAFSSFG SITPTASSKS EDSALTPPEA WGGDKFSEKF NQLANEKFSD KFSHLHAPSR
LAVSSTGAST SGSMFSSSRD FPLSHGQTNF ANASLEFPRI RDFSSTFETS STQTDNNLPS
SPLFTKGITA PGNIDSLRLS PNFTRRFSTY AERISTTSSF SDGASLSLGG SPKIKKTGSE
TREEVLNHLL ARPETVVATE AGAMPLMNQG GLKQSQTDQQ QVMGSSNFTL QLFQRTLEGT
LDSFQNSIHD DVRNLHIEIL RQFHMHEMEM SKVLSSILEN QAEQMKELKL LRKENQELRQ
RL
