PUS10_MOUSE
ID PUS10_MOUSE Reviewed; 527 AA.
AC Q9D3U0; Q3UM90; Q8BSZ4; Q8CDM2; Q9CSI7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=tRNA pseudouridine synthase Pus10;
DE EC=5.4.99.25 {ECO:0000250|UniProtKB:Q3MIT2};
DE AltName: Full=Coiled-coil domain-containing protein 139 {ECO:0000250|UniProtKB:Q3MIT2};
DE AltName: Full=tRNA pseudouridine 55 synthase;
DE Short=Psi55 synthase;
DE AltName: Full=tRNA pseudouridylate synthase;
DE AltName: Full=tRNA-uridine isomerase;
GN Name=Pus10 {ECO:0000312|MGI:MGI:1921717};
GN Synonyms=Ccdc139 {ECO:0000250|UniProtKB:Q3MIT2};
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].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Extraembryonic tissue, Mammary gland, Placenta, Testis, and Thymus;
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 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Protein with different functions depending on its subcellular
CC location: involved in miRNA processing in the nucleus and acts as a
CC tRNA pseudouridylate synthase in the cytoplasm. In the cytoplasm, acts
CC as a pseudouridylate synthase by catalyzing synthesis of
CC pseudouridine(54) and pseudouridine(55) from uracil-54 and uracil-55,
CC respectively, in the psi GC loop of a subset of tRNAs. tRNA
CC pseudouridylate synthase activity is enhanced by the presence of 1-
CC methyladenosine at position 53-61 of tRNAs. Does not show tRNA
CC pseudouridylate synthase activity in the nucleus. In the nucleus,
CC promotes primary microRNAs (pri-miRNAs) processing independently of its
CC RNA pseudouridylate synthase activity. Binds pri-miRNAs. Modulator of
CC TRAIL/TNFSF10-induced cell death via activation of procaspase-8 and BID
CC cleavage. Required for the progression of the apoptotic signal through
CC intrinsic mitochondrial cell death. {ECO:0000250|UniProtKB:Q3MIT2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA;
CC Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25;
CC Evidence={ECO:0000250|UniProtKB:Q3MIT2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42533;
CC Evidence={ECO:0000250|UniProtKB:Q3MIT2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(54) in tRNA = pseudouridine(54) in tRNA;
CC Xref=Rhea:RHEA:57876, Rhea:RHEA-COMP:10193, Rhea:RHEA-COMP:14141,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:Q3MIT2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57877;
CC Evidence={ECO:0000250|UniProtKB:Q3MIT2};
CC -!- SUBUNIT: Interacts with components of the microprocessor complex DROSHA
CC and DGCR8. {ECO:0000250|UniProtKB:Q3MIT2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3MIT2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q3MIT2}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q3MIT2}. Note=Localizes mainly in the nucleus.
CC tRNA pseudouridylate synthase activity is restricted to the cytoplasm.
CC Translocates from nucleus to mitochondria during TRAIL-induced
CC apoptosis. {ECO:0000250|UniProtKB:Q3MIT2}.
CC -!- PTM: Proteolytically cleaved during TRAIL-induced cell death. Cleaved,
CC in vitro, either by caspase-3 (CASP3) or caspase-8 (CASP8).
CC {ECO:0000250|UniProtKB:Q3MIT2}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase Pus10 family.
CC {ECO:0000305}.
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DR EMBL; AK017063; BAB30576.1; -; mRNA.
DR EMBL; AK012737; BAB28439.1; -; mRNA.
DR EMBL; AK028368; BAC25908.1; -; mRNA.
DR EMBL; AK029866; BAC26650.1; -; mRNA.
DR EMBL; AK088562; BAC40426.1; -; mRNA.
DR EMBL; AK145055; BAE26208.1; -; mRNA.
DR EMBL; AL672049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL805916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX255874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025555; AAH25555.1; -; mRNA.
DR CCDS; CCDS24479.1; -.
DR RefSeq; NP_001028826.1; NM_001033654.2.
DR RefSeq; NP_082580.1; NM_028304.2.
DR RefSeq; NP_083232.1; NM_028956.4.
DR AlphaFoldDB; Q9D3U0; -.
DR SMR; Q9D3U0; -.
DR STRING; 10090.ENSMUSP00000050395; -.
DR iPTMnet; Q9D3U0; -.
DR PhosphoSitePlus; Q9D3U0; -.
DR EPD; Q9D3U0; -.
DR jPOST; Q9D3U0; -.
DR MaxQB; Q9D3U0; -.
