U2AF1_DROME
ID U2AF1_DROME Reviewed; 264 AA.
AC Q94535; Q9VPN4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Splicing factor U2af 38 kDa subunit;
DE AltName: Full=U2 auxiliary factor 38 kDa subunit;
DE AltName: Full=U2 snRNP auxiliary factor small subunit;
GN Name=U2af38; ORFNames=CG3582;
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 [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Embryo;
RX PubMed=8816800; DOI=10.1073/pnas.93.19.10333;
RA Rudner D.Z., Kanaar R., Breger K.S., Rio D.C.;
RT "Mutations in the small subunit of the Drosophila U2AF splicing factor
RT cause lethality and developmental defects.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10333-10337(1996).
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.
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Necessary for the splicing of pre-mRNA. Binds to the
CC polypyrimidine tract of introns early during spliceosome assembly (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associates with a 65 kDa protein. {ECO:0000250}.
CC -!- INTERACTION:
CC Q94535; Q24562: U2af50; NbExp=4; IntAct=EBI-121011, EBI-165226;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; U67066; AAB17271.1; -; mRNA.
DR EMBL; AE014134; AAF51512.1; -; Genomic_DNA.
DR EMBL; AY058537; AAL13766.1; -; mRNA.
DR PIR; JC6125; JC6125.
DR RefSeq; NP_001259814.1; NM_001272885.1.
DR RefSeq; NP_477208.1; NM_057860.4.
DR AlphaFoldDB; Q94535; -.
DR SMR; Q94535; -.
DR BioGRID; 59457; 5.
DR DIP; DIP-23299N; -.
DR IntAct; Q94535; 4.
DR STRING; 7227.FBpp0305600; -.
DR iPTMnet; Q94535; -.
DR PaxDb; Q94535; -.
DR PRIDE; Q94535; -.
DR EnsemblMetazoa; FBtr0078133; FBpp0077792; FBgn0017457.
DR EnsemblMetazoa; FBtr0333408; FBpp0305600; FBgn0017457.
DR GeneID; 33201; -.
DR KEGG; dme:Dmel_CG3582; -.
DR CTD; 33201; -.
DR FlyBase; FBgn0017457; U2af38.
DR VEuPathDB; VectorBase:FBgn0017457; -.
DR eggNOG; KOG2202; Eukaryota.
DR GeneTree; ENSGT00950000183152; -.
DR HOGENOM; CLU_059852_1_0_1; -.
DR InParanoid; Q94535; -.
DR OMA; NDGEDRW; -.
DR OrthoDB; 1340384at2759; -.
DR PhylomeDB; Q94535; -.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-72187; mRNA 3'-end processing.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q94535; -.
DR BioGRID-ORCS; 33201; 0 hits in 3 CRISPR screens.
DR ChiTaRS; U2af38; fly.
DR GenomeRNAi; 33201; -.
DR PRO; PR:Q94535; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0017457; Expressed in oviduct (Drosophila) and 25 other tissues.
DR ExpressionAtlas; Q94535; baseline and differential.
DR Genevisible; Q94535; DM.
DR GO; GO:0005634; C:nucleus; IC:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0089701; C:U2AF complex; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
DR GO; GO:0008187; F:poly-pyrimidine tract binding; IDA:FlyBase.
DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:FlyBase.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:FlyBase.
DR GO; GO:0008380; P:RNA splicing; IMP:FlyBase.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR009145; U2AF_small.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR12620; PTHR12620; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR PRINTS; PR01848; U2AUXFACTOR.
DR SMART; SM00361; RRM_1; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..264
FT /note="Splicing factor U2af 38 kDa subunit"
FT /id="PRO_0000081997"
FT DOMAIN 44..149
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 12..40
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 151..178
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 190..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..215
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 66
FT /note="H -> D (in Ref. 1; AAB17271)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 29877 MW; 577285FB66FDB2F5 CRC64;
MAEYLASIFG TEKDKVNCSF YFKIGACRHG DRCSRIHNKP TFSQTVLLQN LYVNPQNSAK
SADGSHLVAN VSDEEMQEHY DNFFEDVFVE CEDKYGEIEE MNVCDNLGDH LVGNVYIKFR
NEADAEKAAN DLNNRWFGGR PVYSELSPVT DFREACCRQY EMGECTRSGF CNFMHLKPIS
RELRRYLYSR RRRARSRSRS PGRRRGSRSR SRSPGRRGGG RGDGVGGGNY LNNERDNMRG
NDRGNDRDRR KGGGGGGGGG GGRY
