RBM5B_XENLA
ID RBM5B_XENLA Reviewed; 749 AA.
AC Q6DDU9;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=RNA-binding protein 5-B;
DE AltName: Full=RNA-binding motif protein 5-B;
GN Name=rbm5-b;
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 (JUL-2004) 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; BC077408; AAH77408.1; -; mRNA.
DR RefSeq; NP_001086761.1; NM_001093292.1.
DR AlphaFoldDB; Q6DDU9; -.
DR PRIDE; Q6DDU9; -.
DR DNASU; 446596; -.
DR GeneID; 446596; -.
DR KEGG; xla:446596; -.
DR CTD; 446596; -.
DR Xenbase; XB-GENE-6256678; rbm5.S.
DR OMA; ELREREX; -.
DR OrthoDB; 786674at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 446596; 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; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR13948:SF21; PTHR13948:SF21; 2.
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.
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..749
FT /note="RNA-binding protein 5-B"
FT /id="PRO_0000376807"
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 677..723
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 REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 84292 MW; 94F9860052BE0D5B CRC64;
MGSDKRVSRS ERSGRYGSAF DRDDRDDRDS RSRRRDSEYK RYRDERNDQY DDYRDYESPE
RERMRDRERR NSDRSEDGYH SDGDYMDHDY RQDYYMDEKE SKTIMLRGLP ININENDIRE
LVESFEGPQP ADVRLMKRKT GLSRGFAFVE FYHLQDATRW MEANQKKLVI QGKTIAMHYS
NPRPKFEDWL CNKCGLYNFR RRLKCFRCGA AKAESDMEAP SGSSETPQSA DYYSDSGYVS
SAIILRNIGP HTVVDSILSA LAPYVSLVVS NIRLIKDKQT QQNRGFAFVQ LPSALEASQL
LQILQTLHPP LKIDGKTIGV DFAKSARKDL VLPDGHRVSA FSVASTAIAA AQWSATQPAQ
QSGEAGDYAY LQQGQEGNSN FGQCSQDYQP FYQTQTAAVD QDTAPQSEGS PVPATTSAVV
CQSPQMYQQP GSPTQSGTST AASTTPASTT STEEATTPTA IVPGVKYSVP DTSTYQYDES
SGYYYDPQTG LYYDPNSQYY YNSLTQQYLY WDGEKQTYLP AADGTGQSGA QPNGANPGTS
KEGKEKKEKP KSKTAQQIAK DMERWAKSLN KQKENFKNSF QPLSSRDEER KESAAADAGF
ALFEKKQGAL FERQFLPDMM MMMVNTEEEK PPNAKYRDRA AERREKYGIP EPPEPKRKRF
DPTVVNYEQP TKDGIDNSNI GNKMLQAMGW KEGSGLGRKS QGITAPIQAQ VRMRGAGLGA
KGSSYGVNTS DSYKDAVKKA MFARFSEME
