RO60_XENLA
ID RO60_XENLA Reviewed; 538 AA.
AC P42700;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=RNA-binding protein RO60 {ECO:0000250|UniProtKB:P10155};
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:0000250|UniProtKB:P10155};
GN Synonyms=trove2 {ECO:0000250|UniProtKB:P10155};
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 [MRNA].
RC TISSUE=Embryo, and Ovary;
RX PubMed=7688474; DOI=10.1073/pnas.90.15.7250;
RA O'Brien C.A., Margelot K., Wolin S.L.;
RT "Xenopus Ro ribonucleoproteins: members of an evolutionarily conserved
RT class of cytoplasmic ribonucleoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7250-7254(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) ALONE AND IN COMPLEX WITH RNA AND
RP MAGNESIUM IONS, FUNCTION, RNA-BINDING REGION, METAL-BINDING SITES, AND
RP DOMAIN.
RX PubMed=15907467; DOI=10.1016/j.cell.2005.03.009;
RA Stein A.J., Fuchs G., Fu C., Wolin S.L., Reinisch K.M.;
RT "Structural insights into RNA quality control: the Ro autoantigen binds
RT misfolded RNAs via its central cavity.";
RL Cell 121:529-539(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH RNA AND MAGNNESIUM
RP IONS, FUNCTION, AND DOMAIN.
RX PubMed=17041599; DOI=10.1038/nsmb1156;
RA Fuchs G., Stein A.J., Fu C., Reinisch K.M., Wolin S.L.;
RT "Structural and biochemical basis for misfolded RNA recognition by the Ro
RT autoantigen.";
RL Nat. Struct. Mol. Biol. 13:1002-1009(2006).
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 (PubMed:15907467, PubMed:17041599). May play roles in cilia
CC formation and/or maintenance (By similarity).
CC {ECO:0000250|UniProtKB:O08848, ECO:0000269|PubMed:15907467,
CC ECO:0000269|PubMed:17041599}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P10155}.
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.
CC -!- DOMAIN: The MIDAS-like motif in the VWFA-like domain binds divalent
CC metal cations. {ECO:0000269|PubMed:15907467,
CC ECO:0000269|PubMed:17041599}.
CC -!- SIMILARITY: Belongs to the Ro 60 kDa family. {ECO:0000305}.
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DR EMBL; L15430; AAC38001.1; -; mRNA.
DR PIR; I51560; I51560.
DR RefSeq; NP_001079344.1; NM_001085875.2.
DR PDB; 1YVP; X-ray; 2.20 A; A/B=1-538.
DR PDB; 1YVR; X-ray; 1.95 A; A=1-538.
DR PDB; 2I91; X-ray; 2.65 A; A/B=1-538.
DR PDBsum; 1YVP; -.
DR PDBsum; 1YVR; -.
DR PDBsum; 2I91; -.
DR AlphaFoldDB; P42700; -.
DR SMR; P42700; -.
DR PRIDE; P42700; -.
DR GeneID; 378688; -.
DR KEGG; xla:378688; -.
DR CTD; 378688; -.
DR Xenbase; XB-GENE-968761; ro60.L.
DR EvolutionaryTrace; P42700; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 378688; Expressed in pancreas and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034336; F:misfolded RNA binding; IDA:MGI.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
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 3D-structure; Cilium biogenesis/degradation; Cytoplasm; Metal-binding;
KW Reference proteome; Ribonucleoprotein; RNA-binding.
FT CHAIN 1..538
FT /note="RNA-binding protein RO60"
FT /id="PRO_0000174171"
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:0000269|PubMed:15907467,
FT ECO:0000269|PubMed:17041599"
FT REGION 361..538
FT /note="VWFA-like domain"
FT /evidence="ECO:0000305"
FT BINDING 378
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:15907467,
FT ECO:0000269|PubMed:17041599"
FT BINDING 380
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:15907467,
FT ECO:0000269|PubMed:17041599"
FT BINDING 445
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:15907467,
FT ECO:0000269|PubMed:17041599"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2I91"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:1YVR"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 50..66
FT /evidence="ECO:0007829|PDB:1YVR"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:2I91"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:1YVR"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1YVP"
FT HELIX 105..118
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:1YVR"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:1YVR"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 220..236
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 266..274
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 278..290
FT /evidence="ECO:0007829|PDB:1YVR"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 299..308
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 311..316
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 321..333
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 347..359
FT /evidence="ECO:0007829|PDB:1YVR"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 379..382
FT /evidence="ECO:0007829|PDB:1YVR"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 392..406
FT /evidence="ECO:0007829|PDB:1YVR"
FT STRAND 408..420
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 430..437
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 449..456
FT /evidence="ECO:0007829|PDB:1YVR"
FT STRAND 462..468
FT /evidence="ECO:0007829|PDB:1YVR"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 479..490
FT /evidence="ECO:0007829|PDB:1YVR"
FT STRAND 495..500
FT /evidence="ECO:0007829|PDB:1YVR"
FT STRAND 502..509
FT /evidence="ECO:0007829|PDB:1YVR"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:1YVR"
FT HELIX 526..534
FT /evidence="ECO:0007829|PDB:1YVR"
SQ SEQUENCE 538 AA; 60688 MW; 548C17B0AE9EBFD6 CRC64;
MEATMDQTQP LNEKQVPNSE GCYVWQVSDM NRLRRFLCFG SEGGTYYIEE KKLGQENAEA
LLRLIEDGKG CEVVQEIKTF SQEGRAAKQE PTLFALAVCS QCSDIKTKQA AFRAVPEVCR
IPTHLFTFIQ FKKDLKEGMK CGMWGRALRK AVSDWYNTKD ALNLAMAVTK YKQRNGWSHK
DLLRLSHIKP ANEGLTMVAK YVSKGWKEVQ EAYKEKELSP ETEKVLKYLE ATERVKRTKD
ELEIIHLIDE YRLVREHLLT IHLKSKEIWK SLLQDMPLTA LLRNLGKMTA DSVLAPASSE
VSSVCERLTN EKLLKKARIH PFHILVALET YKKGHGNRGK LRWIPDTSIV EALDNAFYKS
FKLVEPTGKR FLLAIDVSAS MNQRVLGSIL NASVVAAAMC MLVARTEKDS HMVAFSDEML
PCPITVNMLL HEVVEKMSDI TMGSTDCALP MLWAQKTNTA ADIFIVFTDC ETNVEDVHPA
TALKQYREKM GIPAKLIVCA MTSNGFSIAD PDDRGMLDIC GFDSGALDVI RNFTLDLI
