WDR1_RAT
ID WDR1_RAT Reviewed; 606 AA.
AC Q5RKI0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=WD repeat-containing protein 1;
GN Name=Wdr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Noone T.E., Hubberstey A.V.;
RT "Human WDR1 interacts with actin and is involved in cell attachment and
RT cytoskeletal rearrangement.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 44-81; 127-147; 162-180; 204-219; 290-306 AND 490-534,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15337274; DOI=10.1016/j.neulet.2004.06.053;
RA Shin D.H., Lee E., Chung Y.H., Mun G.H., Park J., Lomax M.I., Oh S.H.;
RT "Subcellular localization of WD40 repeat 1 protein in PC12 rat
RT pheochromocytoma cells.";
RL Neurosci. Lett. 367:399-403(2004).
CC -!- FUNCTION: Induces disassembly of actin filaments in conjunction with
CC ADF/cofilin family proteins. Enhances cofilin-mediated actin severing.
CC Involved in cytokinesis. Involved in chemotactic cell migration by
CC restricting lamellipodial membrane protrusions. Involved in myocardium
CC sarcomere organization. Required for cardiomyocyte growth and
CC maintenance. Involved in megakaryocyte maturation and platelet
CC shedding. Required for the establishment of planar cell polarity (PCP)
CC during follicular epithelium development and for cell shape changes
CC during PCP; the function seems to implicate cooperation with CFL1
CC and/or DSTN/ADF. Involved in the generation/maintenance of cortical
CC tension. Involved in assembly and maintenance of epithelial apical cell
CC junctions and plays a role in the organization of the perijunctional
CC actomyosin belt (By similarity). {ECO:0000250|UniProtKB:O75083,
CC ECO:0000250|UniProtKB:O88342}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15337274}. Cell projection, podosome
CC {ECO:0000250|UniProtKB:O75083}.
CC -!- SIMILARITY: Belongs to the WD repeat AIP1 family. {ECO:0000305}.
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DR EMBL; AY986483; AAX94056.1; -; mRNA.
DR EMBL; BC085864; AAH85864.1; -; mRNA.
DR RefSeq; NP_001014157.1; NM_001014135.1.
DR AlphaFoldDB; Q5RKI0; -.
DR SMR; Q5RKI0; -.
DR BioGRID; 262322; 3.
DR STRING; 10116.ENSRNOP00000024012; -.
DR iPTMnet; Q5RKI0; -.
DR PhosphoSitePlus; Q5RKI0; -.
DR SwissPalm; Q5RKI0; -.
DR World-2DPAGE; 0004:Q5RKI0; -.
DR jPOST; Q5RKI0; -.
DR PaxDb; Q5RKI0; -.
DR PRIDE; Q5RKI0; -.
DR Ensembl; ENSRNOT00000024012; ENSRNOP00000024012; ENSRNOG00000028498.
DR GeneID; 360950; -.
DR KEGG; rno:360950; -.
DR CTD; 9948; -.
DR RGD; 1305789; Wdr1.
DR eggNOG; KOG0318; Eukaryota.
DR GeneTree; ENSGT00390000009416; -.
DR HOGENOM; CLU_015246_3_0_1; -.
DR InParanoid; Q5RKI0; -.
DR OMA; TNPAKHT; -.
DR OrthoDB; 325552at2759; -.
DR PhylomeDB; Q5RKI0; -.
DR TreeFam; TF300821; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR PRO; PR:Q5RKI0; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000028498; Expressed in colon and 19 other tissues.
DR Genevisible; Q5RKI0; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0030043; P:actin filament fragmentation; ISO:RGD.
DR GO; GO:0043297; P:apical junction assembly; ISO:RGD.
DR GO; GO:0030865; P:cortical cytoskeleton organization; ISO:RGD.
DR GO; GO:0042247; P:establishment of planar polarity of follicular epithelium; ISO:RGD.
DR GO; GO:0040011; P:locomotion; IBA:GO_Central.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; ISO:RGD.
DR GO; GO:0002446; P:neutrophil mediated immunity; ISO:RGD.
DR GO; GO:1990266; P:neutrophil migration; ISO:RGD.
DR GO; GO:0030220; P:platelet formation; ISO:RGD.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISO:RGD.
DR GO; GO:0030834; P:regulation of actin filament depolymerization; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:0048713; P:regulation of oligodendrocyte differentiation; IDA:MGI.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:RGD.
DR GO; GO:0045214; P:sarcomere organization; ISO:RGD.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011045; N2O_reductase_N.
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; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50974; SSF50974; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cell junction; Cell projection; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..606
FT /note="WD repeat-containing protein 1"
FT /id="PRO_0000271365"
FT REPEAT 4..45
FT /note="WD 1"
FT REPEAT 48..87
FT /note="WD 2"
FT REPEAT 93..135
FT /note="WD 3"
FT REPEAT 138..176
FT /note="WD 4"
FT REPEAT 180..218
FT /note="WD 5"
FT REPEAT 224..263
FT /note="WD 6"
FT REPEAT 270..306
FT /note="WD 7"
FT REPEAT 311..351
FT /note="WD 8"
FT REPEAT 358..408
FT /note="WD 9"
FT REPEAT 432..474
FT /note="WD 10"
FT REPEAT 480..518
FT /note="WD 11"
FT REPEAT 523..561
FT /note="WD 12"
FT REPEAT 566..604
FT /note="WD 13"
FT MOD_RES 28
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75083"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75083"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75083"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75083"
FT MOD_RES 238
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75083"
FT MOD_RES 480
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75083"
SQ SEQUENCE 606 AA; 66181 MW; 9A3A08A7235EE993 CRC64;
MPYEIKKVFA SLPQVERGVS KILGGDPKGD NFLYTNGKCV ILRNIDNPAV ADIYTEHAHQ
VVVAKYAPSG FYIASGDISG KLRIWDTTQK EHILKYEYQP FAGKIKDIAW TEDSKRIAVV
GEGREKFGAV FLWDTGSSVG EITGHNKVIN SVDIKQNRPY RLATGSDDNC AAFFEGPPFK
FKFTIGDHSR FVNCVRFSPD GNRFATASAD GQIFIYDGKT GEKVCALGGS KAHDGGIYAI
SWSPDSTHLL SASGDKTSKI WDVNVNSVVS TFPMGSNVLD QQLGCLWQKD HLLSISLSGY
INYLDKNNPS KPLRVIKGHS KSIQCLTVHK NGGKSYIYSG SHDGHINYWD SETGENDSFS
GKGHTNQVSR MTVDESGQLV SCSMDDTVRY TNLTLRDYSG QGVVKLDVQP KCVAVGPGGY
TVVVCIGQIV LLKDQKKCFS IDNPGYEPEV VAVHPGGDTV AVGGSDGNVR VYSILGATLK
DEGKLLEAKG PVTDLAYSHD GAFLAVCDAS KVVTVFSVAD GYSENNVFYG HHAKIVCLAW
SPDNEHFASG GMDMMVYVWT LSDPETKVKI QDAHRLHHVS SLAWLDEHTL VTTSHDASVK
EWTITY
