WDR1_HUMAN
ID WDR1_HUMAN Reviewed; 606 AA.
AC O75083; A8K6E9; A8MPU4; O75313; Q8N6E5; Q9UG05; Q9UG78; Q9UQE0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=WD repeat-containing protein 1;
DE AltName: Full=Actin-interacting protein 1;
DE Short=AIP1;
DE AltName: Full=NORI-1;
GN Name=WDR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lymphoid tissue;
RA Abe Y., Nezu K., Ueda N.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP VAL-185.
RC TISSUE=Colon, Eye, and Mammary gland;
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 [6]
RP PROTEIN SEQUENCE OF 2-17 (ISOFORMS 1/2).
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-606 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP PROTEIN SEQUENCE OF 290-306 (ISOFORMS 1/2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [10]
RP FUNCTION.
RX PubMed=15629458; DOI=10.1016/j.bbrc.2004.11.156;
RA Fujibuchi T., Abe Y., Takeuchi T., Imai Y., Kamei Y., Murase R., Ueda N.,
RA Shigemoto K., Yamamoto H., Kito K.;
RT "AIP1/WDR1 supports mitotic cell rounding.";
RL Biochem. Biophys. Res. Commun. 327:268-275(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP FUNCTION.
RX PubMed=18494608; DOI=10.1042/bj20071655;
RA Kato A., Kurita S., Hayashi A., Kaji N., Ohashi K., Mizuno K.;
RT "Critical roles of actin-interacting protein 1 in cytokinesis and
RT chemotactic migration of mammalian cells.";
RL Biochem. J. 414:261-270(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28; LYS-81; LYS-95; LYS-115 AND
RP LYS-480, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=22721921; DOI=10.1016/j.ejcb.2012.05.005;
RA Cervero P., Himmel M., Kruger M., Linder S.;
RT "Proteomic analysis of podosome fractions from macrophages reveals
RT similarities to spreading initiation centres.";
RL Eur. J. Cell Biol. 91:908-922(2012).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25792565; DOI=10.1152/ajpgi.00446.2014;
RA Lechuga S., Baranwal S., Ivanov A.I.;
RT "Actin-interacting protein 1 controls assembly and permeability of
RT intestinal epithelial apical junctions.";
RL Am. J. Physiol. 308:G745-G756(2015).
RN [20]
RP INVOLVEMENT IN PFITS, VARIANTS PFITS LYS-7 DEL; ASN-26; ARG-121; VAL-286
RP AND MET-424, AND FUNCTION.
RX PubMed=27557945; DOI=10.1182/blood-2016-03-706028;
RA Kuhns D.B., Fink D.L., Choi U., Sweeney C., Lau K., Priel D.L., Riva D.,
RA Mendez L., Uzel G., Freeman A.F., Olivier K.N., Anderson V.L., Currens R.,
RA Mackley V., Kang A., Al-Adeli M., Mace E., Orange J.S., Kang E.,
RA Lockett S.J., Chen D., Steinbach P.J., Hsu A.P., Zarember K.A.,
RA Malech H.L., Gallin J.I., Holland S.M.;
RT "Cytoskeletal abnormalities and neutrophil dysfunction in WDR1
RT deficiency.";
RL Blood 128:2135-2143(2016).
RN [21]
RP INVOLVEMENT IN PFITS, VARIANT PFITS PHE-293, CHARACTERIZATION OF VARIANT
RP PFITS PHE-293, AND SUBCELLULAR LOCATION.
RX PubMed=27994071; DOI=10.1084/jem.20161228;
RA Standing A.S., Malinova D., Hong Y., Record J., Moulding D., Blundell M.P.,
RA Nowak K., Jones H., Omoyinmi E., Gilmour K.C., Medlar A., Stanescu H.,
RA Kleta R., Anderson G., Nanthapisal S., Gomes S.M., Klein N.,
RA Eleftheriou D., Thrasher A.J., Brogan P.A.;
RT "Autoinflammatory periodic fever, immunodeficiency, and thrombocytopenia
RT (PFIT) caused by mutation in actin-regulatory gene WDR1.";
RL J. Exp. Med. 214:59-71(2017).
