TYW5_MOUSE
ID TYW5_MOUSE Reviewed; 315 AA.
AC A2RSX7; Q3UT82; Q4KL17;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=tRNA wybutosine-synthesizing protein 5 {ECO:0000305};
DE EC=1.14.11.42 {ECO:0000250|UniProtKB:A2RUC4};
DE AltName: Full=tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-C(2))-hydroxylase;
GN Name=Tyw5;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Egg;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 10-315 (ISOFORM 2).
RC TISSUE=Brain, and Thyroid;
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).
CC -!- FUNCTION: tRNA hydroxylase that acts as a component of the wybutosine
CC biosynthesis pathway. Wybutosine is a hyper modified guanosine with a
CC tricyclic base found at the 3'-position adjacent to the anticodon of
CC eukaryotic phenylalanine tRNA. Catalyzes the hydroxylation of 7-(a-
CC amino-a-carboxypropyl)wyosine (yW-72) into undermodified
CC hydroxywybutosine (OHyW*). OHyW* being further transformed into
CC hydroxywybutosine (OHyW) by LCMT2/TYW4. OHyW is a derivative of
CC wybutosine found in higher eukaryotes. {ECO:0000250|UniProtKB:A2RUC4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 7-[(3S)-3-amino-3-carboxypropyl]wyosine(37)
CC in tRNA(Phe) + O2 = 7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine(37)
CC in tRNA(Phe) + CO2 + succinate; Xref=Rhea:RHEA:37899, Rhea:RHEA-
CC COMP:10379, Rhea:RHEA-COMP:11848, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:73543, ChEBI:CHEBI:73603; EC=1.14.11.42;
CC Evidence={ECO:0000250|UniProtKB:A2RUC4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37900;
CC Evidence={ECO:0000250|UniProtKB:A2RUC4};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:A2RUC4};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:A2RUC4};
CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC {ECO:0000250|UniProtKB:A2RUC4}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A2RUC4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2RSX7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2RSX7-2; Sequence=VSP_029107, VSP_029108;
CC -!- SIMILARITY: Belongs to the TYW5 family. {ECO:0000305}.
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DR EMBL; AK139666; BAE24098.1; -; mRNA.
DR EMBL; BC099495; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC132289; AAI32290.1; -; mRNA.
DR CCDS; CCDS14966.2; -. [A2RSX7-1]
DR RefSeq; NP_001032831.2; NM_001037742.2. [A2RSX7-1]
DR AlphaFoldDB; A2RSX7; -.
DR SMR; A2RSX7; -.
DR STRING; 10090.ENSMUSP00000125427; -.
DR PhosphoSitePlus; A2RSX7; -.
DR EPD; A2RSX7; -.
DR MaxQB; A2RSX7; -.
DR PaxDb; A2RSX7; -.
DR PeptideAtlas; A2RSX7; -.
DR PRIDE; A2RSX7; -.
DR ProteomicsDB; 298159; -. [A2RSX7-1]
DR ProteomicsDB; 298160; -. [A2RSX7-2]
DR Antibodypedia; 34079; 91 antibodies from 19 providers.
DR Ensembl; ENSMUST00000079998; ENSMUSP00000078912; ENSMUSG00000048495. [A2RSX7-2]
DR Ensembl; ENSMUST00000162686; ENSMUSP00000125427; ENSMUSG00000048495. [A2RSX7-1]
DR GeneID; 68736; -.
DR KEGG; mmu:68736; -.
DR UCSC; uc007baz.2; mouse. [A2RSX7-1]
DR UCSC; uc007bbb.2; mouse. [A2RSX7-2]
DR CTD; 129450; -.
DR MGI; MGI:1915986; Tyw5.
DR VEuPathDB; HostDB:ENSMUSG00000048495; -.
DR eggNOG; KOG2132; Eukaryota.
DR GeneTree; ENSGT00940000158493; -.
DR HOGENOM; CLU_016785_4_0_1; -.
DR InParanoid; A2RSX7; -.
DR OMA; PLYDDRP; -.
DR OrthoDB; 1385616at2759; -.
DR PhylomeDB; A2RSX7; -.
DR TreeFam; TF332364; -.
DR UniPathway; UPA00375; -.
DR BioGRID-ORCS; 68736; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Tyw5; mouse.
DR PRO; PR:A2RSX7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; A2RSX7; protein.
DR Bgee; ENSMUSG00000048495; Expressed in spermatocyte and 238 other tissues.
DR ExpressionAtlas; A2RSX7; baseline and differential.
DR Genevisible; A2RSX7; MM.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0102524; F:tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0031591; P:wybutosine biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR029612; TYW5.
DR PANTHER; PTHR12461:SF50; PTHR12461:SF50; 1.
DR Pfam; PF13621; Cupin_8; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; tRNA processing.
FT CHAIN 1..315
FT /note="tRNA wybutosine-synthesizing protein 5"
FT /id="PRO_0000309275"
FT DOMAIN 102..267
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 106
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 166
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT VAR_SEQ 72..121
FT /note="SKNFVYRTLPFNKLVQRAAEETHKEFFISEDEKYYLRSLGEDPRKDVADI
FT -> KLYLLTSWSREQPKKHIKNSSFQRMRNTTYGHLEKTQGRMLQTSDSSSHH (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029107"
FT VAR_SEQ 122..315
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029108"
FT CONFLICT 5
FT /note="R -> H (in Ref. 2; AAI32290)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 36633 MW; 26B51EF4662C55A3 CRC64;
MAEQRLPVPR LRGVSREQFM EHLYPQRKPL VLEGLDLGSC TSKWTVDYLS QVGGTKEVKI
HVAAVPQMDF ISKNFVYRTL PFNKLVQRAA EETHKEFFIS EDEKYYLRSL GEDPRKDVAD
IRQQFPSLGG DITFPMFFRE EQFFSSVFRI SSPGLQLWTH YDVMDNFLIQ VTGKKRITLF
NPRDAQYLYL SGSKSEVLNI DSPDLDKYPL FPKARRYECS LEAGDVLFIP ALWFHNVVSE
EFGVGVNIFW KHLPSECYDT TDTYGNKDPV AASRAVQILD RALKTLAELP EEYRDFYARQ
MVLRIQDKAY SKNFE
