ID ROA1_RAT Reviewed; 320 AA. AC P04256; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 192. DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A1; DE Short=hnRNP A1; DE AltName: Full=Helix-destabilizing protein; DE Short=HDP; DE AltName: Full=Single-strand RNA-binding protein; DE AltName: Full=hnRNP core protein A1; DE Contains: DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed; GN Name=Hnrnpa1; Synonyms=Hnrpa1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=3005291; DOI=10.1016/s0021-9258(17)35679-x; RA Cobianchi F., Sengupta D.N., Zmudzka B.Z., Wilson S.H.; RT "Structure of rodent helix-destabilizing protein revealed by cDNA RT cloning."; RL J. Biol. Chem. 261:3536-3543(1986). RN [2] RP SEQUENCE REVISION TO 182. RA Cobianchi F.; RL Submitted (MAY-1986) to the EMBL/GenBank/DDBJ databases. RN [3] RP PARTIAL PROTEIN SEQUENCE. RX PubMed=2447078; DOI=10.1016/s0021-9258(19)35461-4; RA Cobianchi F., Karpel R.L., Williams K.R., Notario V., Wilson S.H.; RT "Mammalian heterogeneous nuclear ribonucleoprotein complex protein A1. RT Large-scale overproduction in Escherichia coli and cooperative binding to RT single-stranded nucleic acids."; RL J. Biol. Chem. 263:1063-1071(1988). RN [4] RP PROTEIN SEQUENCE OF 16-31, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus; RA Lubec G., Diao W.; RL Submitted (NOV-2006) to UniProtKB. RN [5] RP METHYLATION AT ARG-194; ARG-206; ARG-218; ARG-225 AND ARG-232. RX PubMed=24098712; DOI=10.1371/journal.pone.0075669; RA Friend L.R., Landsberg M.J., Nouwens A.S., Wei Y., Rothnagel J.A., RA Smith R.; RT "Arginine methylation of hnRNP A2 does not directly govern its subcellular RT localization."; RL PLoS ONE 8:E75669-E75669(2013). CC -!- FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles, CC transport of poly(A) mRNA from the nucleus to the cytoplasm and CC modulation of splice site selection. Plays a role in the splicing of CC pyruvate kinase PKM by binding repressively to sequences flanking PKM CC exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion CC and production of the PKM M2 isoform. Binds to the IRES and thereby CC inhibits the translation of the apoptosis protease activating factor CC APAF1. May bind to specific miRNA hairpins. CC {ECO:0000250|UniProtKB:P09651}. CC -!- SUBUNIT: Identified in the spliceosome C complex. Identified in a CC IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. CC Interacts with SEPT6. Interacts with C9orf72. Interacts with KHDRBS1. CC Interacts with UBQLN2 (By similarity). Interacts with PPIA/CYPA (By CC similarity). {ECO:0000250|UniProtKB:P09651}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09651}. Cytoplasm CC {ECO:0000250|UniProtKB:P09651}. Note=Localized in cytoplasmic mRNP CC granules containing untranslated mRNAs. Shuttles continuously between CC the nucleus and the cytoplasm along with mRNA. Component of CC ribonucleosomes. {ECO:0000250|UniProtKB:P09651}. CC -!- PTM: Sumoylated. {ECO:0000250}. 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; M12156; AAA41314.1; -; mRNA. DR PIR; A38304; A38304. DR RefSeq; NP_058944.2; NM_017248.3. DR AlphaFoldDB; P04256; -. DR BMRB; P04256; -. DR SMR; P04256; -. DR BioGRID; 248211; 7. DR FunCoup; P04256; 2006. DR IntAct; P04256; 2. DR STRING; 10116.ENSRNOP00000052160; -. DR GlyGen; P04256; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P04256; -. DR PhosphoSitePlus; P04256; -. DR SwissPalm; P04256; -. DR jPOST; P04256; -. DR PaxDb; 10116-ENSRNOP00000052160; -. DR GeneID; 29578; -. DR KEGG; rno:29578; -. DR UCSC; RGD:69234; rat. DR AGR; RGD:69234; -. DR CTD; 3178; -. DR RGD; 69234; Hnrnpa1. DR eggNOG; KOG0118; Eukaryota. DR InParanoid; P04256; -. DR PhylomeDB; P04256; -. DR Reactome; R-RNO-6803529; FGFR2 alternative splicing. DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway. DR Reactome; R-RNO-72203; Processing of Capped Intron-Containing Pre-mRNA. DR Reactome; R-RNO-9770562; mRNA Polyadenylation. DR PRO; PR:P04256; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL. DR GO; GO:0005654; C:nucleoplasm; ISS:HGNC-UCL. DR GO; GO:1990826; C:nucleoplasmic periphery of the nuclear pore complex; IDA:RGD. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB. DR GO; GO:0005681; C:spliceosomal complex; ISS:HGNC-UCL. DR GO; GO:0045202; C:synapse; ISO:RGD. DR GO; GO:0003677; F:DNA binding; ISO:RGD. DR GO; GO:1990814; F:DNA/DNA annealing activity; IDA:RGD. DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISO:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:RGD. DR GO; GO:0003729; F:mRNA binding; IDA:RGD. DR GO; GO:0036002; F:pre-mRNA binding; ISO:RGD. DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD. DR GO; GO:0003723; F:RNA binding; IDA:RGD. DR GO; GO:0033592; F:RNA strand annealing activity; IDA:RGD. DR GO; GO:1990825; F:sequence-specific mRNA binding; IDA:RGD. DR GO; GO:0003697; F:single-stranded DNA binding; ISS:HGNC-UCL. DR GO; GO:0003727; F:single-stranded RNA binding; IDA:RGD. DR GO; GO:0061752; F:telomeric repeat-containing RNA binding; ISO:RGD. DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISO:RGD. DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD. DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:RGD. DR GO; GO:0035865; P:cellular response to potassium ion; IDA:RGD. DR GO; GO:1903936; P:cellular response to sodium arsenite; ISS:UniProtKB. DR GO; GO:0051170; P:import into nucleus; ISS:HGNC-UCL. DR GO; GO:0030324; P:lung development; IEP:RGD. DR GO; GO:0008584; P:male gonad development; IEP:RGD. