PUS1_MOUSE
ID PUS1_MOUSE Reviewed; 423 AA.
AC Q9WU56; Q3UUC6; Q791J1; Q8C250; Q8VDQ3; Q9EQD1; Q9JJE5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Pseudouridylate synthase 1 homolog {ECO:0000305};
DE EC=5.4.99.- {ECO:0000269|PubMed:10094309, ECO:0000269|PubMed:15327771};
DE AltName: Full=tRNA pseudouridine synthase 1 {ECO:0000305};
DE EC=5.4.99.12 {ECO:0000269|PubMed:10094309};
DE AltName: Full=tRNA pseudouridine(38-40) synthase;
DE AltName: Full=tRNA pseudouridylate synthase I;
DE AltName: Full=tRNA-uridine isomerase I;
DE Flags: Precursor;
GN Name=Pus1 {ECO:0000303|PubMed:10094309, ECO:0000312|MGI:MGI:1929237};
GN ORFNames=MNCb-0873;
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] (ISOFORM 2), FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10094309; DOI=10.1017/s1355838299981591;
RA Chen J., Patton J.R.;
RT "Cloning and characterization of a mammalian pseudouridine synthase.";
RL RNA 5:409-419(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2 AND 3), FUNCTION, AND
RP ALTERNATIVE SPLICING (ISOFORM 4).
RC STRAIN=129/SvJ;
RX PubMed=11085940; DOI=10.1042/bj3520465;
RA Chen J., Patton J.R.;
RT "Mouse pseudouridine synthase 1: gene structure and alternative splicing of
RT pre-mRNA.";
RL Biochem. J. 352:465-473(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Spinal cord;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION IN A COMPLEX WITH RARG AND
RP SRA1.
RX PubMed=15327771; DOI=10.1016/j.molcel.2004.06.044;
RA Zhao X., Patton J.R., Davis S.L., Florence B., Ames S.J., Spanjaard R.A.;
RT "Regulation of nuclear receptor activity by a pseudouridine synthase
RT through posttranscriptional modification of steroid receptor RNA
RT activator.";
RL Mol. Cell 15:549-558(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416 AND THR-422, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27197761; DOI=10.1038/srep26202;
RA Mangum J.E., Hardee J.P., Fix D.K., Puppa M.J., Elkes J., Altomare D.,
RA Bykhovskaya Y., Campagna D.R., Schmidt P.J., Sendamarai A.K., Lidov H.G.,
RA Barlow S.C., Fischel-Ghodsian N., Fleming M.D., Carson J.A., Patton J.R.;
RT "Pseudouridine synthase 1 deficient mice, a model for Mitochondrial
RT Myopathy with Sideroblastic Anemia, exhibit muscle morphology and
RT physiology alterations.";
RL Sci. Rep. 6:26202-26202(2016).
CC -!- FUNCTION: Pseudouridylate synthase that catalyzes pseudouridylation of
CC tRNAs and mRNAs (PubMed:10094309, PubMed:15327771, PubMed:27197761).
CC Acts on positions 27/28 in the anticodon stem and also positions 34 and
CC 36 in the anticodon of an intron containing tRNA (PubMed:10094309).
CC Also catalyzes pseudouridylation of mRNAs: mediates pseudouridylation
CC of mRNAs with the consensus sequence 5'-UGUAG-3' (By similarity). Acts
CC as a regulator of pre-mRNA splicing by mediating pseudouridylation of
CC pre-mRNAs at locations associated with alternatively spliced regions
CC (By similarity). Pseudouridylation of pre-mRNAs near splice sites
CC directly regulates mRNA splicing and mRNA 3'-end processing (By
CC similarity). Involved in regulation of nuclear receptor activity
CC through pseudouridylation of SRA1 mRNA (PubMed:15327771).
CC {ECO:0000250|UniProtKB:Q9Y606, ECO:0000269|PubMed:10094309,
CC ECO:0000269|PubMed:15327771, ECO:0000269|PubMed:27197761}.
CC -!- FUNCTION: [Isoform 3]: Does not form pseudouridine when expressed in
CC vitro. {ECO:0000269|PubMed:11085940}.
