NEDD1_BOVIN
ID NEDD1_BOVIN Reviewed; 659 AA.
AC Q3B7M6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein NEDD1;
DE AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 1;
DE Short=NEDD-1;
GN Name=NEDD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for mitosis progression. Promotes the nucleation of
CC microtubules from the spindle. {ECO:0000250|UniProtKB:Q8NHV4}.
CC -!- SUBUNIT: Interacts with FAM29A. Interacts with HSPA1A and HSPA1B.
CC Interacts with gamma-tubulin in a HSPA1A/B-dependent manner.
CC {ECO:0000250|UniProtKB:Q8NHV4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q8NHV4}.
CC -!- PTM: During mitosis, prior phosphorylation on Thr-549 by CDK1 promotes
CC subsequent phosphorylation by PLK1 on Thr-382, Ser-426 and Ser-636.
CC Phosphorylated NEDD1 can interact with gamma-tubulin for targeting the
CC gamma-tubulin ring complex (gTuRC) to the centrosome, an important step
CC for spindle formation. {ECO:0000250|UniProtKB:Q8NHV4}.
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DR EMBL; BC107541; AAI07542.1; -; mRNA.
DR RefSeq; NP_001030410.1; NM_001035333.2.
DR AlphaFoldDB; Q3B7M6; -.
DR SMR; Q3B7M6; -.
DR STRING; 9913.ENSBTAP00000002464; -.
DR PaxDb; Q3B7M6; -.
DR PRIDE; Q3B7M6; -.
DR Ensembl; ENSBTAT00000002464; ENSBTAP00000002464; ENSBTAG00000001894.
DR GeneID; 519463; -.
DR KEGG; bta:519463; -.
DR CTD; 121441; -.
DR VEuPathDB; HostDB:ENSBTAG00000001894; -.
DR VGNC; VGNC:31982; NEDD1.
DR eggNOG; KOG4378; Eukaryota.
DR GeneTree; ENSGT00390000001561; -.
DR HOGENOM; CLU_415014_0_0_1; -.
DR InParanoid; Q3B7M6; -.
DR OMA; RHLKYSS; -.
DR OrthoDB; 234690at2759; -.
DR TreeFam; TF329816; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000001894; Expressed in oocyte and 107 other tissues.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0000242; C:pericentriolar material; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..659
FT /note="Protein NEDD1"
FT /id="PRO_0000246163"
FT REPEAT 1..31
FT /note="WD 1"
FT REPEAT 32..71
FT /note="WD 2"
FT REPEAT 75..114
FT /note="WD 3"
FT REPEAT 117..156
FT /note="WD 4"
FT REPEAT 160..200
FT /note="WD 5"
FT REPEAT 204..244
FT /note="WD 6"
FT REPEAT 246..285
FT /note="WD 7"
FT REPEAT 289..332
FT /note="WD 8"
FT REGION 383..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 382
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8NHV4"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHV4"
FT MOD_RES 426
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8NHV4"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHV4"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHV4"
FT MOD_RES 549
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q8NHV4"
FT MOD_RES 636
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8NHV4"
SQ SEQUENCE 659 AA; 71204 MW; 3B5E69997BE5D158 CRC64;
MQENLRFASS GDDVKIWDAS SMTLVDKFNP HTAPHAISSV CWSSNNNFLV TASSSGDKIV
VSSCKCKPVP LLELGEGQKQ TCVSLNSTSM YLVSGGLNNT VNIWDLKSKR VHRSLKDHKD
EVTCVTYNWN DCYIASGSLS GEIILHSVTT NLSSTPFGHG SNQSIRHLKY SLFKKSLLGS
VSDNGIVTLW DVNSQSPYHN FDSTHKAPAS GICFSPVNEL LFVTVGLDKR IILYDTSSKK
LVKTLVADAP LTAVDFMPDG ATLAIGSSRG KIYQYDLRML KSPIKTISAH KTSVQCIAFQ
YSTVLSKSGL NKGCSNKPTA VNKRTANVSA GGGGAQNPGV VREAATTSIA TVPPQPTAAA
VGKGAVAPQD KAGLPRSINT DTLSKEAESG KNQDFSNFDD SGKSSLGDMF SPVRDDAVVS
KGGDESIGKG DGLDFLPQLN SVFPPRKNPV VSSTSVLHSS PLNVFMGSPG KEENENHDLT
AESKKMYLGK QESKDSFKQF AKLISGAETG NLNASPSSNQ TRSPEKFEKP EKEIEAQLIN
EPPGNGSSTP NPKIASSVTA GVAGSLSEKI VDTIGNSRPN APLSSVQIRF IQNMIQETLD
DFREACHRDI VNLQVEMIKQ FHMQLNEMHS LLERYSVNEG LVAEIERLRE ENKRLRAHF
