RBY1A_MOUSE
ID RBY1A_MOUSE Reviewed; 380 AA.
AC O35698; E9Q856;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=RNA-binding motif protein, Y chromosome, family 1 member A1;
DE AltName: Full=RNA-binding motif protein 1;
DE AltName: Full=Y chromosome RNA recognition motif 1;
GN Name=Rbmy1a1; Synonyms=Rbm;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9499427; DOI=10.1093/hmg/7.4.715;
RA Mahadevaiah S.K., Odorisio T., Elliott D.J., Rattigan A., Szot M.,
RA Laval S.H., Washburn L.L., McCarrey J.R., Cattanach B.M., Lovell-Badge R.,
RA Burgoyne P.S.;
RT "Mouse homologues of the human AZF candidate gene RBM are expressed in
RT spermatogonia and spermatids, and map to a Y chromosome deletion interval
RT associated with a high incidence of sperm abnormalities.";
RL Hum. Mol. Genet. 7:715-727(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP INTERACTION WITH SFRS3.
RX PubMed=10823932; DOI=10.1073/pnas.97.11.5717;
RA Elliott D.J., Bourgeois C.F., Klink A., Stevenin J., Cooke H.J.;
RT "A mammalian germ cell-specific RNA-binding protein interacts with
RT ubiquitously expressed proteins involved in splice site selection.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5717-5722(2000).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=12356914; DOI=10.1242/jcs.00111;
RA Turner J.M.A., Mahadevaiah S.K., Elliott D.J., Garchon H.-J., Pehrson J.R.,
RA Jaenisch R., Burgoyne P.S.;
RT "Meiotic sex chromosome inactivation in male mice with targeted disruptions
RT of Xist.";
RL J. Cell Sci. 115:4097-4105(2002).
RN [5]
RP OVEREXPRESSION.
RX PubMed=15051956; DOI=10.1159/000076821;
RA Szot M., Grigoriev V., Mahadevaiah S.K., Ojarikre O.A., Toure A.,
RA von Glasenapp E., Rattigan A., Turner J.M.A., Elliott D.J., Burgoyne P.S.;
RT "Does Rbmy have a role in sperm development in mice?";
RL Cytogenet. Genome Res. 103:330-336(2003).
RN [6]
RP ERRATUM OF PUBMED:15051956.
RA Szot M., Grigoriev V., Mahadevaiah S.K., Ojarikre O.A., Toure A.,
RA von Glasenapp E., Rattigan A., Turner J.M.A., Elliott D.J., Burgoyne P.S.;
RL Cytogenet. Genome Res. 105:160-160(2004).
CC -!- FUNCTION: RNA-binding protein involved in pre-mRNA splicing. Required
CC for sperm development. Acts additively with TRA2B to promote exon 7
CC inclusion of the survival motor neuron SMN. Binds non-specifically to
CC mRNAs.
CC -!- SUBUNIT: Interacts with splicing factor proteins SFRS3/SRP20,
CC TRA2B/SFRS10, KHDRBS1/SAM68 and KHDRBS3. {ECO:0000269|PubMed:10823932}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:9499427}.
CC -!- DEVELOPMENTAL STAGE: Only expressed in spermatogonia and early
CC spermatocytes, suggesting that expression is inactivated in the XY body
CC during meiosis. {ECO:0000269|PubMed:12356914,
CC ECO:0000269|PubMed:9499427}.
CC -!- MISCELLANEOUS: The RBMY1 proteins are encoded by repeated regions of
CC the Y chromosome. The exact number of functional copies is unclear and
CC may vary between individuals, and some of them may represent
CC pseudogenes.
CC -!- MISCELLANEOUS: Overexpression of Rbmy proteins in mice carrying the
CC Y(d1) deletion that removes most of the multi-copy Rbmy gene cluster
CC does not have any effect and fails to reduce the frequency of abnormal
CC sperm. These results raize the question of the role of Rbmy proteins in
CC sperm development.
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DR EMBL; Y15131; CAA75403.1; -; mRNA.
DR EMBL; AC132601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30546.1; -.
DR RefSeq; NP_001159856.1; NM_001166384.1.
DR RefSeq; NP_001257442.1; NM_001270513.1.
DR RefSeq; NP_001257444.1; NM_001270515.1.
DR RefSeq; NP_001257445.1; NM_001270516.1.
DR RefSeq; NP_035383.2; NM_011253.2.