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:RGD. DR GO; GO:0051168; P:nuclear export; ISS:HGNC-UCL. DR GO; GO:0045760; P:positive regulation of action potential; IMP:RGD. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:RGD. DR GO; GO:0043484; P:regulation of RNA splicing; ISO:RGD. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:RGD. DR GO; GO:0016070; P:RNA metabolic process; TAS:RGD. DR GO; GO:0008380; P:RNA splicing; ISO:RGD. DR CDD; cd12761; RRM1_hnRNPA1; 1. DR FunFam; 3.30.70.330:FF:000048; Heterogeneous nuclear ribonucleoprotein a1 isoform; 1. DR FunFam; 3.30.70.330:FF:000429; Heterogeneous nuclear ribonucleoprotein A1-like 2; 1. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR021662; HnRNPA1/A2_C. DR InterPro; IPR034845; hnRNPA1_RRM1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR48026:SF2; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1-RELATED; 1. DR PANTHER; PTHR48026; HOMOLOGOUS TO DROSOPHILA SQD (SQUID) PROTEIN; 1. DR Pfam; PF11627; HnRNPA1_LC; 1. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50102; RRM; 2. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond; KW Methylation; mRNA processing; mRNA splicing; mRNA transport; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; KW Spliceosome; Transport; Ubl conjugation. FT CHAIN 1..320 FT /note="Heterogeneous nuclear ribonucleoprotein A1" FT /id="PRO_0000424513" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000250|UniProtKB:P09651" FT CHAIN 2..320 FT /note="Heterogeneous nuclear ribonucleoprotein A1, N- FT terminally processed" FT /id="PRO_0000081831" FT DOMAIN 14..97 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 105..184 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 4..94 FT /note="Globular A domain" FT REGION 95..185 FT /note="Globular B domain" FT REGION 188..216 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 218..240 FT /note="RNA-binding RGG-box" FT REGION 268..305 FT /note="Nuclear targeting sequence" FT /evidence="ECO:0000250" FT REGION 271..320 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 197..216 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 276..294 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 308..320 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 2 FT /note="N-acetylserine; in Heterogeneous nuclear FT ribonucleoprotein A1, N-terminally processed" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 3 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 22 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P49312" FT MOD_RES 192 FT /note="Phosphoserine; by MKNK2" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 194 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000269|PubMed:24098712" FT MOD_RES 194 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 194 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P49312" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 206 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000269|PubMed:24098712" FT MOD_RES 206 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 206 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 218 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000269|PubMed:24098712" FT MOD_RES 218 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 225 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000269|PubMed:24098712" FT MOD_RES 225 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 225 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 232 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000269|PubMed:24098712" FT MOD_RES 232 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 284 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 285 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 298 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 300 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 309 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 310 FT /note="Phosphoserine; by MKNK2" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 311 FT /note="Phosphoserine; by MKNK2" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 312 FT /note="Phosphoserine; by MKNK2" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 313 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 316 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09651" FT MOD_RES 318 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P09651" FT CROSSLNK 3 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P09651" FT CROSSLNK 8 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P09651" FT CROSSLNK 78 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P09651" FT CROSSLNK 113 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250" FT CROSSLNK 179 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P09651" FT CROSSLNK 183 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P09651" FT CROSSLNK 298 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P09651" FT CONFLICT 9 FT /note="E -> G (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 27 FT /note="D -> E (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 320 AA; 34212 MW; 44FF5578B5AF8AE1 CRC64; MSKSESPKEP EQLRKLFIGG LSFETTDESL RSHFEQWGTL TDCVVMRDPN TKRSRGFGFV TYATVEEVDA AMNARPHKVD GRVVEPKRAV SREDSQRPGA HLTVKKIFVG GIKEDTEEHH LRDYFEQYGK IEVIEIMTDR GSGKKRGFAF VTFDDHDSVD KIVIQKYHTV NGHNCEVRKA LCKQEMASAS SSQRGRSGSG NFGGGRGGGF GGNDNFGRGG NFSGRGGFGG SRGGGGYGGS GDGYNGFGND GSNFGGGGSY NDFGNYNNQS SNFGPMKGGN FGGRSSGPYG GGGQYFAKPR NQGGYGGSSS SSSYGSGRRF //