ID   RBMX2_RAT               Reviewed;         328 AA.
AC   B0BN49;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=RNA-binding motif protein, X-linked 2;
GN   Name=Rbmx2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in pre-mRNA splicing as component of the activated
CC       spliceosome. {ECO:0000250|UniProtKB:Q9Y388}.
CC   -!- SUBUNIT: Part of the activated spliceosome B/catalytic step 1
CC       spliceosome, one of the forms of the spliceosome which has a well-
CC       formed active site but still cannot catalyze the branching reaction and
CC       is composed of at least 52 proteins, the U2, U5 and U6 snRNAs and the
CC       pre-mRNA. {ECO:0000250|UniProtKB:Q9Y388}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y388}.
CC   -!- SIMILARITY: Belongs to the IST3 family. {ECO:0000305}.
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; BC158684; AAI58685.1; -; mRNA.
DR   RefSeq; NP_001107258.2; NM_001113786.2.
DR   AlphaFoldDB; B0BN49; -.
DR   SMR; B0BN49; -.
DR   STRING; 10116.ENSRNOP00000043159; -.
DR   iPTMnet; B0BN49; -.
DR   PhosphoSitePlus; B0BN49; -.
DR   PaxDb; B0BN49; -.
DR   Ensembl; ENSRNOT00000048922; ENSRNOP00000043159; ENSRNOG00000007371.
DR   GeneID; 367930; -.
DR   KEGG; rno:367930; -.
DR   UCSC; RGD:1562693; rat.
DR   CTD; 51634; -.
DR   RGD; 1562693; Rbmx2.
DR   eggNOG; KOG0126; Eukaryota.
DR   GeneTree; ENSGT00890000139472; -.
DR   HOGENOM; CLU_045495_1_0_1; -.
DR   InParanoid; B0BN49; -.
DR   OMA; ISPEGSW; -.
DR   OrthoDB; 1484811at2759; -.
DR   PhylomeDB; B0BN49; -.
DR   PRO; PR:B0BN49; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000007371; Expressed in testis and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR   GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   CDD; cd12411; RRM_ist3_like; 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; IPR000504; RRM_dom.
DR   InterPro; IPR045844; RRM_Ist3-like.
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   Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; Spliceosome; Ubl conjugation.
FT   CHAIN           1..328
FT                   /note="RNA-binding motif protein, X-linked 2"
FT                   /id="PRO_0000414749"
FT   DOMAIN          36..114
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          118..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..315
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         140
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R0F5"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R0F5"
FT   MOD_RES         274
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y388"
FT   CROSSLNK        8
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y388"
FT   CROSSLNK        246
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y388"
SQ   SEQUENCE   328 AA;  37829 MW;  933009FE1432D6A7 CRC64;
     MNPLTKVKLI NELNEREVQL GVAEKVSWHS EYKDSAWIFL GGLPYELTEG DIICVFSQYG
     EIVNINLVRD KKTGKSKGFC FLCYEDQRST VLAVDNFNGI KIKGRTIRVD HVANYRAPQE
     SEDVDDVTRE LQEKGCGAKT PPSSPPEVSE DEDAKVTKKP KKDKKEKKKK KEKEKTERPV
     QAELPSCSRS KTVKETDEQS AKKHSSKPSE RAQKSECRER KKSHSGSPDG RTSCRGRAEE
     PEWEAKKEKH KHEHKPSSRR EGEEKSRDKD RGRSSGTHSS RHHGHSEGRS HRSRSRSRSR
     SPDRSHRHKK HRYSHERESF HASDRRHY