ROA3_RAT
ID ROA3_RAT Reviewed; 379 AA.
AC Q6URK4; Q6URK3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A3;
DE Short=hnRNP A3;
GN Name=Hnrnpa3; Synonyms=Hnrpa3;
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] (ISOFORMS 1 AND 2), FUNCTION, PROTEIN SEQUENCE
RP OF 114-126, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=11886857; DOI=10.1074/jbc.m200050200;
RA Ma A.S.W., Moran-Jones K., Shan J., Munro T.P., Snee M.J., Hoek K.S.,
RA Smith R.;
RT "Heterogeneous nuclear ribonucleoprotein A3, a novel RNA trafficking
RT response element-binding protein.";
RL J. Biol. Chem. 277:18010-18020(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP METHYLATION AT ARG-214; ARG-216; ARG-226; ARG-239; ARG-246 AND ARG-286.
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: Plays a role in cytoplasmic trafficking of RNA. Binds to the
CC cis-acting response element, A2RE. May be involved in pre-mRNA
CC splicing. {ECO:0000269|PubMed:11886857}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of
CC ribonucleosomes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=a;
CC IsoId=Q6URK4-1; Sequence=Displayed;
CC Name=2; Synonyms=b;
CC IsoId=Q6URK4-2; Sequence=VSP_011400;
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DR EMBL; AY363226; AAQ63630.1; -; mRNA.
DR EMBL; AY363227; AAQ63631.1; -; mRNA.
DR EMBL; BC081878; AAH81878.1; -; mRNA.
DR RefSeq; NP_001104764.1; NM_001111294.1. [Q6URK4-1]
DR RefSeq; NP_001104765.1; NM_001111295.1. [Q6URK4-2]
DR RefSeq; NP_937765.1; NM_198132.3. [Q6URK4-1]
DR RefSeq; XP_008760133.1; XM_008761911.2. [Q6URK4-2]
DR RefSeq; XP_008760134.1; XM_008761912.2. [Q6URK4-2]
DR AlphaFoldDB; Q6URK4; -.
DR SMR; Q6URK4; -.
DR BioGRID; 263224; 5.
DR IntAct; Q6URK4; 7.
DR MINT; Q6URK4; -.
DR STRING; 10116.ENSRNOP00000041984; -.
DR iPTMnet; Q6URK4; -.
DR PhosphoSitePlus; Q6URK4; -.
DR jPOST; Q6URK4; -.
DR PaxDb; Q6URK4; -.
DR PRIDE; Q6URK4; -.
DR Ensembl; ENSRNOT00000078872; ENSRNOP00000069876; ENSRNOG00000052968. [Q6URK4-1]
DR GeneID; 362152; -.
DR KEGG; rno:362152; -.
DR UCSC; RGD:727807; rat. [Q6URK4-1]
DR CTD; 220988; -.
DR RGD; 727807; Hnrnpa3.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000153147; -.
DR HOGENOM; CLU_012062_1_0_1; -.
DR InParanoid; Q6URK4; -.
DR OMA; NTAPWGV; -.
DR OrthoDB; 1202220at2759; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q6URK4; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000052968; Expressed in thymus and 20 other tissues.
DR Genevisible; Q6URK4; RN.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0035770; C:ribonucleoprotein granule; IDA:RGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IMP:RGD.
DR GO; GO:0051033; F:RNA transmembrane transporter activity; IMP:RGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IMP:RGD.
DR CDD; cd12763; RRM1_hnRNPA3; 1.
DR CDD; cd12582; RRM2_hnRNPA3; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034513; hnRNPA3_RRM1.
DR InterPro; IPR034516; hnRNPA3_RRM2.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing;
KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Spliceosome; Ubl conjugation.
FT CHAIN 1..379
FT /note="Heterogeneous nuclear ribonucleoprotein A3"
FT /id="PRO_0000081840"
FT DOMAIN 35..118
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 126..205
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 52
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 52
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 76
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 134
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 214
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:24098712"
FT MOD_RES 214
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 216
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:24098712"
FT MOD_RES 216
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 226
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:24098712"
FT MOD_RES 226
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 239
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:24098712"
FT MOD_RES 239
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BG05"
FT MOD_RES 246
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:24098712"
FT MOD_RES 246
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 257
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG05"
FT MOD_RES 286
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24098712"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 355
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 361
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 365
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 374
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51991"
FT VAR_SEQ 1..23
FT /note="MEVKPPPGRPQPDSGRRRRRRGE -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11886857"
FT /id="VSP_011400"
SQ SEQUENCE 379 AA; 39652 MW; D83C400A2B096E9B CRC64;
MEVKPPPGRP QPDSGRRRRR RGEEGHDPKE PEQLRKLFIG GLSFETTDDS LREHFEKWGT
LTDCVVMRDP QTKRSRGFGF VTYSCVEEVD AAMCARPHKV DGRVVEPKRA VSREDSVKPG
AHLTVKKIFV GGIKEDTEEY NLRDYFEKYG KIETIEVMED RQSGKKRGFA FVTFDDHDTV
DKIVVQKYHT INGHNCEVKK ALSKQEMQSA GSQRGRGGGS GNFMGRGGNF GGGGGNFGRG
GNFGGRGGYG GGGGGSRGSY GGGDGGYNGF GGDGGNYGGG PGYSSRGGYG GGGPGYGNQG
GGYGGGGGGY DGYNEGGNFG GGNYGGGGNY NDFGNYSGQQ QSNYGPMKGG SFGGRSSGSP
YGGGYGSGGG SGGYGSRRF