RN [22]
RP INVOLVEMENT IN PFITS, VARIANTS PFITS GLN-145; SER-501 AND VAL-572,
RP CHARACTERIZATION OF VARIANTS PFITS GLN-145; SER-501 AND VAL-572, FUNCTION,
RP AND TISSUE SPECIFICITY.
RX PubMed=29751004; DOI=10.1016/j.jaci.2018.04.023;
RA Pfajfer L., Mair N.K., Jimenez-Heredia R., Genel F., Gulez N., Ardeniz O.,
RA Hoeger B., Bal S.K., Madritsch C., Kalinichenko A., Chandra Ardy R.,
RA Gerceker B., Rey-Barroso J., Ijspeert H., Tangye S.G., Simonitsch-Klupp I.,
RA Huppa J.B., van der Burg M., Dupre L., Boztug K.;
RT "Mutations affecting the actin regulator WD repeat-containing protein 1
RT lead to aberrant lymphoid immunity.";
RL J. Allergy Clin. Immunol. 142:1589-1604(2018).
CC -!- FUNCTION: Induces disassembly of actin filaments in conjunction with
CC ADF/cofilin family proteins (PubMed:15629458, PubMed:27557945,
CC PubMed:29751004). Enhances cofilin-mediated actin severing (By
CC similarity). Involved in cytokinesis. Involved in chemotactic cell
CC migration by restricting lamellipodial membrane protrusions
CC (PubMed:18494608). Involved in myocardium sarcomere organization.
CC Required for cardiomyocyte growth and maintenance (By similarity).
CC Involved in megakaryocyte maturation and platelet shedding. Required
CC for the 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 (By
CC similarity). Involved in assembly and maintenance of epithelial apical
CC cell junctions and plays a role in the organization of the
CC perijunctional actomyosin belt (PubMed:25792565).
CC {ECO:0000250|UniProtKB:O88342, ECO:0000250|UniProtKB:Q9W7F2,
CC ECO:0000269|PubMed:15629458, ECO:0000269|PubMed:18494608,
CC ECO:0000269|PubMed:25792565, ECO:0000269|PubMed:27557945,
CC ECO:0000269|PubMed:29751004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27994071}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5RKI0}. Cell
CC projection, podosome {ECO:0000269|PubMed:22721921}. Cell junction
CC {ECO:0000269|PubMed:25792565}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75083-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75083-3; Sequence=VSP_012926;
CC -!- TISSUE SPECIFICITY: Expressed in peripheral blood mononuclear cells (at
CC protein level). {ECO:0000269|PubMed:29751004}.
CC -!- DISEASE: Periodic fever, immunodeficiency, and thrombocytopenia
CC syndrome (PFITS) [MIM:150550]: An immunologic disorder with variable
CC manifestations including early-onset recurrent respiratory infections,
CC stomatitis, cutaneous infections, and neutropenia.
CC {ECO:0000269|PubMed:27557945, ECO:0000269|PubMed:27994071,
CC ECO:0000269|PubMed:29751004}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat AIP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD05045.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AF020056; AAD05044.1; -; mRNA.
DR EMBL; AF020260; AAD05045.1; ALT_SEQ; mRNA.
DR EMBL; AB010427; BAA31855.2; -; mRNA.
DR EMBL; AK291614; BAF84303.1; -; mRNA.
DR EMBL; AC005674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000201; AAH00201.1; -; mRNA.
DR EMBL; BC002489; AAH02489.1; -; mRNA.
DR EMBL; BC030541; AAH30541.1; -; mRNA.
DR EMBL; AL050108; CAB43276.1; -; mRNA.
DR EMBL; AL110208; CAB53674.2; -; mRNA.
DR CCDS; CCDS54739.1; -. [O75083-3]
DR CCDS; CCDS54740.1; -. [O75083-1]
DR PIR; T13152; T13152.
