FLACC_DROME
ID FLACC_DROME Reviewed; 1150 AA.
AC Q9VWN4; X2JFQ1; X2JG10;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Fl(2)d-associated complex component {ECO:0000303|PubMed:29535189};
DE AltName: Full=Protein Xiong {ECO:0000303|PubMed:29555755};
GN Name=Flacc {ECO:0000303|PubMed:29535189};
GN Synonyms=Xio {ECO:0000303|PubMed:29555755};
GN ORFNames=CG7358 {ECO:0000312|FlyBase:FBgn0030974};
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] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
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).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND IDENTIFICATION IN THE WMM COMPLEX.
RX PubMed=29535189; DOI=10.1101/gad.309146.117;
RA Knuckles P., Lence T., Haussmann I.U., Jacob D., Kreim N., Carl S.H.,
RA Masiello I., Hares T., Villasenor R., Hess D., Andrade-Navarro M.A.,
RA Biggiogera M., Helm M., Soller M., Buehler M., Roignant J.Y.;
RT "Zc3h13/Flacc is required for adenosine methylation by bridging the mRNA-
RT binding factor Rbm15/Spenito to the m6A machinery component Wtap/Fl(2)d.";
RL Genes Dev. 32:415-429(2018).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, IDENTIFICATION IN THE
RP WMM COMPLEX, AND DISRUPTION PHENOTYPE.
RX PubMed=29555755; DOI=10.1073/pnas.1720945115;
RA Guo J., Tang H.W., Li J., Perrimon N., Yan D.;
RT "Xio is a component of the Drosophila sex determination pathway and RNA N6-
RT methyladenosine-methyladenosine methyltransferase complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:3674-3679(2018).
CC -!- FUNCTION: Associated component of the WMM complex, a complex that
CC mediates N6-methyladenosine (m6A) methylation of mRNAs, a modification
CC that plays a role in the efficiency of mRNA splicing and is required
CC for sex determination (PubMed:29535189, PubMed:29555755). In the WMM
CC complex, acts as a key regulator of m6A methylation by bridging fl(2)d
CC to the RNA-binding component nito (PubMed:29535189). Required for sex
CC determination and dosage compensation via Sxl alternative splicing: m6A
CC methylation acts as a key regulator of Sxl pre-mRNA and promotes
CC female-specific alternative splicing of Sxl, which determines female
CC physiognomy (PubMed:29535189, PubMed:29555755).
CC {ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29555755}.
CC -!- SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex
CC composed of a catalytic subcomplex, named MAC, and of an associated
CC subcomplex, named MACOM (PubMed:29535189, PubMed:29555755). The MAC
CC subcomplex is composed of Ime4/Mettl3 and Mettl14 (PubMed:29535189,
CC PubMed:29555755). The MACOM subcomplex is composed of fl(2)d,
CC Flacc/Xio, Hakai, vir, and, in some cases of nito (PubMed:29535189,
CC PubMed:29555755). {ECO:0000269|PubMed:29535189,
CC ECO:0000269|PubMed:29555755}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29535189,
CC ECO:0000269|PubMed:29555755}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q9VWN4-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9VWN4-2; Sequence=VSP_059626;
CC Name=C;
CC IsoId=Q9VWN4-3; Sequence=VSP_059627, VSP_059628;
CC -!- TISSUE SPECIFICITY: Widely expressed during embryogenesis but shows
CC enrichment in the neuroectoderm. {ECO:0000269|PubMed:29535189}.
CC -!- DEVELOPMENTAL STAGE: Expression is enriched in early embryos, decreases
CC during larval stages, and rises again at pupal stages
CC (PubMed:29555755). Strongly expressed during the maternal-to-zygotic
CC transition, a time where N6-methyladenosine (m6A) methylation of mRNAs
CC is decreasing (PubMed:29535189). {ECO:0000269|PubMed:29535189,
CC ECO:0000269|PubMed:29555755}.
CC -!- DISRUPTION PHENOTYPE: Female-specific lethality, associated with sexual
CC transformation phenotypes (PubMed:29555755). Hemizygous males are
CC sterile (PubMed:29555755). Sexual transformation phenotypes resemble
CC other N6-methyladenosine (m6A) factors, such as sexual transformations,
CC Sxl splicing defect, held-out wings, flightless flies and reduction of
CC m6A levels (PubMed:29555755). {ECO:0000269|PubMed:29555755}.
CC -!- MISCELLANEOUS: Was named Xiong after the Chinese character for
CC maleness. {ECO:0000269|PubMed:29555755}.
CC -!- SIMILARITY: Belongs to the ZC3H13 family. {ECO:0000305}.
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DR EMBL; AE014298; AAF48904.1; -; Genomic_DNA.
DR EMBL; AE014298; AHN59888.1; -; Genomic_DNA.
DR EMBL; AE014298; AHN59889.1; -; Genomic_DNA.
DR EMBL; AY128424; AAM75017.1; -; mRNA.
DR RefSeq; NP_001285418.1; NM_001298489.1. [Q9VWN4-2]
DR RefSeq; NP_001285419.1; NM_001298490.1. [Q9VWN4-3]
DR RefSeq; NP_573339.1; NM_133111.2. [Q9VWN4-1]
DR AlphaFoldDB; Q9VWN4; -.
DR IntAct; Q9VWN4; 4.