DR PaxDb; Q9D3U0; -.
DR PeptideAtlas; Q9D3U0; -.
DR PRIDE; Q9D3U0; -.
DR ProteomicsDB; 302035; -.
DR Antibodypedia; 47429; 114 antibodies from 16 providers.
DR Ensembl; ENSMUST00000020520; ENSMUSP00000020520; ENSMUSG00000020280.
DR Ensembl; ENSMUST00000058163; ENSMUSP00000050395; ENSMUSG00000020280.
DR Ensembl; ENSMUST00000109525; ENSMUSP00000105151; ENSMUSG00000020280.
DR GeneID; 74467; -.
DR KEGG; mmu:74467; -.
DR UCSC; uc007ifk.1; mouse.
DR CTD; 150962; -.
DR MGI; MGI:1921717; Pus10.
DR VEuPathDB; HostDB:ENSMUSG00000020280; -.
DR eggNOG; KOG2364; Eukaryota.
DR GeneTree; ENSGT00390000007529; -.
DR HOGENOM; CLU_028780_2_0_1; -.
DR InParanoid; Q9D3U0; -.
DR OMA; INIDVRH; -.
DR OrthoDB; 1067006at2759; -.
DR PhylomeDB; Q9D3U0; -.
DR TreeFam; TF106109; -.
DR BioGRID-ORCS; 74467; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Pus10; mouse.
DR PRO; PR:Q9D3U0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D3U0; protein.
DR Bgee; ENSMUSG00000020280; Expressed in spermatocyte and 239 other tissues.
DR ExpressionAtlas; Q9D3U0; baseline and differential.
DR Genevisible; Q9D3U0; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070878; F:primary miRNA binding; ISS:UniProtKB.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISS:UniProtKB.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; ISS:UniProtKB.
DR GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; ISS:UniProtKB.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR039894; Pus10-like.
DR PANTHER; PTHR21568; PTHR21568; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Isomerase; Metal-binding; Mitochondrion; Nucleus;
KW Phosphoprotein; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..527
FT /note="tRNA pseudouridine synthase Pus10"
FT /id="PRO_0000299023"
FT REGION 302..315
FT /note="RNA binding forefinger loop"
FT /evidence="ECO:0000255"
FT REGION 440..455
FT /note="RNA binding thumb loop"
FT /evidence="ECO:0000255"
FT COILED 42..87
FT /evidence="ECO:0000255"
FT ACT_SITE 342
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3MIT2"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3MIT2"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3MIT2"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3MIT2"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3MIT2"
FT CONFLICT 7
FT /note="E -> G (in Ref. 1; BAE26208)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="H -> R (in Ref. 1; BAE26208)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="L -> F (in Ref. 1; BAE26208)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="P -> S (in Ref. 1; BAB28439)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="A -> G (in Ref. 1; BAC26650)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="D -> G (in Ref. 1; BAB28439)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="N -> H (in Ref. 1; BAC26650)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="S -> L (in Ref. 1; BAB28439)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="A -> G (in Ref. 1; BAC26650)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="R -> K (in Ref. 1; BAE26208)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="F -> L (in Ref. 1; BAC25908)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="P -> T (in Ref. 1; BAC25908)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 59710 MW; BCD8EEF0BF8658DA CRC64;
MLPLTEENKH VAQLLFSSGT CPRCILRFCG VDLPAPYKHP SKELLNELQK FLEPEKPELI
LEAPNPPLKK IRLHEDGIDN LSEDGKEGVS VTEDESMAEK PSKLRVCNVC LGILQEFCEK
GFITKVCQKV EASGFEFTSV VLSVSFPPQL SVREHAAWLL VKQEMGKQSL SLGRNDVVQL
KEAYKWITHP LFSEELGVPT DGKSLFEVSV VFAHPETAED CHFLGEVCRD CFKPAKNKQS
VFTRMAVLKA LSKIKEEDFL GQFPCPPNSP KTVCTVLEVE CTHGAVFVAG RYNKYSRNLP
QTPWIIDGER KMESSVEELI SDHLLAVFRA ESFNFSSSGR EDVDVRTLGN GRPFAVELLN
PHRVHFTSQE MKELQQTINK SSDKIQVRDL QLVTREAIGH MKEGEEEKTK TYSALIWTNR
AIQKKDIGFL DDLKDLKIDQ KTPLRVLHRR PLAVRTRAIH SMKTHYLDEH HFRLHLKTQA
GTYIKEFVHG DFGRTKPNLG SLMNVTADIL ELDVESVDVD WPPALDD
