WDR1_MOUSE
ID WDR1_MOUSE Reviewed; 606 AA.
AC O88342;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=WD repeat-containing protein 1;
DE AltName: Full=Actin-interacting protein 1;
DE Short=AIP1;
GN Name=Wdr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10036186; DOI=10.1006/geno.1998.5672;
RA Adler H.J., Winnicki R.S., Gong T.-W.L., Lomax M.I.;
RT "A gene upregulated in the acoustically damaged chick basilar papilla
RT encodes a novel WD40 repeat protein.";
RL Genomics 56:59-69(1999).
RN [2]
RP PROTEIN SEQUENCE OF 44-65 AND 162-180, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17515402; DOI=10.1182/blood-2006-10-055087;
RA Kile B.T., Panopoulos A.D., Stirzaker R.A., Hacking D.F., Tahtamouni L.H.,
RA Willson T.A., Mielke L.A., Henley K.J., Zhang J.G., Wicks I.P.,
RA Stevenson W.S., Nurden P., Watowich S.S., Justice M.J.;
RT "Mutations in the cofilin partner Aip1/Wdr1 cause autoinflammatory disease
RT and macrothrombocytopenia.";
RL Blood 110:2371-2380(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95 AND LYS-480, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP FUNCTION.
RX PubMed=24840128; DOI=10.1016/j.ajpath.2014.04.007;
RA Yuan B., Wan P., Chu D., Nie J., Cao Y., Luo W., Lu S., Chen J., Yang Z.;
RT "A cardiomyocyte-specific Wdr1 knockout demonstrates essential functional
RT roles for actin disassembly during myocardial growth and maintenance in
RT mice.";
RL Am. J. Pathol. 184:1967-1980(2014).
RN [8]
RP FUNCTION.
RX PubMed=25915128; DOI=10.1038/ncb3146;
RA Luxenburg C., Heller E., Pasolli H.A., Chai S., Nikolova M., Stokes N.,
RA Fuchs E.;
RT "Wdr1-mediated cell shape dynamics and cortical tension are essential for
RT epidermal planar cell polarity.";
RL Nat. Cell Biol. 17:592-604(2015).
CC -!- FUNCTION: Induces disassembly of actin filaments in conjunction with
CC ADF/cofilin family proteins (By similarity). Enhances cofilin-mediated
CC actin severing (PubMed:25915128). Involved in cytokinesis. Involved in
CC chemotactic cell migration by restricting lamellipodial membrane
CC protrusions (By similarity). Involved in myocardium sarcomere
CC organization. Required for cardiomyocyte growth at the postnatal and
CC maintenance at the adult stage (PubMed:24840128). Involved in
CC neutrophil actin dynamics and migration. Involved in megakaryocyte
CC maturation and platelet shedding (PubMed:17515402). Required for the
CC establishment of planar cell polarity (PCP) during follicular
CC epithelium development and for cell shape changes during PCP; the
CC function seems to implicate cooperation with CFL1 and/or DSTN/ADF.
CC Involved in the generation/maintenance of cortical tension
CC (PubMed:25915128). Involved in assembly and maintenance of epithelial
CC apical cell junctions and plays a role in the organization of the
CC perijunctional actomyosin belt (By similarity).
CC {ECO:0000250|UniProtKB:O75083, ECO:0000250|UniProtKB:Q9W7F2,
CC ECO:0000269|PubMed:24840128, ECO:0000269|PubMed:25915128}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q5RKI0}. Cell projection, podosome
CC {ECO:0000250|UniProtKB:O75083}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. Partial deficiencies disrupt
CC megakaryocyte maturation, platelet shedding and provoke neutrophilic
CC autoinflammatory disease. {ECO:0000269|PubMed:17515402}.
CC -!- SIMILARITY: Belongs to the WD repeat AIP1 family. {ECO:0000305}.
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DR EMBL; AF020055; AAD05043.1; -; mRNA.
DR CCDS; CCDS51485.1; -.
DR RefSeq; NP_035845.1; NM_011715.2.
DR AlphaFoldDB; O88342; -.
DR SMR; O88342; -.
DR BioGRID; 204554; 25.
DR IntAct; O88342; 13.
DR MINT; O88342; -.
DR STRING; 10090.ENSMUSP00000005234; -.
DR iPTMnet; O88342; -.
DR PhosphoSitePlus; O88342; -.
