ROA1_DROME
ID ROA1_DROME Reviewed; 365 AA.
AC P07909; Q24359; Q24360; Q99361; Q9VAU7; Q9VAU8;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A1;
DE Short=hnRNP A1;
DE AltName: Full=PEN repeat clone P9;
DE AltName: Full=hnRNP core protein A1-A;
GN Name=Hrb98DE; Synonyms=Pen9; ORFNames=CG9983;
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] (ISOFORM B).
RC STRAIN=Oregon-R; TISSUE=Pupae;
RX PubMed=3031652; DOI=10.1073/pnas.84.7.1819;
RA Haynes S.R., Rebbert M.L., Mozer B.A., Forquignon F., Dawid I.B.;
RT "Pen repeat sequences are GGN clusters and encode a glycine-rich domain in
RT a Drosophila cDNA homologous to the rat helix destabilizing protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:1819-1823(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A; B; D AND E), AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo, Ovary, and Pupae;
RX PubMed=2104660; DOI=10.1128/mcb.10.1.316-323.1990;
RA Haynes S.R., Raychaudhuri G., Beyer A.L.;
RT "The Drosophila Hrb98DE locus encodes four protein isoforms homologous to
RT the A1 protein of mammalian heterogeneous nuclear ribonucleoprotein
RT complexes.";
RL Mol. Cell. Biol. 10:316-323(1990).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM D).
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).
CC -!- FUNCTION: This protein is a component of ribonucleosomes.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=B; Synonyms=C;
CC IsoId=P07909-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P07909-2; Sequence=VSP_005827;
CC Name=E;
CC IsoId=P07909-3; Sequence=VSP_005828;
CC Name=D; Synonyms=F;
CC IsoId=P07909-4; Sequence=VSP_005829;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Highest
CC zygotic expression found in adult females and pupae.
CC {ECO:0000269|PubMed:2104660}.
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DR EMBL; M15766; AAA70426.1; -; mRNA.
DR EMBL; M25545; AAA28621.1; -; Genomic_DNA.
DR EMBL; M28871; AAA28621.1; JOINED; Genomic_DNA.
DR EMBL; M28872; AAA28621.1; JOINED; Genomic_DNA.
DR EMBL; M33955; AAA28621.1; JOINED; Genomic_DNA.
DR EMBL; M31560; AAA28621.1; JOINED; Genomic_DNA.
DR EMBL; M25545; AAA28622.1; -; Genomic_DNA.
DR EMBL; M28870; AAA28622.1; JOINED; Genomic_DNA.
DR EMBL; M28872; AAA28622.1; JOINED; Genomic_DNA.
DR EMBL; M33955; AAA28622.1; JOINED; Genomic_DNA.
DR EMBL; M31560; AAA28622.1; JOINED; Genomic_DNA.
DR EMBL; M25545; AAA28623.1; -; Genomic_DNA.
DR EMBL; M28870; AAA28623.1; JOINED; Genomic_DNA.
DR EMBL; M28872; AAA28623.1; JOINED; Genomic_DNA.
DR EMBL; M33955; AAA28623.1; JOINED; Genomic_DNA.
DR EMBL; M31560; AAA28623.1; JOINED; Genomic_DNA.
DR EMBL; M25545; AAA28624.1; -; Genomic_DNA.
DR EMBL; M28871; AAA28624.1; JOINED; Genomic_DNA.
DR EMBL; M28872; AAA28624.1; JOINED; Genomic_DNA.
DR EMBL; M33955; AAA28624.1; JOINED; Genomic_DNA.
DR EMBL; M31560; AAA28624.1; JOINED; Genomic_DNA.
DR EMBL; AE014297; AAF56800.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF56801.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14141.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14143.1; -; Genomic_DNA.
DR EMBL; AY061448; AAL28996.1; -; mRNA.
DR PIR; A26459; A26459.
DR RefSeq; NP_524543.1; NM_079819.3. [P07909-1]
DR RefSeq; NP_733249.1; NM_170370.2. [P07909-2]
DR RefSeq; NP_733250.1; NM_170371.2. [P07909-3]
DR RefSeq; NP_733251.1; NM_170372.2. [P07909-1]
DR RefSeq; NP_733252.1; NM_170373.2. [P07909-4]
DR RefSeq; NP_733253.1; NM_170374.2. [P07909-4]
DR AlphaFoldDB; P07909; -.
