RBM5A_XENLA
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 03-AUG-2022, entry version 63.
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}.
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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 CTD; 779346; -.
DR Xenbase; XB-GENE-494991; rbm5.L.
DR OMA; TIMGVIR; -.
DR OrthoDB; 786674at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 779346; Expressed in brain and 19 other 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; cd12752; RRM1_RBM5; 1.
DR CDD; cd12755; RRM2_RBM5; 1.
DR Gene3D; 3.30.70.330; -; 2.
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; IPR033094; RBM5.
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:SF21; PTHR13948:SF21; 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; SSF54928; SSF54928; 2.
DR SUPFAM; SSF90209; SSF90209; 1.
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