CC -!- FUNCTION: [Isoform 4]: Does not form pseudouridine when expressed in
CC vitro. {ECO:0000269|PubMed:11085940}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in tRNA = a pseudouridine in tRNA;
CC Xref=Rhea:RHEA:54572, Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13934,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000269|PubMed:10094309, ECO:0000269|PubMed:15327771,
CC ECO:0000269|PubMed:27197761};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA;
CC Xref=Rhea:RHEA:22376, Rhea:RHEA-COMP:10085, Rhea:RHEA-COMP:10087,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.12;
CC Evidence={ECO:0000269|PubMed:10094309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in mRNA = a pseudouridine in mRNA;
CC Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:Q9Y606};
CC -!- SUBUNIT: Monomer (By similarity). Forms a complex with RARG and the
CC SRA1 RNA in the nucleus (PubMed:15327771).
CC {ECO:0000250|UniProtKB:Q9Y606, ECO:0000269|PubMed:15327771}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y606}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y606}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9Y606}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9WU56-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WU56-2; Sequence=VSP_020114;
CC Name=3;
CC IsoId=Q9WU56-3; Sequence=VSP_020114, VSP_021792;
CC Name=4;
CC IsoId=Q9WU56-4; Sequence=VSP_020114, VSP_021791;
CC -!- DISRUPTION PHENOTYPE: Impaired muscle morphology and physiology leading
CC to impaired exercise capacity (PubMed:27197761). Mice were born at the
CC expected Mendelian frequency (PubMed:27197761). At 14 weeks, mice
CC display reduced exercise capacity, probably caused by alterations in
CC muscle metabolism related to mitochondrial content and oxidative
CC capacity (PubMed:27197761). Cells show reduced pseudouridylation of
CC cytoplasmic and mitochondrial tRNAs (PubMed:27197761).
CC {ECO:0000269|PubMed:27197761}.
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95047.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC40817.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF116237; AAD21041.1; -; mRNA.
DR EMBL; AF269250; AAG35307.1; -; Genomic_DNA.
DR EMBL; AF269250; AAG35308.1; -; Genomic_DNA.
DR EMBL; AB041563; BAA95047.1; ALT_FRAME; mRNA.
DR EMBL; AK089258; BAC40817.1; ALT_INIT; mRNA.
DR EMBL; AK138570; BAE23701.1; -; mRNA.
DR EMBL; BC021446; AAH21446.2; -; mRNA.
DR EMBL; BC034359; AAH34359.2; -; mRNA.
DR CCDS; CCDS19531.1; -. [Q9WU56-1]
DR CCDS; CCDS39212.1; -. [Q9WU56-2]
DR CCDS; CCDS84929.1; -. [Q9WU56-4]
DR RefSeq; NP_001020733.1; NM_001025562.2. [Q9WU56-2]
DR RefSeq; NP_001334319.1; NM_001347390.1. [Q9WU56-4]
DR RefSeq; NP_062674.2; NM_019700.4. [Q9WU56-1]
DR RefSeq; XP_011247847.1; XM_011249545.2.
DR RefSeq; XP_017176503.1; XM_017321014.1. [Q9WU56-2]
DR RefSeq; XP_017176504.1; XM_017321015.1. [Q9WU56-2]
DR AlphaFoldDB; Q9WU56; -.
DR SMR; Q9WU56; -.
DR BioGRID; 207924; 9.
DR STRING; 10090.ENSMUSP00000083844; -.
DR iPTMnet; Q9WU56; -.
DR PhosphoSitePlus; Q9WU56; -.
DR EPD; Q9WU56; -.
DR MaxQB; Q9WU56; -.
DR PaxDb; Q9WU56; -.
DR PeptideAtlas; Q9WU56; -.
DR PRIDE; Q9WU56; -.
DR ProteomicsDB; 300133; -. [Q9WU56-1]
DR ProteomicsDB; 300134; -. [Q9WU56-2]
DR ProteomicsDB; 300135; -. [Q9WU56-3]
DR ProteomicsDB; 300136; -. [Q9WU56-4]
DR Antibodypedia; 32008; 166 antibodies from 28 providers.