DR AlphaFoldDB; O35698; -.
DR SMR; O35698; -.
DR IntAct; O35698; 1.
DR STRING; 10090.ENSMUSP00000097930; -.
DR iPTMnet; O35698; -.
DR PhosphoSitePlus; O35698; -.
DR PaxDb; O35698; -.
DR PRIDE; O35698; -.
DR DNASU; 19657; -.
DR Ensembl; ENSMUST00000100360; ENSMUSP00000097930; ENSMUSG00000094658.
DR Ensembl; ENSMUST00000169382; ENSMUSP00000129249; ENSMUSG00000093987.
DR Ensembl; ENSMUST00000171534; ENSMUSP00000130080; ENSMUSG00000094658.
DR Ensembl; ENSMUST00000179508; ENSMUSP00000136939; ENSMUSG00000093918.
DR Ensembl; ENSMUST00000180310; ENSMUSP00000137266; ENSMUSG00000095948.
DR Ensembl; ENSMUST00000187277; ENSMUSP00000140704; ENSMUSG00000093987.
DR Ensembl; ENSMUST00000188091; ENSMUSP00000140216; ENSMUSG00000095948.
DR Ensembl; ENSMUST00000189592; ENSMUSP00000139527; ENSMUSG00000093918.
DR Ensembl; ENSMUST00000190283; ENSMUSP00000139659; ENSMUSG00000095948.
DR GeneID; 100862365; -.
DR GeneID; 100862394; -.
DR GeneID; 100862398; -.
DR GeneID; 19657; -.
DR KEGG; mmu:100862365; -.
DR KEGG; mmu:100862394; -.
DR KEGG; mmu:100862398; -.
DR KEGG; mmu:19657; -.
DR UCSC; uc009uzq.2; mouse.
DR CTD; 19657; -.
DR MGI; MGI:104732; Rbmy1a1.
DR VEuPathDB; HostDB:ENSMUSG00000093918; -.
DR VEuPathDB; HostDB:ENSMUSG00000093987; -.
DR VEuPathDB; HostDB:ENSMUSG00000094658; -.
DR VEuPathDB; HostDB:ENSMUSG00000095948; -.
DR eggNOG; ENOG502QS9N; Eukaryota.
DR GeneTree; ENSGT00940000163524; -.
DR HOGENOM; CLU_042286_0_0_1; -.
DR InParanoid; O35698; -.
DR OrthoDB; 1579773at2759; -.
DR PhylomeDB; O35698; -.
DR TreeFam; TF331833; -.
DR BioGRID-ORCS; 100862365; 0 hits in 9 CRISPR screens.
DR BioGRID-ORCS; 100862394; 0 hits in 7 CRISPR screens.
DR BioGRID-ORCS; 100862398; 0 hits in 14 CRISPR screens.
DR BioGRID-ORCS; 19657; 1 hit in 23 CRISPR screens.
DR PRO; PR:O35698; -.
DR Proteomes; UP000000589; Chromosome Y.
DR RNAct; O35698; protein.
DR Bgee; ENSMUSG00000093918; Expressed in testis.
DR Genevisible; O35698; MM.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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 Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Activator; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..380
FT /note="RNA-binding motif protein, Y chromosome, family 1
FT member A1"
FT /id="PRO_0000341540"
FT DOMAIN 8..86
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 82..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 183
FT /note="E -> A (in Ref. 1; CAA75403)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 43216 MW; 2B086AA82BF22A85 CRC64;
MAETNQPGKI FIGGLNIKTR QKTLQEIFGR FGPVARVILM RDRETKKSRG FAFLTFRRLA
DAKNAVKEMN GVILDGKRIK VKQARRPSSL ESGSKKRPPS FSRTRGASRI LKCGRGGRSR
ARSGPSCEGN LGGDRYTPNF NVSSSGRHFA VKRNPSSKRD DPPSKRSATS AQTRSNTGLR
GREPHRREIS RNMPRGEPAS SRRDEYPLPR DYGQSSNDRK YESTSRGYCD YGNYHSREES
ASKVFSDHAG YLGGRDRDFS EYLSGNSYRD TYRSYGRFHE APSARGGNNR YDDYSNSQDG
YGGRGEPYIS NRSNIYSSDY ERSGRQEVLP PPIDREYFDR EGRQERGHSP KDGLYSASRE
SYSSNTKIWG IPWRSWRKQI
