ID   RBM22_XENLA             Reviewed;         417 AA.
AC   Q7ZXB5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Pre-mRNA-splicing factor RBM22;
DE   AltName: Full=RNA-binding motif protein 22;
GN   Name=rbm22;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-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; BC045067; AAH45067.1; -; mRNA.
DR   RefSeq; NP_001080776.1; NM_001087307.1.
DR   AlphaFoldDB; Q7ZXB5; -.
DR   SMR; Q7ZXB5; -.
DR   BioGRID; 98711; 1.
DR   IntAct; Q7ZXB5; 1.
DR   MaxQB; Q7ZXB5; -.
DR   DNASU; 380469; -.
DR   GeneID; 380469; -.
DR   KEGG; xla:380469; -.
DR   CTD; 380469; -.
DR   Xenbase; XB-GENE-971204; rbm22.S.
DR   OMA; PYFRKGR; -.
DR   OrthoDB; 1272857at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 380469; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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_0000250553"
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..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..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        369..394
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   417 AA;  46538 MW;  B3D0A2925D767544 CRC64;
     MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR PFTVFRWCPG
     VRMRFKKTEV CQTCSKLKNV CQTCLLDLEY GLPIQVRDTG VSLKDEMPRS DVNKEYYTQN
     MEREIANSDG TRPVGALGKA TSSSDMLLKL ARTTPYYKRN RPHICSFWVK GECKRGEECP
     YRHEKPTDPD DPLADQNIKD RFYGINDPVA DKLLKRASTM PRLDPPEDKS ITTLYVGGLG
     DTISESELRN HFYQFGEIRT ITVVQRQQCA FIQFATRQSA ETAAEKSFNK LIVNGRRLNV
     KWGRSQAARG KEREHDGSGD PGMKFEPVPG LPGALPPPPT EEESSANYFN LPPNGSAALV
     NISLPPPPGL SGPPPGFGPH MFPPMAPPPF LRAPGHIHYP SQDPQRMGAH AGKPSSG