CWC22_DROME
ID CWC22_DROME Reviewed; 1330 AA.
AC Q9VJ87; A8WHI6; C9QPF2; Q8SXP2; Q95R63;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Pre-mRNA-splicing factor CWC22 homolog;
DE AltName: Full=Nucampholin;
GN Name=ncm; ORFNames=CG12750;
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, and 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=15998720; DOI=10.1534/genetics.105.045021;
RA Coelho C.M., Kolevski B., Walker C.D., Lavagi I., Shaw T., Ebert A.,
RA Leevers S.J., Marygold S.J.;
RT "A genetic screen for dominant modifiers of a small-wing phenotype in
RT Drosophila melanogaster identifies proteins involved in splicing and
RT translation.";
RL Genetics 171:597-614(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-191; THR-201; SER-219;
RP SER-221; THR-1108; SER-1111; SER-1180; SER-1181 AND TYR-1182, 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 [8]
RP INTERACTION WITH EIF4AIII.
RX PubMed=22961380; DOI=10.1038/nsmb.2380;
RA Barbosa I., Haque N., Fiorini F., Barrandon C., Tomasetto C.,
RA Blanchette M., Le Hir H.;
RT "Human CWC22 escorts the helicase eIF4AIII to spliceosomes and promotes
RT exon junction complex assembly.";
RL Nat. Struct. Mol. Biol. 19:983-990(2012).
CC -!- FUNCTION: Required for pre-mRNA splicing and for exon-junction complex
CC (EJC) assembly. Hinders eIF4AIII from non-specifically binding RNA and
CC escorts it to the splicing machinery to promote EJC assembly on mature
CC mRNAs. {ECO:0000250|UniProtKB:Q9HCG8}.
CC -!- SUBUNIT: Component of the spliceosome C complex (By similarity).
CC Interacts with eIF4AIII (PubMed:22961380).
CC {ECO:0000250|UniProtKB:Q9HCG8, ECO:0000269|PubMed:22961380}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q9HCG8}.
CC -!- SIMILARITY: Belongs to the CWC22 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL29144.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABX00754.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF53667.3; -; Genomic_DNA.
DR EMBL; AY061596; AAL29144.1; ALT_INIT; mRNA.
DR EMBL; AY089504; AAL90242.1; -; mRNA.
DR EMBL; BT100034; ACX54942.1; -; mRNA.
DR EMBL; BT031132; ABX00754.1; ALT_FRAME; mRNA.
DR RefSeq; NP_609877.2; NM_136033.3.
DR AlphaFoldDB; Q9VJ87; -.
DR SMR; Q9VJ87; -.
DR BioGRID; 61094; 8.
DR IntAct; Q9VJ87; 4.
DR STRING; 7227.FBpp0080638; -.
DR iPTMnet; Q9VJ87; -.
DR PaxDb; Q9VJ87; -.
DR PRIDE; Q9VJ87; -.
DR EnsemblMetazoa; FBtr0081088; FBpp0080638; FBgn0086707.
DR GeneID; 35099; -.
DR KEGG; dme:Dmel_CG12750; -.
DR CTD; 35099; -.
DR FlyBase; FBgn0086707; ncm.
DR VEuPathDB; VectorBase:FBgn0086707; -.
DR eggNOG; KOG2140; Eukaryota.
DR GeneTree; ENSGT00940000153458; -.
DR HOGENOM; CLU_006308_1_0_1; -.
DR InParanoid; Q9VJ87; -.
DR OMA; QDSDEFN; -.
DR OrthoDB; 304858at2759; -.
DR PhylomeDB; Q9VJ87; -.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9VJ87; -.
DR BioGRID-ORCS; 35099; 1 hit in 1 CRISPR screen.
DR ChiTaRS; ncm; fly.
DR GenomeRNAi; 35099; -.
DR PRO; PR:Q9VJ87; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0086707; Expressed in eye disc (Drosophila) and 33 other tissues.
DR Genevisible; Q9VJ87; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR Pfam; PF02847; MA3; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51366; MI; 1.
