ROA3_MOUSE
ID ROA3_MOUSE Reviewed; 379 AA.
AC Q8BG05; Q8BHF8;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A3;
DE Short=hnRNP A3;
GN Name=Hnrnpa3; Synonyms=Hnrpa3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Bayarsaihan D.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Colon, and Eye;
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 PROTEIN SEQUENCE OF 114-126, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-226; ARG-239; ARG-246 AND
RP ARG-257, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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 splicing
CC (By similarity). {ECO:0000250}.
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;
CC IsoId=Q8BG05-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BG05-2; Sequence=VSP_007350;
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DR EMBL; AF463524; AAN76992.1; -; mRNA.
DR EMBL; BC023828; AAH23828.1; -; mRNA.
DR EMBL; BC023908; AAH23908.1; -; mRNA.
DR EMBL; BC038364; AAH38364.1; -; mRNA.
DR EMBL; BC064824; AAH64824.1; -; mRNA.
DR CCDS; CCDS16149.1; -. [Q8BG05-1]
DR CCDS; CCDS50610.1; -. [Q8BG05-2]
DR RefSeq; NP_444493.1; NM_053263.1. [Q8BG05-2]
DR RefSeq; NP_666242.2; NM_146130.3. [Q8BG05-1]
DR RefSeq; NP_932758.1; NM_198090.2. [Q8BG05-1]
DR RefSeq; XP_011237818.1; XM_011239516.2.
DR AlphaFoldDB; Q8BG05; -.
DR SMR; Q8BG05; -.
DR BioGRID; 230827; 82.
DR IntAct; Q8BG05; 42.
DR MINT; Q8BG05; -.
DR STRING; 10090.ENSMUSP00000107595; -.
DR iPTMnet; Q8BG05; -.
DR PhosphoSitePlus; Q8BG05; -.
DR SwissPalm; Q8BG05; -.
DR REPRODUCTION-2DPAGE; Q8BG05; -.
DR EPD; Q8BG05; -.
DR jPOST; Q8BG05; -.
DR MaxQB; Q8BG05; -.
DR PaxDb; Q8BG05; -.
DR PRIDE; Q8BG05; -.
DR ProteomicsDB; 300563; -. [Q8BG05-1]
DR ProteomicsDB; 300564; -. [Q8BG05-2]
DR TopDownProteomics; Q8BG05-1; -. [Q8BG05-1]
DR Antibodypedia; 19537; 131 antibodies from 23 providers.
DR DNASU; 229279; -.
DR Ensembl; ENSMUST00000090792; ENSMUSP00000088298; ENSMUSG00000059005. [Q8BG05-1]
DR Ensembl; ENSMUST00000111962; ENSMUSP00000107593; ENSMUSG00000059005. [Q8BG05-2]
DR Ensembl; ENSMUST00000111964; ENSMUSP00000107595; ENSMUSG00000059005. [Q8BG05-1]
DR Ensembl; ENSMUST00000164947; ENSMUSP00000126069; ENSMUSG00000059005. [Q8BG05-2]
DR GeneID; 229279; -.
DR KEGG; mmu:229279; -.
DR UCSC; uc008ken.2; mouse. [Q8BG05-1]
DR CTD; 220988; -.
DR MGI; MGI:1917171; Hnrnpa3.
DR VEuPathDB; HostDB:ENSMUSG00000059005; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000153147; -.
DR HOGENOM; CLU_012062_1_0_1; -.
DR InParanoid; Q8BG05; -.
DR OMA; NTAPWGV; -.
DR PhylomeDB; Q8BG05; -.
DR TreeFam; TF314808; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR BioGRID-ORCS; 229279; 12 hits in 73 CRISPR screens.
DR ChiTaRS; Hnrnpa3; mouse.
DR PRO; PR:Q8BG05; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BG05; protein.
DR Bgee; ENSMUSG00000059005; Expressed in embryonic post-anal tail and 257 other tissues.
DR ExpressionAtlas; Q8BG05; baseline and differential.
DR Genevisible; Q8BG05; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0035770; C:ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0051033; F:RNA transmembrane transporter activity; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; ISO:MGI.
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_0000081839"
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:0000250|UniProtKB:Q6URK4"
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:0000250|UniProtKB:Q6URK4"
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:0007744|PubMed:24129315"
FT MOD_RES 226
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 239
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 239
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 246
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 246
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 257
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 286
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6URK4"
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:0000250|UniProtKB:P51991"
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:15489334, ECO:0000303|Ref.1"
FT /id="VSP_007350"
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