DR DNASU; 56361; -.
DR Ensembl; ENSMUST00000031481; ENSMUSP00000031481; ENSMUSG00000029507. [Q9WU56-2]
DR Ensembl; ENSMUST00000031483; ENSMUSP00000031483; ENSMUSG00000029507. [Q9WU56-1]
DR Ensembl; ENSMUST00000112426; ENSMUSP00000108045; ENSMUSG00000029507. [Q9WU56-4]
DR Ensembl; ENSMUST00000170468; ENSMUSP00000130814; ENSMUSG00000029507. [Q9WU56-2]
DR GeneID; 56361; -.
DR KEGG; mmu:56361; -.
DR UCSC; uc008yrm.1; mouse. [Q9WU56-4]
DR UCSC; uc008yrn.1; mouse. [Q9WU56-1]
DR CTD; 80324; -.
DR MGI; MGI:1929237; Pus1.
DR VEuPathDB; HostDB:ENSMUSG00000029507; -.
DR eggNOG; KOG2553; Eukaryota.
DR GeneTree; ENSGT00950000183160; -.
DR HOGENOM; CLU_021971_3_0_1; -.
DR InParanoid; Q9WU56; -.
DR PhylomeDB; Q9WU56; -.
DR BRENDA; 4.2.1.70; 3474.
DR BRENDA; 5.4.99.B22; 3474.
DR BioGRID-ORCS; 56361; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Pus1; mouse.
DR PRO; PR:Q9WU56; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9WU56; protein.
DR Bgee; ENSMUSG00000029507; Expressed in ectoplacental cone and 217 other tissues.
DR ExpressionAtlas; Q9WU56; baseline and differential.
DR Genevisible; Q9WU56; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:MGI.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:MGI.
DR GO; GO:0002153; F:steroid receptor RNA activator RNA binding; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IDA:UniProtKB.
DR CDD; cd02568; PseudoU_synth_PUS1_PUS2; 1.
DR Gene3D; 3.30.70.580; -; 1.
DR Gene3D; 3.30.70.660; -; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001406; PsdUridine_synth_TruA.
DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR InterPro; IPR041708; PUS1/PUS2-like.
DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR PANTHER; PTHR11142; PTHR11142; 1.
DR Pfam; PF01416; PseudoU_synth_1; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00071; hisT_truA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Isomerase; Mitochondrion; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome;
KW Transit peptide; tRNA processing.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..423
FT /note="Pseudouridylate synthase 1 homolog"
FT /id="PRO_0000057518"
FT REGION 32..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9Y606"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y606"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 422
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10094309,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT /id="VSP_020114"
FT VAR_SEQ 98..143
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021791"
FT VAR_SEQ 143
FT /note="K -> KPLRTSACFCLYTGFLFHW (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_021792"
FT CONFLICT 48
FT /note="K -> E (in Ref. 4; BAC40817)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="G -> D (in Ref. 4; BAC40817)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="G -> V (in Ref. 5; AAH21446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 47502 MW; C71FDBF60F29295A CRC64;
MGFPRLWAAL LRNWGRWTAR PGPRVPGLPP MAGNKVPPAL ASHQPDRKGR GGWVWEETEH
PAKRVKGGED EEPPRKLPKR KIVLLMAYSG KGYHGMQRNL GSSQFRTIED DLVSALVQAG
CIPENHGTDM RKMSFQRCAR TDKGVSAAGQ VVSLKVWLID DILDKINSHL PSHIRILGLK
RVTGGFNSKN KCDARTYCYM LPTFAFAHKD RDVQDESYRL SAETLQQVNR LLACYKGTHN
FHNFTSQKGP REPSARRYIL EMYCEEPFVR EGLEFAVIKV KGQSFMMHQI RKMVGLVVAI
VKGYAPESVL ERSWGEEKVD VPKAPGLGLV LERVHFEKYN QRFGGDGLHE PLDWTQEEGK
VTAFKEQYIY PTIVSTERDE RSMAQWLNTL PIHNFSGTAL GAADTGAKVP SSLEGSEGDG
DTD
