RBM42_BOVIN
ID RBM42_BOVIN Reviewed; 448 AA.
AC Q0P5L0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=RNA-binding protein 42;
DE AltName: Full=RNA-binding motif protein 42;
GN Name=RBM42;
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=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds (via the RRM domain) to the 3'-untranslated region
CC (UTR) of CDKN1A mRNA. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HNRNPK. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Upon stress response, localizes with HNRNPK in cytoplasmic
CC aggregates of stalled translational preinitiation complexes called
CC stress granules. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM RBM42 family. {ECO:0000305}.
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; BC119904; AAI19905.1; -; mRNA.
DR RefSeq; NP_001069673.1; NM_001076205.1.
DR AlphaFoldDB; Q0P5L0; -.
DR SMR; Q0P5L0; -.
DR STRING; 9913.ENSBTAP00000017884; -.
DR PaxDb; Q0P5L0; -.
DR PRIDE; Q0P5L0; -.
DR GeneID; 540172; -.
DR KEGG; bta:540172; -.
DR CTD; 79171; -.
DR eggNOG; KOG0226; Eukaryota.
DR InParanoid; Q0P5L0; -.
DR OrthoDB; 1249623at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR CDD; cd12383; RRM_RBM42; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034215; RBM42_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BTD8"
FT CHAIN 2..448
FT /note="RNA-binding protein 42"
FT /id="PRO_0000307749"
FT DOMAIN 349..427
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..448
FT /note="Necessary for interaction with HNRNPK"
FT /evidence="ECO:0000250"
FT REGION 286..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTD8"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTD8"
FT MOD_RES 149
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTD8"
SQ SEQUENCE 448 AA; 47187 MW; F74332BD3A707A61 CRC64;
MAGAGPAPGL PGAGGPVVPG PGAGIPGKSG EERLKEMEAE MALFEQEVLG APVTGIPTAV
PAVPTVPTVE AMQVPAAPVI RPIIATNTYQ QVQQTLEARA AAAATVVPPM VGGPPFVGPV
GFGPGDRSHL DSPEAREAMF LRRAAAGPRP MALRPPHQAL VGPPLPGPPG PPMMLPPMAR
APGPPLGSMA ALRPPLEEPA TPRELGLGLG LGLKEKEEAV VAAAAGLEEA SAVVAVGAGG
APAGPAVIGP SLPLALAMPL PEPEPLPLPL EVVRGLLPPL RIPELLSLRP RPRPPRPEPP
PGLMALEVPE PLSEDKKKGK PEKLKRCIRT AAGSSWEDPS LLEWDADDFR IFCGDLGNEV
NDDILARAFS RFPSFLKAKV IRDKRTGKTK GYGFVSFKDP SDYVRAMREM NGKYVGSRPI
KLRKSMWKDR NLDVVRKKQK EKKKLGLR