ROA1_BOVIN
ID ROA1_BOVIN Reviewed; 320 AA.
AC P09867; Q2KJC4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
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 AltName: Full=Single-strand RNA-binding protein;
DE AltName: Full=Unwinding protein 1;
DE Short=UP1;
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-196, METHYLATION AT ARG-194, AND BLOCKED N-TERMINUS.
RC TISSUE=Thymus;
RX PubMed=3032834; DOI=10.1111/j.1399-3011.1987.tb02226.x;
RA Merrill B.M., Lopresti M.B., Stone K.L., Williams K.R.;
RT "Amino acid sequence of UP1, an hnRNP-derived single-stranded nucleic acid
RT binding protein from calf thymus.";
RL Int. J. Pept. Protein Res. 29:21-39(1987).
RN [3]
RP PROTEIN SEQUENCE OF 2-196, METHYLATION AT ARG-194, AND BLOCKED N-TERMINUS.
RC TISSUE=Thymus;
RX PubMed=2994041; DOI=10.1073/pnas.82.17.5666;
RA Williams K.R., Stone K.L., Lopresti M.B., Merrill B.M., Planck S.R.;
RT "Amino acid sequence of the UP1 calf thymus helix-destabilizing protein and
RT its homology to an analogous protein from mouse myeloma.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5666-5670(1985).
RN [4]
RP PROTEIN SEQUENCE OF 2-185.
RC TISSUE=Thymus;
RX PubMed=3941105; DOI=10.1016/s0021-9258(17)36178-1;
RA Merrill B.M., Lopresti M.B., Stone K.L., Williams K.R.;
RT "High pressure liquid chromatography purification of UP1 and UP2, two
RT related single-stranded nucleic acid-binding proteins from calf thymus.";
RL J. Biol. Chem. 261:878-883(1986).
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: UP1 is derived from A1 by proteolytic degradation.
CC -!- PTM: The N-terminus is blocked.
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; BC105413; AAI05414.1; -; mRNA.
DR PIR; A27241; A27241.
DR RefSeq; NP_001039376.1; NM_001045911.1.
DR AlphaFoldDB; P09867; -.
DR BMRB; P09867; -.
DR SMR; P09867; -.
DR STRING; 9913.ENSBTAP00000002033; -.
DR iPTMnet; P09867; -.
DR PaxDb; P09867; -.
DR PeptideAtlas; P09867; -.
DR PRIDE; P09867; -.
DR Ensembl; ENSBTAT00000002033; ENSBTAP00000002033; ENSBTAG00000001553.
DR GeneID; 505093; -.
DR KEGG; bta:505093; -.
DR CTD; 3178; -.
DR VEuPathDB; HostDB:ENSBTAG00000001553; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00950000183123; -.
DR HOGENOM; CLU_012062_1_0_1; -.
DR InParanoid; P09867; -.
DR OrthoDB; 1202220at2759; -.
DR TreeFam; TF351342; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000001553; Expressed in thymus and 105 other tissues.
DR ExpressionAtlas; P09867; baseline.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:1903936; P:cellular response to sodium arsenite; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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_0000424508"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:2994041,
FT ECO:0000269|PubMed:3032834, ECO:0000269|PubMed:3941105"
FT CHAIN 2..320
FT /note="Heterogeneous nuclear ribonucleoprotein A1, N-
FT terminally processed"
FT /id="PRO_0000081827"
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 182..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..240
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000250"
FT REGION 268..305
FT /note="Nuclear targeting sequence (M9)"
FT /evidence="ECO:0000250"
FT REGION 274..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Polar residues"
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, ECO:0000305"
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:2994041,
FT ECO:0000269|PubMed:3032834"
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:0000250|UniProtKB:P09651"
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:0000250|UniProtKB:P09651"
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:0000250|UniProtKB:P09651"
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:0000250|UniProtKB:P04256"
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"
SQ SEQUENCE 320 AA; 34196 MW; 59485C9FA1FF8AE1 CRC64;
MSKSESPKEP EQLRKLFIGG LSFETTDESL RSHFEQWGTL TDCVVMRDPN TKRSRGFGFV
TYATVEEVDA AMNARPHKVD GRVVEPKRAV SREDSQRPGA HLTVKKIFVG GIKEDTEEHH
LRDYFEQYGK IEVIEIMTDR GSGKKRGFAF VTFDDHDSVD KIVIQKYHTV NGHNCEVRKA
LSKQEMASAS SSQRGRSGSG NFGGGRGGGF GGNDNFGRGG NFSGRGGFGG SRGGGGYGGS
GDGYNGFGND GSNFGGGGSY NDFGNYNNQS SNFGPMKGGN FGGRSSGPYG GGGQYFAKPR
NQGGYGGSSS SSSYGSGRRF
