DCAF1_DROME
ID DCAF1_DROME Reviewed; 1544 AA.
AC Q9W2F2; Q5U167; Q86PE6; Q8MT13;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein mahjong;
DE AltName: Full=DDB1- and CUL4-associated factor-like 1;
DE AltName: Full=VPRBP-like protein;
GN Name=mahj; ORFNames=CG10080;
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 [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 [2]
RP GENOME REANNOTATION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-565; SER-569 AND SER-955, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH L(2)GL.
RX PubMed=20644714; DOI=10.1371/journal.pbio.1000422;
RA Tamori Y., Bialucha C.U., Tian A.G., Kajita M., Huang Y.C., Norman M.,
RA Harrison N., Poulton J., Ivanovitch K., Disch L., Liu T., Deng W.M.,
RA Fujita Y.;
RT "Involvement of Lgl and Mahjong/VprBP in cell competition.";
RL PLoS Biol. 8:E1000422-E1000422(2010).
CC -!- FUNCTION: Probable substrate recognition component of tsome E3
CC ubiquitin-protein ligase complex (By similarity). Plays a key role in
CC cell competition via its interaction with l(2)gl. {ECO:0000250,
CC ECO:0000269|PubMed:20644714}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the CUL4-RBX1-DDB1-DCAF1 E3 ubiquitin-protein
CC ligase complex (By similarity). Interacts with l(2)gl. {ECO:0000250,
CC ECO:0000269|PubMed:20644714}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The DWD boxes are required for interaction with DDB1.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mutants develop more slowly and die at
CC a late pupal stage. Zygotic mutants do not have obvious patterning
CC defects during embryonic or larval development but cells undergo
CC apoptosis when surrounded by wild-type cells in the wing disk
CC epithelium. {ECO:0000269|PubMed:20644714}.
CC -!- SIMILARITY: Belongs to the VPRBP/DCAF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO24927.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAV36910.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF46740.2; -; Genomic_DNA.
DR EMBL; AY118444; AAM48473.2; -; mRNA.
DR EMBL; BT003172; AAO24927.1; ALT_FRAME; mRNA.
DR EMBL; BT016025; AAV36910.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001246451.1; NM_001259522.2.
DR RefSeq; NP_611592.2; NM_137748.4.
DR AlphaFoldDB; Q9W2F2; -.
DR SMR; Q9W2F2; -.
DR BioGRID; 63088; 15.
DR IntAct; Q9W2F2; 2.
DR STRING; 7227.FBpp0293270; -.
DR iPTMnet; Q9W2F2; -.
DR PaxDb; Q9W2F2; -.
DR PRIDE; Q9W2F2; -.
DR EnsemblMetazoa; FBtr0071658; FBpp0071575; FBgn0034641.
DR EnsemblMetazoa; FBtr0304728; FBpp0293270; FBgn0034641.
DR GeneID; 37462; -.
DR KEGG; dme:Dmel_CG10080; -.
DR UCSC; CG10080-RA; d. melanogaster.
DR CTD; 37462; -.
DR FlyBase; FBgn0034641; mahj.
DR VEuPathDB; VectorBase:FBgn0034641; -.
DR eggNOG; KOG1832; Eukaryota.
DR GeneTree; ENSGT00390000005874; -.
DR HOGENOM; CLU_001785_1_0_1; -.
DR InParanoid; Q9W2F2; -.
DR OMA; ECSQDQA; -.
DR OrthoDB; 105679at2759; -.
DR PhylomeDB; Q9W2F2; -.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9W2F2; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 37462; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 37462; -.
DR PRO; PR:Q9W2F2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034641; Expressed in cleaving embryo and 24 other tissues.
DR ExpressionAtlas; Q9W2F2; baseline and differential.
DR Genevisible; Q9W2F2; DM.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035212; P:cell competition in a multicellular organism; IMP:FlyBase.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR033270; VPRBP/DCAF1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13129; PTHR13129; 1.