DR SMR; P07909; -.
DR BioGRID; 68261; 33.
DR DIP; DIP-19217N; -.
DR IntAct; P07909; 8.
DR STRING; 7227.FBpp0084669; -.
DR PaxDb; P07909; -.
DR DNASU; 43385; -.
DR EnsemblMetazoa; FBtr0085298; FBpp0084667; FBgn0001215. [P07909-2]
DR EnsemblMetazoa; FBtr0085299; FBpp0084668; FBgn0001215. [P07909-3]
DR EnsemblMetazoa; FBtr0085300; FBpp0084669; FBgn0001215. [P07909-1]
DR EnsemblMetazoa; FBtr0085301; FBpp0084670; FBgn0001215. [P07909-1]
DR EnsemblMetazoa; FBtr0085302; FBpp0084671; FBgn0001215. [P07909-4]
DR EnsemblMetazoa; FBtr0085303; FBpp0084672; FBgn0001215. [P07909-4]
DR GeneID; 43385; -.
DR KEGG; dme:Dmel_CG9983; -.
DR CTD; 43385; -.
DR FlyBase; FBgn0001215; Hrb98DE.
DR VEuPathDB; VectorBase:FBgn0001215; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000167175; -.
DR HOGENOM; CLU_012062_1_3_1; -.
DR InParanoid; P07909; -.
DR OMA; NTAPWGV; -.
DR PhylomeDB; P07909; -.
DR SignaLink; P07909; -.
DR BioGRID-ORCS; 43385; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Hrb98DE; fly.
DR GenomeRNAi; 43385; -.
DR PRO; PR:P07909; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0001215; Expressed in eye disc (Drosophila) and 26 other tissues.
DR ExpressionAtlas; P07909; baseline and differential.
DR Genevisible; P07909; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:FlyBase.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
DR GO; GO:0034046; F:poly(G) binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IGI:FlyBase.
DR GO; GO:0036099; P:female germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0033119; P:negative regulation of RNA splicing; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IMP:FlyBase.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP: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; 2.
DR PROSITE; PS50102; RRM; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Nucleus; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding.
FT CHAIN 1..365
FT /note="Heterogeneous nuclear ribonucleoprotein A1"
FT /id="PRO_0000081834"
FT DOMAIN 31..107
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 122..199
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..21
FT /note="MVNSNQNQNGNSNGHDDDFPQ -> MGGHDNWNNGQNEEQD (in
FT isoform E)"
FT /evidence="ECO:0000303|PubMed:2104660"
FT /id="VSP_005828"
FT VAR_SEQ 1..16
FT /note="MVNSNQNQNGNSNGHD -> MGGHDNWNNGQNEEQ (in isoform A)"
FT /evidence="ECO:0000303|PubMed:2104660"
FT /id="VSP_005827"
FT VAR_SEQ 18..21
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:2104660"
FT /id="VSP_005829"
SQ SEQUENCE 365 AA; 39038 MW; BCC707CA2A2EC580 CRC64;
MVNSNQNQNG NSNGHDDDFP QDSITEPEHM RKLFIGGLDY RTTDENLKAH FEKWGNIVDV
VVMKDPRTKR SRGFGFITYS HSSMIDEAQK SRPHKIDGRV VEPKRAVPRQ DIDSPNAGAT
VKKLFVGALK DDHDEQSIRD YFQHFGNIVD INIVIDKETG KKRGFAFVEF DDYDPVDKVV
LQKQHQLNGK MVDVKKALPK QNDQQGGGGG RGGPGGRAGG NRGNMGGGNY GNQNGGGNWN
NGGNNWGNNR GGNDNWGNNS FGGGGGGGGG YGGGNNSWGN NNPWDNGNGG GNFGGGGNNW
NNGGNDFGGY QQNYGGGPQR GGGNFNNNRM QPYQGGGGFK AGGGNQGNYG GNNQGFNNGG
NNRRY
