RBM22_XENTR
ID RBM22_XENTR Reviewed; 417 AA.
AC Q6P616;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Pre-mRNA-splicing factor RBM22;
DE AltName: Full=RNA-binding motif protein 22;
GN Name=rbm22; ORFNames=TEgg040d02.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2003) 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.
CC {ECO:0000250|UniProtKB:Q9NW64}.
CC -!- SUBUNIT: Component of the pre-catalytic and catalytic spliceosome
CC complexes. Component of the postcatalytic spliceosome P complex.
CC {ECO:0000250|UniProtKB:Q9NW64}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NW64}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NW64}. Note=Nearly exclusively nuclear. May be
CC 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; CR761977; CAJ81393.1; -; mRNA.
DR EMBL; BC062518; AAH62518.1; -; mRNA.
DR RefSeq; NP_989108.1; NM_203777.1.
DR AlphaFoldDB; Q6P616; -.
DR SMR; Q6P616; -.
DR STRING; 8364.ENSXETP00000044114; -.
DR PaxDb; Q6P616; -.
DR Ensembl; ENSXETT00000044114; ENSXETP00000044114; ENSXETG00000020435.
DR GeneID; 394713; -.
DR KEGG; xtr:394713; -.
DR CTD; 55696; -.
DR Xenbase; XB-GENE-971198; rbm22.
DR eggNOG; KOG0153; Eukaryota.
DR HOGENOM; CLU_027112_3_0_1; -.
DR InParanoid; Q6P616; -.
DR OMA; QGQHYPY; -.
DR OrthoDB; 1272857at2759; -.
DR PhylomeDB; Q6P616; -.
DR TreeFam; TF314284; -.
DR Reactome; R-XTR-72163; mRNA Splicing - Major Pathway.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000020435; Expressed in gastrula and 19 other tissues.
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:0045292; P:mRNA cis splicing, via spliceosome; 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 Cytoplasm; Developmental protein; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; RNA-binding; Spliceosome; Zinc;
KW Zinc-finger.
FT CHAIN 1..417
FT /note="Pre-mRNA-splicing factor RBM22"
FT /id="PRO_0000250554"
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..417
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 343..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..394
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 46541 MW; 40AEAE24F27A0512 CRC64;
MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR PFTVFRWCPG
VRMRFKKTEV CQTCSKLKNV CQTCLLDLEY GLPIQVRDAG ASLKDEMPRS DVNKEYYTQN
MEREIANSDG TRPVGALGKA TSSSDMLLKL ARTTPYYKRN RPHICSFWVK GECKRGEECP
YRHEKPTDPD DPLADQNIKD RYYGINDPVA DKLLKRASTM PRLDPPEDKS ITTLYVGGLG
DTISESELRN HFYQFGEIRT ITVVQRQQCA FIQFATRQAA EMAAEKSFNK LIVNGRRLNV
KWGRSQAARG KERERDGSSD PGMKLEPVPG LPGALPPPPT EEESSANYFN LPPNGSAALV
NISLPPPPGL SGPPPGYGPH MFPPMAPPPF LRAPGHIHYP SQDPQRMGAH AGKPSSG