RO60_MOUSE
ID RO60_MOUSE Reviewed; 538 AA.
AC O08848; Q9QYD8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=RNA-binding protein Ro60 {ECO:0000312|MGI:MGI:106652};
DE AltName: Full=60 kDa SS-A/Ro ribonucleoprotein {ECO:0000305};
DE Short=60 kDa Ro protein;
DE Short=60 kDa ribonucleoprotein Ro;
DE Short=RoRNP;
DE AltName: Full=TROVE domain family member 2 {ECO:0000250|UniProtKB:P10155};
GN Name=RO60 {ECO:0000312|MGI:MGI:106652};
GN Synonyms=Ssa2 {ECO:0000312|MGI:MGI:106652},
GN Trove2 {ECO:0000312|MGI:MGI:106652};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=9112230; DOI=10.1007/bf00351170;
RA Wang D., Buyon J.P., Chan E.K.L.;
RT "Cloning and expression of mouse 60 kDa ribonucleoprotein SS-A/Ro.";
RL Mol. Biol. Rep. 23:205-210(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=11196703; DOI=10.1038/sj.gene.6363675;
RA Kaufman K.M., Farris A.D., Gross J.K., Kirby M.Y., Harley J.B.;
RT "Characterization and genomic sequence of the murine 60 kD Ro gene.";
RL Genes Immun. 1:265-270(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-538.
RX PubMed=10323459;
RX DOI=10.1002/1529-0131(199905)42:5<1017::aid-anr22>3.0.co;2-7;
RA Scofield R.H., Kaufman K.M., Baber U., James J.A., Harley J.B.,
RA Kurien B.T.;
RT "Immunization of mice with human 60-kd Ro peptides results in epitope
RT spreading if the peptides are highly homologous between human and mouse.";
RL Arthritis Rheum. 42:1017-1024(1999).
RN [4]
RP PROTEIN SEQUENCE OF 271-283, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21289087; DOI=10.1091/mbc.e10-07-0596;
RA Lai C.K., Gupta N., Wen X., Rangell L., Chih B., Peterson A.S., Bazan J.F.,
RA Li L., Scales S.J.;
RT "Functional characterization of putative cilia genes by high-content
RT analysis.";
RL Mol. Biol. Cell 22:1104-1119(2011).
CC -!- FUNCTION: RNA-binding protein that binds to misfolded non-coding RNAs,
CC pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y
CC RNAs (By similarity). May play roles in cilia formation and/or
CC maintenance (PubMed:21289087). {ECO:0000250|UniProtKB:P10155,
CC ECO:0000269|PubMed:21289087}.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs (By similarity). Found in a complex with
CC PUF60 and Y5 RNA (By similarity). Interacts with RAB11FIP5 (By
CC similarity). {ECO:0000250|UniProtKB:P10155}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P10155}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs. {ECO:0000250|UniProtKB:P10155}.
CC -!- TISSUE SPECIFICITY: Highest in brain, followed by lung, muscle, kidney
CC and heart. Lower levels are found in testis, liver and spleen.
CC {ECO:0000269|PubMed:9112230}.
CC -!- DOMAIN: The horseshoe-shaped TROVE domain is built with 7 helical HEAT-
CC like repeats, and is closed by the VWFA-like domain giving rise to a
CC ring-shaped monomer. Single-stranded RNA is bound in the positively
CC charged central cavity (By similarity). {ECO:0000250|UniProtKB:P42700}.
CC -!- DOMAIN: The MIDAS-like motif in the VWFA-like domain binds divalent
CC metal cations. {ECO:0000250|UniProtKB:P42700}.
CC -!- DISRUPTION PHENOTYPE: Cilia absent or reduced, virtually no cilia of
CC the normal 5 uM mean length. {ECO:0000269|PubMed:21289087}.
CC -!- SIMILARITY: Belongs to the Ro 60 kDa family. {ECO:0000305}.
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DR EMBL; U66843; AAC53142.1; -; mRNA.
DR EMBL; AF065398; AAF19049.1; -; Genomic_DNA.
DR EMBL; AF042139; AAC15667.1; -; Genomic_DNA.
DR CCDS; CCDS15345.1; -.
DR RefSeq; NP_038863.1; NM_013835.2.
DR RefSeq; XP_017174940.1; XM_017319451.1.
DR AlphaFoldDB; O08848; -.
DR SMR; O08848; -.
DR BioGRID; 203507; 40.
