ID   RBM22_CHICK             Reviewed;         420 AA.
AC   Q5ZM16;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Pre-mRNA-splicing factor RBM22;
DE   AltName: Full=RNA-binding motif protein 22;
GN   Name=RBM22; ORFNames=RCJMB04_3g16;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719568; CAG31227.1; -; mRNA.
DR   RefSeq; NP_001006151.1; NM_001006151.1.
DR   AlphaFoldDB; Q5ZM16; -.
DR   SMR; Q5ZM16; -.
DR   STRING; 9031.ENSGALP00000007237; -.
DR   PaxDb; Q5ZM16; -.
DR   GeneID; 416270; -.
DR   KEGG; gga:416270; -.
DR   CTD; 55696; -.
DR   VEuPathDB; HostDB:geneid_416270; -.
DR   eggNOG; KOG0153; Eukaryota.
DR   InParanoid; Q5ZM16; -.
DR   OrthoDB; 1272857at2759; -.
DR   PhylomeDB; Q5ZM16; -.
DR   PRO; PR:Q5ZM16; -.
DR   Proteomes; UP000000539; 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: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; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT   CHAIN           1..420
FT                   /note="Pre-mRNA-splicing factor RBM22"
FT                   /id="PRO_0000250551"
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"
SQ   SEQUENCE   420 AA;  46776 MW;  8DE3BC3946661872 CRC64;
     MSTSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR PFTVFRWCPG
     VRMRFKKTEV CQTCSKLKNV CQTCLLDLEY GLPIQVRDAG LSLKDEMPKS DVNKEYYTQN
     MEREIANSDG TRPVGALGKA TSTSDMLLKL ARTTPYYKRN RPHICSFWVK GECKRGEECP
     YRHEKPTDPD DPLADQDIKD RYYGINDPVA DKLLKRASTM PRLDPPDDKT ITTLYVGGLG
     DTITESDLRN HFYQFGEIRT ITVVQRQQCA FIQFATRQAA EVAAEKSFNK LIVNGRRLNV
     KWGRSQAARG KEKDKEGTTE SGIKLEPVPG LPGALPPPPA AEEEASANYF NLPPSGPPAV
     VNIALPPPPG IAPPPPPGFG PHMFHAMGPP PPFMRAPGPI HYPSQDPQRM GAHAGKHSSP