ID RBM5A_XENLA Reviewed; 833 AA. AC A0JMV4; DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 68. DE RecName: Full=RNA-binding protein 5-A; DE AltName: Full=RNA-binding motif protein 5-A; GN Name=rbm5-a; Synonyms=rbm5; 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=Ovary; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the spliceosome A complex. Regulates alternative CC splicing of a number of mRNAs. May modulate splice site pairing after CC recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of CC the intron (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Component of the spliceosome A complex (also known as the CC prespliceosome). Appears to dissociate from the spliceosome upon CC formation of the spliceosome B complex (also known as the precatalytic CC spliceosome), in which the heterotrimeric U4/U6.U5 snRNPs are bound (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RBM5/RBM10 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; BC126019; AAI26020.1; -; mRNA. DR RefSeq; NP_001090434.1; NM_001096965.1. DR RefSeq; XP_018112478.1; XM_018256989.1. DR AlphaFoldDB; A0JMV4; -. DR DNASU; 779346; -. DR GeneID; 779346; -. DR KEGG; xla:779346; -. DR AGR; Xenbase:XB-GENE-494991; -. DR CTD; 779346; -. DR Xenbase; XB-GENE-494991; rbm5.L. DR OMA; CESEHER; -. DR OrthoDB; 298711at2759; -. DR Proteomes; UP000186698; Chromosome 4L. DR Bgee; 779346; Expressed in brain and 19 other cell types or tissues. 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:0003729; F:mRNA binding; ISS:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB. DR GO; GO:0000245; P:spliceosomal complex assembly; ISS:UniProtKB. DR CDD; cd16168; OCRE_RBM5; 1. DR CDD; cd12752; RRM1_RBM5; 1. DR CDD; cd12755; RRM2_RBM5; 1. DR Gene3D; 3.30.70.330; -; 2. DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1. DR InterPro; IPR000467; G_patch_dom. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR041591; OCRE. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR034991; RBM5_RRM1. DR InterPro; IPR034993; RBM5_RRM2. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR013087; Znf_C2H2_type. DR InterPro; IPR001876; Znf_RanBP2. DR InterPro; IPR036443; Znf_RanBP2_sf. DR PANTHER; PTHR13948; RNA-BINDING PROTEIN; 1. DR PANTHER; PTHR13948:SF21; RNA-BINDING PROTEIN 5; 1. DR Pfam; PF01585; G-patch; 1. DR Pfam; PF17780; OCRE; 1. DR Pfam; PF00076; RRM_1; 1. DR Pfam; PF00641; zf-RanBP; 1. DR SMART; SM00443; G_patch; 1. DR SMART; SM00360; RRM; 2. DR SMART; SM00547; ZnF_RBZ; 1. DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50174; G_PATCH; 1. DR PROSITE; PS50102; RRM; 2. DR PROSITE; PS01358; ZF_RANBP2_1; 1. DR PROSITE; PS50199; ZF_RANBP2_2; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. PE 2: Evidence at transcript level; KW Metal-binding; mRNA processing; mRNA splicing; Nucleus; Reference proteome; KW Repeat; RNA-binding; Spliceosome; Zinc; Zinc-finger. FT CHAIN 1..833 FT /note="RNA-binding protein 5-A" FT /id="PRO_0000376806" FT DOMAIN 102..182 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 241..325 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 761..807 FT /note="G-patch" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092" FT ZN_FING 185..214 FT /note="RanBP2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT ZN_FING 667..692 FT /note="C2H2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..87 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 396..458 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 523..559 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 396..454 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 525..540 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 542..559 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 833 AA; 93839 MW; DF5F404E410EB8EE CRC64; MGSDKRVSRS ERSGRYGSGF DRDDRDDRDN RSRRRDSEYK RYRDERSDRY DDYRDYDSPE RDRMRDRERR NSDRSEDGYH SDGDYMDHDY RQDYYMDEKE SKTIMLRGLP ININENDIRE LVESFEGPQP ADVRLMKRKT GLSRGFAFVE FYHLQDSTSW MEANQKKLVI QGKTIAMHYS NPRPKFEDWL CNKCGLYNFR RRLKCFRCGA AKAESDMEAP SGSSEAPQSA DYYSDSGYVS SAIILRNIGP HTVVDSILSA LAPYVSLVVS NIRLIKDKQT QQNRGFAFVQ LPSALEASQL LQILQTLHPP LKIDGKTIGV DFAKSARKDL VLPDGHRVSA FSVASTAIAA AQWSSTQPAQ QSGEGGDYAY LQPGQEGCSN YGQCSQDYQP FYQTQTGAAE QGTAPQAESS SPVPATTSAV VCQSPQMYQQ PGSPTQSSTS TVAASATPAS GTSAEEAAAP NAIVPGLKYS VPDTSTYQYD ESSGYYYDPQ TGLYYDPNSQ YYYNSLTQQY LYWDGEKQTY LPAADGAGQS GTQPNGANPG TSKEGKEKKE KPKSKTAQQI AKDMERWAKS LNKQKENFKN SFQPLRDEER KESAAADAGF ALFEKKQGSL LERQFLPDMM MMVNTEEEKP PNTALVAAYS GDSDNEEENE RFIGAVDDEK LMDWKKLACL LCRRQFPNKD ALTRHQQLSD LHKQNLEVYR RSKLSEQEYE AEQTERESKY RDRAAERRVK YGIPEPPEPK RKRFAPTVVN YEQPTKDGID NSNIGNKMLQ AMGWKEGSGL GRKSQGITAP IQAQVRMRGA GLGAKGSSYG VNTSDSYKDA VRKAMFARFS EME //