DR IntAct; O08848; 2.
DR STRING; 10090.ENSMUSP00000125623; -.
DR iPTMnet; O08848; -.
DR PhosphoSitePlus; O08848; -.
DR EPD; O08848; -.
DR PaxDb; O08848; -.
DR PeptideAtlas; O08848; -.
DR PRIDE; O08848; -.
DR ProteomicsDB; 301632; -.
DR Antibodypedia; 1048; 381 antibodies from 35 providers.
DR DNASU; 20822; -.
DR Ensembl; ENSMUST00000159879; ENSMUSP00000125623; ENSMUSG00000018199.
DR GeneID; 20822; -.
DR KEGG; mmu:20822; -.
DR UCSC; uc007cxd.1; mouse.
DR CTD; 6738; -.
DR MGI; MGI:106652; Ro60.
DR VEuPathDB; HostDB:ENSMUSG00000018199; -.
DR eggNOG; KOG4465; Eukaryota.
DR GeneTree; ENSGT00390000006200; -.
DR HOGENOM; CLU_024421_1_0_1; -.
DR InParanoid; O08848; -.
DR OMA; WWYEWLK; -.
DR OrthoDB; 472016at2759; -.
DR PhylomeDB; O08848; -.
DR TreeFam; TF105990; -.
DR BioGRID-ORCS; 20822; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Ro60; mouse.
DR PRO; PR:O08848; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O08848; protein.
DR Bgee; ENSMUSG00000018199; Expressed in superior surface of tongue and 248 other tissues.
DR ExpressionAtlas; O08848; baseline and differential.
DR Genevisible; O08848; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034336; F:misfolded RNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0030620; F:U2 snRNA binding; IDA:MGI.
DR GO; GO:0035457; P:cellular response to interferon-alpha; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0002520; P:immune system development; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0009411; P:response to UV; IDA:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR Gene3D; 3.40.50.410; -; 2.
DR InterPro; IPR040322; TROVE2.
DR InterPro; IPR008858; TROVE_dom.
DR InterPro; IPR037214; TROVE_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR14202; PTHR14202; 1.
DR Pfam; PF05731; TROVE; 1.
DR SUPFAM; SSF140864; SSF140864; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50988; TROVE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cilium biogenesis/degradation; Cytoplasm;
KW Direct protein sequencing; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding.
FT CHAIN 1..538
FT /note="RNA-binding protein Ro60"
FT /id="PRO_0000174170"
FT DOMAIN 16..369
FT /note="TROVE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00343"
FT REGION 120..284
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P42700"
FT REGION 361..538
FT /note="VWFA-like domain"
FT /evidence="ECO:0000250|UniProtKB:P42700"
FT BINDING 378
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P42700"
FT BINDING 380
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P42700"
FT BINDING 445
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P42700"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P10155"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10155"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10155"
FT MOD_RES 224
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10155"
FT CONFLICT 32..33
FT /note="RL -> V (in Ref. 2; AAF19049)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="D -> G (in Ref. 2; AAF19049)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="V -> I (in Ref. 2; AAF19049)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 60124 MW; 7850DA35D1726BDA CRC64;
MEGSANQLQP LSETQVVNSE GGCVWQVTDM NRLRRFLCFG SEGGTYYIKE QKLGLENAEA
LIRLIEDGRG CEVIQEIKSF SQEGRTAKQE PLLFALAVCS QCADINTKQA AFKAVPEVCR
IPTHLFTFIQ FKKDLKESMK CGMWGRALRK AVADWYNEKG GMAVALVVTK YKQRNGWSHK
DLLRLSHLKP SSEGLAIVTK YITKGWKEVH EEYKEKALSV EAEKLLKYLE AVEKVKRTKD
DLEVIHLIEE HQLVREHLLT NHLKSKEVWK ALLQEMPLTA LLRNLGKMTA NSVLEPGNSE
VSLICEKLSN EKLLKKARIH PFHVLIALET YRAGHGLRGK LKWIPDKDIL QALDAAFYTT
FKTVEPTGKR FLLAVDVSAS MNQRALGSVL NASTVAAAMC MVVTRTEKES SVVAFACDMV
PFPVTTDMTL QQVLTAMNKV PAGNTDCSLP MIWAQKTDTA ADVFVVFTDN ETFAGQVHPA
VALREYRKKM DIPAKLIVCG MTSNGFTIAD PDDRGMLDMC GFDTAALDVI RNFTLDVI