DR STRING; 7227.FBpp0074423; -.
DR PaxDb; Q9VWN4; -.
DR DNASU; 32886; -.
DR EnsemblMetazoa; FBtr0074652; FBpp0074423; FBgn0030974. [Q9VWN4-1]
DR EnsemblMetazoa; FBtr0342879; FBpp0309680; FBgn0030974. [Q9VWN4-2]
DR EnsemblMetazoa; FBtr0342880; FBpp0309681; FBgn0030974. [Q9VWN4-3]
DR GeneID; 32886; -.
DR KEGG; dme:Dmel_CG7358; -.
DR UCSC; CG7358-RA; d. melanogaster. [Q9VWN4-1]
DR CTD; 32886; -.
DR FlyBase; FBgn0030974; Flacc.
DR VEuPathDB; VectorBase:FBgn0030974; -.
DR eggNOG; KOG1874; Eukaryota.
DR HOGENOM; CLU_007189_0_0_1; -.
DR InParanoid; Q9VWN4; -.
DR OMA; QRWQPHR; -.
DR OrthoDB; 263740at2759; -.
DR PhylomeDB; Q9VWN4; -.
DR SignaLink; Q9VWN4; -.
DR BioGRID-ORCS; 32886; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32886; -.
DR PRO; PR:Q9VWN4; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030974; Expressed in eye disc (Drosophila) and 36 other tissues.
DR ExpressionAtlas; Q9VWN4; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0080009; P:mRNA methylation; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007530; P:sex determination; IMP:UniProtKB.
DR GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
DR InterPro; IPR040427; Flacc.
DR PANTHER; PTHR38563; PTHR38563; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Developmental protein; Differentiation;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Sexual differentiation.
FT CHAIN 1..1150
FT /note="Fl(2)d-associated complex component"
FT /id="PRO_0000444613"
FT REGION 1..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 122..147
FT /evidence="ECO:0000255"
FT COILED 269..347
FT /evidence="ECO:0000255"
FT COMPBIAS 19..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..97
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..140
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1048
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 820..830
FT /note="Missing (in isoform B)"
FT /id="VSP_059626"
FT VAR_SEQ 821..842
FT /note="SKLNTVCIKQEDASEDSAGTPE -> RLIFVYFAAETSDAAYHIIWRQ (in
FT isoform C)"
FT /id="VSP_059627"
FT VAR_SEQ 843..1150
FT /note="Missing (in isoform C)"
FT /id="VSP_059628"
SQ SEQUENCE 1150 AA; 128975 MW; 9FDB349AAF9C7D76 CRC64;
MEKKAKESLR RYKKAARHSA THSSSSDSTS DSDSGSSSYS STDSEQGVGG VGVGVGVPGG
AGGPGGSGSV HGHPHTHGHG HHPRSAERHH RKKKSSRRGG SSSGDEPSSS RRKRDKRDHV
QKKLVAKRNH IKRKLKEARL KKRAAAALSG HVHRSLSPTT RAKLKKLAER KRLRAASKEQ
RERDKLRVVQ RDRERDHHRL GSSRSPPSSS TTTTTKIRIH QDIVGKRQKS PGLGSGLGGG
SSSSSSRMHH QLMSREKIII QTRARGRTPS LERERERERE RERERERERH DLSLRERDRR
DRERERAERE AARDKERAEA LARCQERQRE RERLAREKLR RQEEEEGGKR GGPGRDLDLP
PYGSRERSLD TVERERERER SGRHVRDKRE LDPYEREQEY LEERHGHGLI DEMRRYRRRD
LSPMPEHYAP RLRDPRELYS EEERERAYKR AYLDARYSSR EREAWLEARE LRERELQGRE
YRDLETEDTL YPDERERLIR DRERDRERER DRERERNIGP RGDFRPEWER EWEEEGAGGG
PGGPSGTPGR PGGFVGGPKR GKPPAHAGGG PPSQQQHHSA SEPDWDADER ERERERERDR
ERERDREDRP DTGGGGAGGD RPSIKNEPAW LEHDQREKPR GWQQQSSNSG GDWRDNDDAP
PAPSHPHPAS PHHHVHPRGE RGSGRGFRRG GHGHGDHGER PGYRSHPPPL MTLPVQPPGG
YSRGFPHKRL PYGSGRDGAA LGARDGGLPG SSTFLKKHTH APLVSPTQTP LLNPLLNAAK
PNAAAQASAV AAATTAVAAA KAAAQSAANA TTNPGILAQV SKLNTVCIKQ EDASEDSAGT
PELGAQDSPT QSLNLNQSLS SEGNPVKQEL IRTSAVEGEL SEISDSDDDI LNKTDKVRPK
NELPTETEQE MDTNADEVKS EALHIVAGHP IKGEEGDEVL DFEEISDGEL EEDARHKGIG
DALGVDWQGL IAETRQQASD AQAAQQGVDR GTSAKQRWQP YRVLLDLGIS FGMAGEGYAR
CVMEEARQQL LQEKEQGQQR ELDGDEEPPA KIPSPLLDYR EFLASQQQLE PLACVQMGLR
SAAVERQRLV GNVCGPGSRA LSARQDLRLR RQLCGLPARE CEFPRSVPIV GEGLRNLAMQ
MFQRRLLDVK
