ROA1_RAT
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 03-AUG-2022, entry version 176.
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_058944.1; NM_017248.1.
DR AlphaFoldDB; P04256; -.
DR BMRB; P04256; -.
DR SMR; P04256; -.
DR BioGRID; 248211; 5.
DR IntAct; P04256; 2.
DR STRING; 10116.ENSRNOP00000052160; -.
DR iPTMnet; P04256; -.
DR PhosphoSitePlus; P04256; -.
DR SwissPalm; P04256; -.
DR jPOST; P04256; -.
DR PaxDb; P04256; -.
DR PRIDE; P04256; -.
DR GeneID; 29578; -.
DR KEGG; rno:29578; -.
DR UCSC; RGD:69234; rat.
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 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:0005829; C:cytosol; IDA:RGD.
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; IDA:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISS:HGNC-UCL.
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: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:1904579; P:cellular response to thapsigargin; IEP:RGD.
DR GO; GO:1904577; P:cellular response to tunicamycin; IMP:RGD.
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:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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:0016070; P:RNA metabolic process; TAS:RGD.
DR GO; GO:0008380; P:RNA splicing; ISO:RGD.
DR GO; GO:0019087; P:transformation of host cell by virus; IEP:RGD.
DR CDD; cd12761; RRM1_hnRNPA1; 1.
DR CDD; cd12580; RRM2_hnRNPA1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR021662; HnRNPA1_C.
DR InterPro; IPR034845; hnRNPA1_RRM1.
DR InterPro; IPR034803; hnRNPA1_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF11627; HnRNPA1; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 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 303..320
FT /note="Polar residues"
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
