WDR1_DROME
ID WDR1_DROME Reviewed; 608 AA.
AC Q9VU68; Q8IQJ6;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Actin-interacting protein 1;
DE Short=AIP1;
DE AltName: Full=Protein flare;
GN Name=flr; ORFNames=CG10724;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17565945; DOI=10.1534/genetics.107.072959;
RA Ren N., Charlton J., Adler P.N.;
RT "The flare gene, which encodes the AIP1 protein of Drosophila, functions to
RT regulate F-actin disassembly in pupal epidermal cells.";
RL Genetics 176:2223-2234(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Induces disassembly of actin filaments in conjunction with
CC ADF/cofilin family proteins. Essential for organismal and cell
CC viability. Required for the development of normal wing cell planar
CC polarity. {ECO:0000269|PubMed:17565945}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17565945}. Note=At the cell periphery of wing
CC cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9VU68-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9VU68-2; Sequence=VSP_036571;
CC -!- TISSUE SPECIFICITY: Expressed in pupal wing cells.
CC {ECO:0000269|PubMed:17565945}.
CC -!- DISRUPTION PHENOTYPE: Pupals exhibit grossly abnormal epidermal hairs
CC on wings, an abnormal accumulation of F-actin and microtubules, and
CC disruption of the frizzled-based planar cell polarity system.
CC {ECO:0000269|PubMed:17565945}.
CC -!- SIMILARITY: Belongs to the WD repeat AIP1 family. {ECO:0000305}.
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DR EMBL; AE014296; AAF49822.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11835.1; -; Genomic_DNA.
DR EMBL; AY061340; AAL28888.1; -; mRNA.
DR RefSeq; NP_648642.1; NM_140385.4. [Q9VU68-1]
DR RefSeq; NP_729891.1; NM_168543.2. [Q9VU68-2]
DR AlphaFoldDB; Q9VU68; -.
DR SMR; Q9VU68; -.
DR BioGRID; 64849; 10.
DR DIP; DIP-18795N; -.
DR IntAct; Q9VU68; 4.
DR STRING; 7227.FBpp0075581; -.
DR PaxDb; Q9VU68; -.
DR PRIDE; Q9VU68; -.
DR DNASU; 39505; -.
DR EnsemblMetazoa; FBtr0075845; FBpp0075581; FBgn0260049. [Q9VU68-1]
DR EnsemblMetazoa; FBtr0075846; FBpp0075582; FBgn0260049. [Q9VU68-2]
DR GeneID; 39505; -.
DR KEGG; dme:Dmel_CG10724; -.
DR UCSC; CG10724-RA; d. melanogaster.
DR CTD; 797829; -.
DR FlyBase; FBgn0260049; flr.
DR VEuPathDB; VectorBase:FBgn0260049; -.
DR eggNOG; KOG0318; Eukaryota.
DR GeneTree; ENSGT00390000009416; -.
DR HOGENOM; CLU_015246_1_0_1; -.
DR InParanoid; Q9VU68; -.
DR OMA; TNPAKHT; -.
DR PhylomeDB; Q9VU68; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR BioGRID-ORCS; 39505; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39505; -.
DR PRO; PR:Q9VU68; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0260049; Expressed in crop (Drosophila) and 34 other tissues.
DR ExpressionAtlas; Q9VU68; baseline and differential.
DR Genevisible; Q9VU68; DM.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030042; P:actin filament depolymerization; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:UniProtKB.
DR GO; GO:0035317; P:imaginal disc-derived wing hair organization; IMP:FlyBase.
DR GO; GO:0040011; P:locomotion; IBA:GO_Central.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IGI:FlyBase.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0030834; P:regulation of actin filament depolymerization; IMP:UniProtKB.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08662; eIF2A; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Developmental protein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..608
FT /note="Actin-interacting protein 1"
FT /id="PRO_0000051346"
FT REPEAT 62..101
FT /note="WD 1"
FT REPEAT 106..149
FT /note="WD 2"
FT REPEAT 150..190
FT /note="WD 3"
FT REPEAT 193..232
FT /note="WD 4"
FT REPEAT 237..276
FT /note="WD 5"
FT REPEAT 323..362
FT /note="WD 6"
FT REPEAT 366..403
FT /note="WD 7"
FT REPEAT 444..483
FT /note="WD 8"
FT REPEAT 487..526
FT /note="WD 9"
FT REPEAT 531..570
FT /note="WD 10"
FT REPEAT 575..607
FT /note="WD 11"
FT VAR_SEQ 1..12
FT /note="MAQPQPPAYENK -> MSQQAKNE (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_036571"
SQ SEQUENCE 608 AA; 66550 MW; A43F0BC8EA0AE123 CRC64;
MAQPQPPAYE NKNIYATLPR TQRGQPIVLG ADPKGKNFLY TNGNSVIIRN IENPAIADVY
TEHSCAVNVA KYSPSGFYIA SGDASGKIRI WDTVNKEHLL KNEFQPIAGP IKDISWSPDN
QRIVAVGEGR ERFGHVFMSE TGTSVGEISG QSKSINSADF RPARPFRIVT GSEDNTIAVF
EGPPFKFKMT KQDHSRFVQA VRYSPDGKFF ASAGFDGKVF LYDGTSSELV GEFGSPAHKG
GVYALAWKPD STQLLTCSGD KTCRLWTVES RELVSEFVMG TTVDDQQVSC LWQGDNLITV
SLSGVITYLN VADPSKPLRV VKGHNKPITV LGLSDDRSTI YTGSHDGVVT NWNSGSGTND
RITGTGHGNQ INGIAAWGDF VYTCGIDDSL RQFSVEGNSY TDYVVKLNCQ PRGLAILRNE
NIIALACIKE LTLVQDQKKI FSLPIKYEAS SIAVNADTSD VAVGGDDQKL HIYTLKGGVL
EPKVELDHLG AVTDVSYSPD LKYLVACDAH RKVVLYSVEE YKPAHNKEWG FHSARVNTVA
WSPNSLLVAS GSLDTTIIIW SVANPAKHTI IKNAHPQSQI TRLVWLDNNT VISTGQDCNT
KVWHVENI