DR SwissPalm; O88342; -.
DR REPRODUCTION-2DPAGE; IPI00314748; -.
DR REPRODUCTION-2DPAGE; O88342; -.
DR UCD-2DPAGE; O88342; -.
DR CPTAC; non-CPTAC-3680; -.
DR CPTAC; non-CPTAC-3955; -.
DR EPD; O88342; -.
DR jPOST; O88342; -.
DR PaxDb; O88342; -.
DR PeptideAtlas; O88342; -.
DR PRIDE; O88342; -.
DR ProteomicsDB; 297939; -.
DR Antibodypedia; 22867; 169 antibodies from 30 providers.
DR DNASU; 22388; -.
DR Ensembl; ENSMUST00000005234; ENSMUSP00000005234; ENSMUSG00000005103.
DR GeneID; 22388; -.
DR KEGG; mmu:22388; -.
DR UCSC; uc033ije.1; mouse.
DR CTD; 9948; -.
DR MGI; MGI:1337100; Wdr1.
DR VEuPathDB; HostDB:ENSMUSG00000005103; -.
DR eggNOG; KOG0318; Eukaryota.
DR GeneTree; ENSGT00390000009416; -.
DR HOGENOM; CLU_015246_3_0_1; -.
DR InParanoid; O88342; -.
DR OMA; TNPAKHT; -.
DR OrthoDB; 325552at2759; -.
DR PhylomeDB; O88342; -.
DR TreeFam; TF300821; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 22388; 24 hits in 71 CRISPR screens.
DR ChiTaRS; Wdr1; mouse.
DR PRO; PR:O88342; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O88342; protein.
DR Bgee; ENSMUSG00000005103; Expressed in ankle joint and 257 other tissues.
DR ExpressionAtlas; O88342; baseline and differential.
DR Genevisible; O88342; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0030043; P:actin filament fragmentation; IMP:UniProtKB.
DR GO; GO:0043297; P:apical junction assembly; ISO:MGI.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0042247; P:establishment of planar polarity of follicular epithelium; IMP:UniProtKB.
DR GO; GO:0040011; P:locomotion; IBA:GO_Central.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; ISO:MGI.
DR GO; GO:0002446; P:neutrophil mediated immunity; IMP:UniProtKB.
DR GO; GO:1990266; P:neutrophil migration; IMP:UniProtKB.
DR GO; GO:0030220; P:platelet formation; IMP:UniProtKB.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IGI:MGI.
DR GO; GO:0030834; P:regulation of actin filament depolymerization; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0048713; P:regulation of oligodendrocyte differentiation; ISO:MGI.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:MGI.
DR GO; GO:0045214; P:sarcomere organization; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
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 Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50974; SSF50974; 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_0000051342"
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:0007744|PubMed:23806337"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75083"
FT MOD_RES 238
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 480
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 606 AA; 66407 MW; 573CEA1DCD7CA80E CRC64;
MPYEIKKVFA SLPQVERGVS KILGGDPKGD HFLYTNGKCV ILRNIDNPAI ADIYTEHAHQ
VVVAKYAPSG FYIASGDISG KLRIWDTTQK EHLLKYEYQP FAGKIKDIAW TEDSKRIAVV
GEGREKFGAV FLWDTGSSVG EITGHNKVIN SVDIKQTRPY RLATGSDDNC AAFFEGPPFK
FKFTIGDHSR FVNCVRFSPD GNRFATASAD GQIFIYDGKT GEKVCALGES KAHDGGIYAI
SWSPDSTHLL SASGDKTSKI WDVNVNSVVS TFPMGSNVLD QQLGCLWQKD HLLSISLSGY
INYLDKNNPS KPLRVIKGHS KSIQCLTVHR NGGKSYIYSG SHDGHINYWD SETGENDSFS
GKGHTNQVSR MTVNESEQLV SCSMDDTVRY TNLTLRDYSG QGVVKLDVQP KCVAVGPGGY
TVVVCIGQIV LLKDQKKCFS IDNPGYEPEV VAVHPGGDTV AVGGTDGNVR VYSILASTLK
DEGKLLEAKG PVTDVAYSHD GAFLAVCDAS KVVTVFSVAD GYSENNVFYG HHAKIVCLAW
SPDNEHFASG GMDMMVYVWT LSDPETKVKI QDAHRLHHVS SLAWLDEHTL VTTSHDASVK
EWTITY