DR RefSeq; NP_005103.2; NM_005112.4. [O75083-3]
DR RefSeq; NP_059830.1; NM_017491.3. [O75083-1]
DR AlphaFoldDB; O75083; -.
DR SMR; O75083; -.
DR BioGRID; 115273; 171.
DR IntAct; O75083; 53.
DR MINT; O75083; -.
DR STRING; 9606.ENSP00000427687; -.
DR GlyGen; O75083; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75083; -.
DR MetOSite; O75083; -.
DR PhosphoSitePlus; O75083; -.
DR SwissPalm; O75083; -.
DR BioMuta; WDR1; -.
DR OGP; O75083; -.
DR REPRODUCTION-2DPAGE; IPI00746165; -.
DR REPRODUCTION-2DPAGE; O75083; -.
DR UCD-2DPAGE; O75083; -.
DR EPD; O75083; -.
DR jPOST; O75083; -.
DR MassIVE; O75083; -.
DR MaxQB; O75083; -.
DR PaxDb; O75083; -.
DR PeptideAtlas; O75083; -.
DR PRIDE; O75083; -.
DR ProteomicsDB; 49749; -. [O75083-1]
DR ProteomicsDB; 49750; -. [O75083-3]
DR TopDownProteomics; O75083-1; -. [O75083-1]
DR Antibodypedia; 22867; 169 antibodies from 30 providers.
DR DNASU; 9948; -.
DR Ensembl; ENST00000382451.6; ENSP00000371889.2; ENSG00000071127.17. [O75083-3]
DR Ensembl; ENST00000382452.6; ENSP00000371890.2; ENSG00000071127.17. [O75083-1]
DR Ensembl; ENST00000499869.7; ENSP00000427687.1; ENSG00000071127.17. [O75083-1]
DR Ensembl; ENST00000502702.5; ENSP00000426725.1; ENSG00000071127.17. [O75083-3]
DR GeneID; 9948; -.
DR KEGG; hsa:9948; -.
DR MANE-Select; ENST00000499869.7; ENSP00000427687.1; NM_017491.5; NP_059830.1.
DR UCSC; uc032tcf.2; human. [O75083-1]
DR CTD; 9948; -.
DR DisGeNET; 9948; -.
DR GeneCards; WDR1; -.
DR HGNC; HGNC:12754; WDR1.
DR HPA; ENSG00000071127; Low tissue specificity.
DR MalaCards; WDR1; -.
DR MIM; 150550; phenotype.
DR MIM; 604734; gene.
DR neXtProt; NX_O75083; -.
DR OpenTargets; ENSG00000071127; -.
DR PharmGKB; PA37358; -.
DR VEuPathDB; HostDB:ENSG00000071127; -.
DR eggNOG; KOG0318; Eukaryota.
DR GeneTree; ENSGT00390000009416; -.
DR HOGENOM; CLU_015246_3_0_1; -.
DR InParanoid; O75083; -.
DR OMA; TNPAKHT; -.
DR OrthoDB; 325552at2759; -.
DR PhylomeDB; O75083; -.
DR TreeFam; TF300821; -.
DR PathwayCommons; O75083; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; O75083; -.
DR BioGRID-ORCS; 9948; 585 hits in 1084 CRISPR screens.
DR ChiTaRS; WDR1; human.
DR GeneWiki; WDR1; -.
DR GenomeRNAi; 9948; -.
DR Pharos; O75083; Tbio.
DR PRO; PR:O75083; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O75083; protein.
DR Bgee; ENSG00000071127; Expressed in popliteal artery and 208 other tissues.
DR ExpressionAtlas; O75083; baseline and differential.
DR Genevisible; O75083; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0030043; P:actin filament fragmentation; IEA:Ensembl.
DR GO; GO:0043297; P:apical junction assembly; IDA:UniProtKB.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0042247; P:establishment of planar polarity of follicular epithelium; IEA:Ensembl.
DR GO; GO:0040011; P:locomotion; IBA:GO_Central.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IDA:UniProtKB.