DR SMART; SM00667; LisH; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..1544
FT /note="Protein mahjong"
FT /id="PRO_0000287476"
FT DOMAIN 912..944
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1487..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1302..1309
FT /note="DWD box 1"
FT MOTIF 1338..1345
FT /note="DWD box 2"
FT COMPBIAS 40..86
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1468
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1496..1533
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 955
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 48..49
FT /note="DM -> ET (in Ref. 3; AAO24927)"
FT /evidence="ECO:0000305"
FT CONFLICT 1376
FT /note="R -> K (in Ref. 3; AAO24927/AAM48473)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1544 AA; 172085 MW; F70B699513C3DAD5 CRC64;
MSEGSGSENA AAAEAAAEAE AATEAALMAE AVAVAYQSDE EEQPEAEDMP EQAGDNQEED
AAEQQDGGEP EADEDADADD AMSVENAENE SDSGGNAEET AAADRRQATK KELTQIIDKW
EQQQTQNGYD PVPTLRSLAE IFEREKDVYR RKDPDPLDSR HPYRADPSCQ YGLLLKLLFR
KDTFMGKLLN DYLRENYFSR QNVSRSSLEL NILACRLILE IMPGMETSAV FQTAEGDGTI
NRIYSWAEDS IEPLQSYATG LLAEAMEVSD IAINFRDLNI RLVPKMIKRL HMLLAISKSA
TSDVNTSMHN LSADSSTAGM LSWVACASNA SAPQSPQHNG SGLGASSSQH GDASNMSILF
ENSRDAFSVS RYYKRMYIPL HPATADTSQM LIMRFLTSLG EYQEFLAMAF ENNVMQLIFG
YLENLDRRDT CLAYEVLKYL ASLLCHKKFA LEFISHGGLE LLLKVPRPSL ATTGVSIAIY
YLAYCEDAME RICSMQRPLI SELVRYALWI LGRCHDSSKC HATMFFSLSF QFKVILDEFD
AQDGLRKLYN VISVLKILDP SHNDSDNDSD FNEDVECASR QMVRHVCVAL KRYMEAHFFY
KYNSFLCQTN AASPAPSSAH YFNQNPTVAA KLTFDQLNDQ IRTLQEHTSI RAHWQPVDQL
MKLGGITMLL RIIAFSYDWV NSGRSETVRS ALDVLSVCCI IPRVYVVLCE RLLMLDKTTT
SGFCSVLGAA AGEISSDAEV IKSALAVLCH CVCSPIIRKD SGTSLIKFGT SSRKNKANHK
YAEELIERVW ESVCSNNGIV VLLSLMQTKG PITDADCIRG MACRALAGLA RSDRVRQIVS
KLPLFASGQL QTLMRDPILQ EKRAEHVIFQ KYALELLERV SGKTKPLNNP LDPSLSNMHK
ANVIAQTRIQ YNKQQLYQLI FEHLESNGLS QTAQMLQREV GLPLQTPTTR SFHQSPFDYK
SLPSGSSSLS RNRLRSRMQD VNAAIMGNGD LNRSFGEDSS PAGAGGSNAG DGVSIPNFSS
LNTTQTPIKI RRTDRSSVSR SIQKQAMEPG GMSVGLAEDG QLHPKRITLN TIVTEYLTNQ
HSLCNNPVTT CPQFDLYEPH KCPDPKPSRL LSSNYNLTSR HARTQAGFNT SRFDRRYVHT
HFSPWRSIRS ADYEDLEFTC CDLAGKYIIV GTQQGDGRVF NMNDGVEQFF SNCHNFSVDA
IKANRAGDLV ITSSFWRTPT SILWSIADDE FKLKLRLPDV TYCEFSQTVQ DRLLGTQNEC
ATLFDINTGS KVASFTPTIP NLYTKNRATL CRTDELILSD GVLWDVRSGK EIHKFDKFNQ
CISGVFHPNC LEIIANTEVW DLRTFHLLQT VPVLDQRNCT FSPMHVIYGA SLGADRDHDM
ETTTYDTSFN VLDAYDYSSI ATIDVKRNIN DLSVSANGSL IAVVEDYSGY ESKQETYVKI
YAVGVKKSER SEEEDDEEVP ESDEDGSDTG SENTFAIGQN LLGFPLLRNL HGSDNDDEDL
DEDDDDGEPL DSDDDSDDDD GSDNGDDDGD FDVLEYFDRS SSDD
