SNRPA_DROME
ID SNRPA_DROME Reviewed; 216 AA.
AC P43332; Q9W4D7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=U1 small nuclear ribonucleoprotein A;
DE Short=U1 snRNP A;
DE Short=U1-A;
DE Short=U1A;
DE AltName: Full=Sex determination protein snf;
GN Name=snf; Synonyms=D25, fs(1)1621, liz; ORFNames=CG4528;
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].
RX PubMed=1386424; DOI=10.1093/nar/20.14.3645;
RA Harper D.S., Fresco L.D., Keene J.D.;
RT "RNA binding specificity of a Drosophila snRNP protein that shares sequence
RT homology with mammalian U1-A and U2-B' proteins.";
RL Nucleic Acids Res. 20:3645-3650(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC STRAIN=Oregon-R;
RX PubMed=7926776; DOI=10.1101/gad.8.8.914;
RA Flickinger T.W., Salz H.K.;
RT "The Drosophila sex determination gene snf encodes a nuclear protein with
RT sequence and functional similarity to the mammalian U1A snRNP protein.";
RL Genes Dev. 8:914-925(1994).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
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 [6]
RP INTERACTION WITH THE SMN COMPLEX.
RX PubMed=18621711; DOI=10.1073/pnas.0802287105;
RA Kroiss M., Schultz J., Wiesner J., Chari A., Sickmann A., Fischer U.;
RT "Evolution of an RNP assembly system: a minimal SMN complex facilitates
RT formation of UsnRNPs in Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10045-10050(2008).
CC -!- FUNCTION: Binds stem loop II of U1 snRNA. It is the first snRNP to
CC interact with pre-mRNA. This interaction is required for the subsequent
CC binding of U2 snRNP and the U4/U6/U5 tri-snRNP (By similarity). Plays a
CC role in regulating sex-lethal splicing. {ECO:0000250,
CC ECO:0000269|PubMed:7926776}.
CC -!- SUBUNIT: Belongs to the spliceosome where it is associated with snRNP
CC U1. Interacts with the SMN complex. {ECO:0000269|PubMed:18621711}.
CC -!- INTERACTION:
CC P43332; Q9V3N8: THG; NbExp=3; IntAct=EBI-174177, EBI-131989;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the RRM U1 A/B'' family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M89775; AAA28441.1; -; mRNA.
DR EMBL; L29521; AAA28903.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF46017.1; -; Genomic_DNA.
DR EMBL; AY061491; AAL29039.1; -; mRNA.
DR PIR; A54279; A54279.
DR RefSeq; NP_511045.1; NM_078490.4.
DR PDB; 2AYM; NMR; -; A=134-216.
DR PDB; 2B0G; NMR; -; A=134-216.
DR PDB; 2K3K; NMR; -; A=1-98.
DR PDB; 6F4G; X-ray; 1.90 A; B/E=1-96.
DR PDB; 6F4H; X-ray; 2.00 A; A/C/E=1-96.
DR PDB; 6F4I; X-ray; 1.49 A; A/B/C/D/E/F=1-96.
DR PDB; 6F4J; X-ray; 1.42 A; C/D=1-96.
DR PDBsum; 2AYM; -.
DR PDBsum; 2B0G; -.
DR PDBsum; 2K3K; -.
DR PDBsum; 6F4G; -.
DR PDBsum; 6F4H; -.
DR PDBsum; 6F4I; -.
DR PDBsum; 6F4J; -.
DR AlphaFoldDB; P43332; -.
DR BMRB; P43332; -.
DR SMR; P43332; -.
DR BioGRID; 57952; 40.
DR DIP; DIP-23676N; -.
DR IntAct; P43332; 4.
DR STRING; 7227.FBpp0070716; -.
DR PaxDb; P43332; -.
DR PRIDE; P43332; -.
DR DNASU; 31442; -.
DR EnsemblMetazoa; FBtr0070748; FBpp0070716; FBgn0003449.
DR GeneID; 31442; -.
DR KEGG; dme:Dmel_CG4528; -.
DR CTD; 31442; -.
DR FlyBase; FBgn0003449; snf.
DR VEuPathDB; VectorBase:FBgn0003449; -.
DR eggNOG; KOG4206; Eukaryota.
DR GeneTree; ENSGT00390000007046; -.
DR HOGENOM; CLU_041869_1_1_1; -.
DR InParanoid; P43332; -.
DR OMA; NQTIYVN; -.
DR OrthoDB; 1608132at2759; -.
DR PhylomeDB; P43332; -.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 31442; 1 hit in 3 CRISPR screens.
DR ChiTaRS; snf; fly.
DR EvolutionaryTrace; P43332; -.
DR GenomeRNAi; 31442; -.
DR PRO; PR:P43332; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003449; Expressed in eye disc (Drosophila) and 29 other tissues.
DR ExpressionAtlas; P43332; baseline and differential.
DR Genevisible; P43332; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:FlyBase.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IDA:FlyBase.
DR GO; GO:0005681; C:spliceosomal complex; ISS:FlyBase.
DR GO; GO:0005685; C:U1 snRNP; ISS:FlyBase.
DR GO; GO:0005686; C:U2 snRNP; ISS:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:FlyBase.
DR GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:FlyBase.
DR GO; GO:0097158; F:pre-mRNA intronic pyrimidine-rich binding; IDA:FlyBase.
DR GO; GO:0035614; F:snRNA stem-loop binding; IDA:FlyBase.
DR GO; GO:0030619; F:U1 snRNA binding; IDA:FlyBase.
DR GO; GO:0030620; F:U2 snRNA binding; IDA:FlyBase.
DR GO; GO:0019099; P:female germ-line sex determination; NAS:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007539; P:primary sex determination, soma; NAS:FlyBase.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:FlyBase.
DR GO; GO:0008380; P:RNA splicing; TAS:FlyBase.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..216
FT /note="U1 small nuclear ribonucleoprotein A"
FT /id="PRO_0000081890"
FT DOMAIN 7..86
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 142..216
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 97..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 49
FT /note="R -> H (in allele SNF1621; sterile)"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:6F4J"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:6F4J"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:6F4J"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:6F4J"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:6F4J"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:6F4J"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:6F4J"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:6F4J"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:2K3K"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6F4J"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:6F4J"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:2AYM"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:2AYM"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:2AYM"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:2AYM"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:2AYM"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:2AYM"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:2AYM"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:2AYM"
SQ SEQUENCE 216 AA; 24547 MW; 5B736FFE36523373 CRC64;
MEMLPNQTIY INNLNEKIKK EELKKSLYAI FSQFGQILDI VALKTLKMRG QAFVIFKEIG
SASNALRTMQ GFPFYDKPMQ IAYSKSDSDI VAKIKGTFKE RPKKVKPPKP APGTDEKKDK
KKKPSSAENS NPNAQTEQPP NQILFLTNLP EETNEMMLSM LFNQFPGFKE VRLVPNRHDI
AFVEFTTELQ SNAAKEALQG FKITPTHAMK ITFAKK
