RBM5_RAT
ID RBM5_RAT Reviewed; 815 AA.
AC B2GV05;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=RNA-binding protein 5;
DE AltName: Full=RNA-binding motif protein 5;
GN Name=Rbm5;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-78; SER-621 AND
RP SER-624, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. May both positively and negatively regulate apoptosis by
CC regulating the alternative splicing of several genes involved in this
CC process, including FAS and CASP2/caspase-2. In the case of FAS,
CC promotes production of a soluble form of FAS that inhibits apoptosis.
CC In the case of CASP2/caspase-2, promotes production of a catalytically
CC active form of CASP2/Caspase-2 that induces apoptosis (By similarity).
CC {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.
CC Interacts with U2AF2; this interaction is direct. Also interacts with
CC ACIN1, PRPF8, SFRS3, SNRPB, SNRPN, SNRNP70 and SNRNP200; these
CC interactions may be indirect (By 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; CH473954; EDL77217.1; -; Genomic_DNA.
DR EMBL; BC166477; AAI66477.1; -; mRNA.
DR RefSeq; NP_001094018.1; NM_001100548.1.
DR RefSeq; XP_006243800.1; XM_006243738.3.
DR RefSeq; XP_006243801.1; XM_006243739.3.
DR AlphaFoldDB; B2GV05; -.
DR BMRB; B2GV05; -.
DR STRING; 10116.ENSRNOP00000024529; -.
DR iPTMnet; B2GV05; -.
DR PhosphoSitePlus; B2GV05; -.
DR jPOST; B2GV05; -.
DR PaxDb; B2GV05; -.
DR PeptideAtlas; B2GV05; -.
DR PRIDE; B2GV05; -.
DR GeneID; 300996; -.
DR KEGG; rno:300996; -.
DR UCSC; RGD:1305059; rat.
DR CTD; 10181; -.
DR RGD; 1305059; Rbm5.
DR VEuPathDB; HostDB:ENSRNOG00000018153; -.
DR eggNOG; KOG0154; Eukaryota.
DR InParanoid; B2GV05; -.
DR OMA; TIMGVIR; -.
DR OrthoDB; 786674at2759; -.
DR PhylomeDB; B2GV05; -.
DR TreeFam; TF315789; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:B2GV05; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000018153; Expressed in thymus and 20 other tissues.
DR Genevisible; B2GV05; RN.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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 1: Evidence at protein level;
KW Apoptosis; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spliceosome; Zinc;
KW Zinc-finger.
FT CHAIN 1..815
FT /note="RNA-binding protein 5"
FT /id="PRO_0000376805"
FT DOMAIN 98..178
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 231..315
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 743..789
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 181..210
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 647..672
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..809
FT /note="Required for interaction with U2AF2"
FT /evidence="ECO:0000250"
FT REGION 407..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..535
FT /note="Sufficient for interaction with ACIN1, PRPF8, SFRS3,
FT SNRPB, SNRPN, SNRNP70 and SNRNP200"
FT /evidence="ECO:0000250"
FT REGION 508..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52756"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52756"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52756"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52756"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 815 AA; 92352 MW; 6A76B02ECD879813 CRC64;
MGSDKRVSRT ERSGRYGSII DRDDRDERES RSRRRDSDYK RSSDDRRGDR YDDYRDYDSP
ERERERRNSD RSEDGYHSDG DYGEHDYRHD ISDERESKTI MLRGLPITIT ESDIREMMES
FEGPQPADVR LMKRKTGVSR GFAFVEFYHL QDATSWMEAN QKKLVIQGKH IAMHYSNPRP
KFEDWLCNKC CLNNFRKRLK CFRCGADKFD SEQEVPPGTT ESVQSVDYYC DTIILRNIAP
HTVVDSIMTA LSPYASLAVN NIRLIKDKQT QQNRGFAFVQ LSSAMDASQL LQILQSLHPP
LKIDGKTIGV DFAKSARKDL VLPDGNRVSA FSVASTAIAA AQWSSTQSQS GEGGNVDYSY
MQPGQDGYTQ YTQYSQDYQQ FYQQQTGGLE SDASATSGTT VTTTSAAVVS QSPQLYNQTS
NPPGSPTEEA QPSTSTSTQA PAASPTGVVP GTKYAVPDTS TYQYDESSGY YYDPTTGLYY
DPNSQYYYNS LTQQYLYWDG EKETYVPAAE SSSNQQAGLP STKEGKEKKE KPKSKTAQQI
AKDMERWAKS LNKQKENFKN SFQPVNSLRE EERRESAAAD AGFALFEKKG ALAERQQLIP
ELVRNGDEEN PLKRGLVAAY SGDSDNEEEL VERLESEEEK LADWKKMACL LCRRQFPNRD
ALVRHQQLSD LHKQNMDIYR RSRLSEQELE ALELREREMK YRDRAAERRE KYGIPEPPEP
KRKKQFDAGT VNYEQPTKDG IDHSNIGNKM LQAMGWREGS GLGRKCQGIT APIEAQVRLK
GAGLGAKGSA YGLSGADSYK DAVRKAMFAR FTEME