DR GO; GO:0002446; P:neutrophil mediated immunity; IEA:Ensembl.
DR GO; GO:1990266; P:neutrophil migration; IEA:Ensembl.
DR GO; GO:0030220; P:platelet formation; IEA:Ensembl.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0030834; P:regulation of actin filament depolymerization; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0048713; P:regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
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; 4.
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; Alternative splicing; Cell junction;
KW Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Disease variant; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..606
FT /note="WD repeat-containing protein 1"
FT /id="PRO_0000051341"
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:0007744|PubMed:19608861"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 238
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 480
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 47..186
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012926"
FT VARIANT 7
FT /note="Missing (in PFITS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27557945"
FT /id="VAR_084593"
FT VARIANT 26
FT /note="D -> N (in PFITS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27557945"
FT /id="VAR_084594"
FT VARIANT 121
FT /note="G -> R (in PFITS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27557945"
FT /id="VAR_084595"
FT VARIANT 145
FT /note="H -> Q (in PFITS; unknown pathological significance;
FT almost complete loss of protein expression in peripheral
FT blood mononuclear cells)"
FT /evidence="ECO:0000269|PubMed:29751004"
FT /id="VAR_084596"
FT VARIANT 185
FT /note="I -> V (in dbSNP:rs13441)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_013445"
FT VARIANT 286
FT /note="L -> V (in PFITS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27557945"
FT /id="VAR_084597"
FT VARIANT 293
FT /note="L -> F (in PFITS; contrary to wild-type, which shows
FT a uniform distribution throughout the cytoplasm, forms
FT cytoplasmic aggregates, which contain pyrin/MEFV, hence
FT might trigger spontaneous inflammasome activation)"
FT /evidence="ECO:0000269|PubMed:27994071"
FT /id="VAR_084598"
FT VARIANT 424
FT /note="V -> M (in PFITS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27557945"
FT /id="VAR_084599"
FT VARIANT 501
FT /note="G -> S (in PFITS; unknown pathological significance;
FT almost complete loss of protein expression in peripheral
FT blood mononuclear cells)"
FT /evidence="ECO:0000269|PubMed:29751004"
FT /id="VAR_084600"
FT VARIANT 572
FT /note="D -> V (in PFITS; almost complete loss of protein
FT expression in peripheral blood mononuclear cells)"
FT /evidence="ECO:0000269|PubMed:29751004"
FT /id="VAR_084601"
SQ SEQUENCE 606 AA; 66194 MW; 8C08C31D5CD097F1 CRC64;
MPYEIKKVFA SLPQVERGVS KIIGGDPKGN NFLYTNGKCV ILRNIDNPAL ADIYTEHAHQ
VVVAKYAPSG FYIASGDVSG KLRIWDTTQK EHLLKYEYQP FAGKIKDIAW TEDSKRIAVV
GEGREKFGAV FLWDSGSSVG EITGHNKVIN SVDIKQSRPY RLATGSDDNC AAFFEGPPFK
FKFTIGDHSR FVNCVRFSPD GNRFATASAD GQIYIYDGKT GEKVCALGGS KAHDGGIYAI
SWSPDSTHLL SASGDKTSKI WDVSVNSVVS TFPMGSTVLD QQLGCLWQKD HLLSVSLSGY
INYLDRNNPS KPLHVIKGHS KSIQCLTVHK NGGKSYIYSG SHDGHINYWD SETGENDSFA
GKGHTNQVSR MTVDESGQLI SCSMDDTVRY TSLMLRDYSG QGVVKLDVQP KCVAVGPGGY
AVVVCIGQIV LLKDQRKCFS IDNPGYEPEV VAVHPGGDTV AIGGVDGNVR LYSILGTTLK
DEGKLLEAKG PVTDVAYSHD GAFLAVCDAS KVVTVFSVAD GYSENNVFYG HHAKIVCLAW
SPDNEHFASG GMDMMVYVWT LSDPETRVKI QDAHRLHHVS SLAWLDEHTL VTTSHDASVK
EWTITY
