RBM22_BOVIN
ID RBM22_BOVIN Reviewed; 420 AA.
AC Q3B7L8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Pre-mRNA-splicing factor RBM22;
DE AltName: Full=RNA-binding motif protein 22;
GN Name=RBM22;
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 (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the activated
CC spliceosome. Involved in the first step of pre-mRNA splicing. Binds
CC directly to the internal stem-loop (ISL) domain of the U6 snRNA and to
CC the pre-mRNA intron near the 5' splice site during the activation and
CC catalytic phases of the spliceosome cycle. Involved in both
CC translocations of the nuclear SLU7 to the cytoplasm and the cytosolic
CC calcium-binding protein PDCD6 to the nucleus upon cellular stress
CC responses. {ECO:0000250|UniProtKB:Q9NW64}.
CC -!- SUBUNIT: Component of the pre-catalytic and catalytic spliceosome
CC complexes. Component of the postcatalytic spliceosome P complex.
CC Interacts with PDCD6; the interaction induces translocation of PDCD6 in
CC the cytoplasm. Interacts with PPIL1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NW64}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NW64}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NW64}. Note=Nearly exclusively nuclear.
CC Translocated from the nucleus to the cytoplasm after heat shock cell
CC treatment. May be shuttling between the nucleus and the cytosol.
CC {ECO:0000250|UniProtKB:Q9NW64}.
CC -!- DOMAIN: The C-terminal RRM domain and the zinc finger motif are
CC necessary for RNA-binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLT11 family. {ECO:0000305}.
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DR EMBL; BC107551; AAI07552.1; -; mRNA.
DR RefSeq; NP_001032907.1; NM_001037818.1.
DR AlphaFoldDB; Q3B7L8; -.
DR SMR; Q3B7L8; -.
DR STRING; 9913.ENSBTAP00000040478; -.
DR PaxDb; Q3B7L8; -.
DR PRIDE; Q3B7L8; -.
DR GeneID; 512330; -.
DR KEGG; bta:512330; -.
DR CTD; 55696; -.
DR eggNOG; KOG0153; Eukaryota.
DR InParanoid; Q3B7L8; -.
DR OrthoDB; 1272857at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IBA:GO_Central.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036002; F:pre-mRNA binding; ISS:UniProtKB.
DR GO; GO:0017070; F:U6 snRNA binding; ISS:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR039171; Cwc2/Slt11.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR14089; PTHR14089; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Isopeptide bond; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Spliceosome; Transport; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT CHAIN 2..420
FT /note="Pre-mRNA-splicing factor RBM22"
FT /id="PRO_0000250545"
FT DOMAIN 232..305
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 159..186
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 303..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
SQ SEQUENCE 420 AA; 46930 MW; 2A230BD62C88C7DE CRC64;
MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR PFTVFRWCPG
VRMRFKKTEV CQTCSKLKNV CQTCLLDLEY GLPIQVRDAG LSFKDDMPKS DVNKEYYTQN
MEREISNSDG TRPVGMLGKA TSTSDMLLKL ARTTPYYKRN RPHICSFWVK GECKRGEECP
YRHEKPTDPD DPLADQNIKD RYYGINDPVA DKLLKRASTM PRLDPPEDKT ITTLYVGGLG
DTITETDLRN HFYQFGEIRT ITVVQRQQCA FIQFATRQAA EVAAEKSFNK FIVNGRRLNV
KWGRSQAARG KEKEKDGTTD SGIKLEPVPG LPGALPPPPA AEEEASANYF NLPPSGPPAV
VNIALPPPPG IAPPPPPGFG PHMFHPMGPP PPFMRAPGPI HYPSQDPQRM GAHAGKHSSP
