RBM7_BOVIN
ID RBM7_BOVIN Reviewed; 262 AA.
AC Q3MHY8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=RNA-binding protein 7 {ECO:0000250|UniProtKB:Q9Y580};
DE AltName: Full=RNA-binding motif protein 7 {ECO:0000250|UniProtKB:Q9Y580};
GN Name=RBM7 {ECO:0000250|UniProtKB:Q9Y580};
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=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding subunit of the trimeric nuclear exosome targeting
CC (NEXT) complex, a complex that functions as an RNA exosome cofactor
CC that directs a subset of non-coding short-lived RNAs for exosomal
CC degradation. NEXT is involved in surveillance and turnover of aberrant
CC transcripts and non-coding RNAs. Binds preferentially polyuridine
CC sequences and associates with newly synthesized RNAs, including pre-
CC mRNAs and short-lived exosome substrates such as promoter upstream
CC transcripts (PROMPTs), enhancer RNAs (eRNAs), and 3'-extended products
CC from small nuclear RNAs (snRNAs). Participates in several biological
CC processes including DNA damage response (DDR) and stress response.
CC During stress response, activation of the p38MAPK-MK2 pathway decreases
CC RBM7-RNA-binding and subsequently the RNA exosome degradation
CC activities, thereby modulating the turnover of non-coding
CC transcriptome. Participates in DNA damage response (DDR), through its
CC interaction with MEPCE and LARP7, the core subunits of 7SK snRNP
CC complex, that release the positive transcription elongation factor b
CC (P-TEFb) complex from the 7SK snRNP. In turn, activation of P-TEFb
CC complex induces the transcription of P-TEFb-dependent DDR genes to
CC promote cell viability. {ECO:0000250|UniProtKB:Q9Y580}.
CC -!- SUBUNIT: Component of the nuclear exosome targeting (NEXT) complex
CC composed of MTREX, ZCCHC8, and RBM7 that directs a subset of non-coding
CC short-lived RNAs for exosomal degradation. Interacts with ZCCHC8 and
CC SF3B2/SAP145. Binds to MTREX through ZCCHC8. Interacts with YWHAE and
CC YWHAZ; these interactions are stress-dependent and RBM7 phosphorylation
CC dependent; release RNA from the NEXT complex and may affect RNA
CC targeting to the nuclear RNA exosomome for degradation. Interacts with
CC MEPCE and LARP7, the core subunits of 7SK snRNP; upon genotoxic stress
CC this interaction is enhanced, triggering the release of inactive P-TEFb
CC complex from the core and P-TEFb complex activation.
CC {ECO:0000250|UniProtKB:Q9Y580}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9Y580}. Nucleus {ECO:0000250|UniProtKB:Q9CQT2}.
CC Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:Q9Y580}.
CC -!- DOMAIN: The RRM domain mediates RNA binding; the RNA must have four
CC nucleotides for efficient binding. Mediates the interaction of NEXT
CC complex with promoter upstream transcripts (PROMPTs) and potentially
CC aberrant forms of other non coding RNAs, such as snRNAs. The RRM domain
CC exhibits specificity for polyuridine sequences.
CC {ECO:0000250|UniProtKB:Q9Y580}.
CC -!- PTM: Phosphorylated at Ser-133 by MAPK14/p38-alpha-activated
CC MAPKAPK2/MK2; this phosphorylation is stress-dependent; this
CC phosphorylation decreases its RNA-binding capacity therefore affecting
CC RNA nuclear exosome-mediated degradation. This phosphorylation mediates
CC YWHAE and YWHAZ interactions. {ECO:0000250|UniProtKB:Q9Y580}.
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; BC104518; AAI04519.1; -; mRNA.
DR RefSeq; NP_001029659.1; NM_001034487.1.
DR AlphaFoldDB; Q3MHY8; -.
DR SMR; Q3MHY8; -.
DR STRING; 9913.ENSBTAP00000010804; -.
DR PaxDb; Q3MHY8; -.
DR Ensembl; ENSBTAT00000010804; ENSBTAP00000010804; ENSBTAG00000008219.
DR GeneID; 515307; -.
DR KEGG; bta:515307; -.
DR CTD; 10179; -.
DR VEuPathDB; HostDB:ENSBTAG00000008219; -.
DR eggNOG; KOG4454; Eukaryota.
DR GeneTree; ENSGT00870000136493; -.
DR HOGENOM; CLU_087967_0_0_1; -.
DR InParanoid; Q3MHY8; -.
DR OMA; SHDYDSR; -.
DR OrthoDB; 1298240at2759; -.
DR TreeFam; TF323596; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000008219; Expressed in endometrium and 107 other tissues.
DR ExpressionAtlas; Q3MHY8; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd12592; RRM_RBM7; 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; IPR034500; RBM7_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; Meiosis; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y580"
FT CHAIN 2..262
FT /note="RNA-binding protein 7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000230990"
FT DOMAIN 10..87
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 25..35
FT /note="ZCCHC8 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y580"
FT REGION 59..76
FT /note="ZCCHC8 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y580"
FT REGION 95..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y580"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQT2"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQT2"
FT MOD_RES 149
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y580"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y580"
SQ SEQUENCE 262 AA; 29963 MW; 9EEE7CDADC4B779F CRC64;
MGAAAAEADR TLFVGNLETK VTEELLFELF HQAGPVIKVK IPKDKDGKPK QFAFVNFKHE
VSVPYAMNLL NGIKLFGRPI KIQFRAGSSH ASQEVSLSYP QHHVGNSSPT STSPSRTVDN
MTPSAQTIQR SFSSSENFQR QAVMNNVLRQ MSYGGKFGSP HLDQSGFSPS AQSHNHTFNQ
SSSSQWRQDT PSSQRKVRLN SHPYVMDRHY SREQRYSDLS DHHYRGNRDD FFYEDRNHDG
WSHDYDNRRD SGRNGKWRSS RH