PE 1: Evidence at protein level;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1330
FT /note="Pre-mRNA-splicing factor CWC22 homolog"
FT /id="PRO_0000302011"
FT DOMAIN 420..603
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 710..826
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 1..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..273
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1010
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 191
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1111
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 1180
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1182
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 1051
FT /note="H -> R (in Ref. 3; AAL29144)"
FT /evidence="ECO:0000305"
FT CONFLICT 1169
FT /note="N -> K (in Ref. 3; AAL29144)"
FT /evidence="ECO:0000305"
FT CONFLICT 1281
FT /note="R -> RGERSDRGERSDR (in Ref. 3; AAL29144)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1330 AA; 151637 MW; 7E22E91BDB7930E2 CRC64;
MGESDAESDS SSNSSSSDTS SGSDSDARSE SSSSESSGRE EEEAKQEESA KDAKKTDDTD
RGEKRAKERD AGQDEQPTEQ KKTPAAEPRS ERQHISHSAG VEKQQEEAVA AAEAESEKLN
EAKKVETPVQ RKEEAEASSV TKELNSPKAQ EENAARELEE RRKDEEQPVT TNGSSKESPV
EAAAETVKPP TADHIEEGEI TDKDEDDLPT KEEKKAVASK SPPKETQRKQ SRSPDGKRRR
PRSSSRSPSP SSRRRRRSRS KGSRTRSRSK SPIRRRSNSL ERRRVERQRR HEERDKRDEE
RAKEREKRHQ KGEPTSSRRR DDSREKKRSP ERKRDRSSST PKSKSSKTPR HTETTETNAD
NETVTEPAAK ITERQRKTVD VLTSRTGGAY IPPAKLRMMQ SQITDKSSAA YQRIAWEALK
KSIHGYINKV NVTNIAIITR ELLRENIVRG RGLLSRSIIQ AQAASPTFTH VYAALVSIIN
SKFPNIGELL LKRLVIQFRR AFRRNDKMVC MSATRFIGHL VNQRVAHEIL ALEILTLLVE
TPTDDSVEVA IAFLKECGMK LTEVSSKGIG AIFEMLRNIL HEGKLDKRVQ YMIEVLFQIR
KDGFKDHQAV VPELELVEED DQFTHLMMLD EATETEDILN VFKFDDNYAE NEDKYKGLSR
EILGSDDGSS SGSGSGSDSD SDSDGESGSD AEKKAEAGDI IDSTETNLIA LRRTIYLTIN
SSLDYEECAH KLMKMQLKPG QEIELCHMFL DCCAEQRTYE KFYGLLAQRF CNINKIYIPP
FEEIFKDTYQ TTHRLDTNRL RNVSKFFAHL LFTDAISWDV LECIQLNEDD TTSSSRIFIK
ILFQELAEYM GLGKLNAKLK DDVLVESIAG LFPKDNPRNT RFSINFFTSI GLGGLTDDLR
RFLKNAPKSV PAINAEILAN AGGNPFRDGS APAGNTKVAP SSSSSSSSSS DTDSEDSSEE
DSSSDSSSES SSSDSSSEPK KKRKRKDKDK KKSKKATKEK SKKTKNKKKK KKAEKEQEKE
KEKQRKSKKE KEKDKKRKKE EKKAAKKKSK HRRKSQESSD SSGSEDSDKS TSESSDSSNS
SSDESDAEPQ AKIKRQEHVE KNKFRGRTQD SDEFNLEGPG SKNRFQPNGN GQRRRDNSTG
RERNRENSSY DRERNRGNSS YDRERKRGNS SYDRERNRES SYDKERKNRN AVAHDRQRKR
DRSRSYERPT IRENSAPREK RMESSRSEKD SRRGDRSSRN ERSDRGERSD RGERSDRGER
SDRGERSDRG ERSDRGERSD REKERSRAKE RERDRDRDLK GQRERKRERD DGSRDRSRRE
RSSRRSKGRS
