PUS1_RAT
ID PUS1_RAT Reviewed; 423 AA.
AC Q4KM92;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Pseudouridylate synthase 1 homolog {ECO:0000305};
DE EC=5.4.99.- {ECO:0000250|UniProtKB:Q9Y606};
DE AltName: Full=tRNA pseudouridine synthase 1 {ECO:0000305};
DE EC=5.4.99.12 {ECO:0000250|UniProtKB:Q9Y606};
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:0000312|RGD:1311871};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416 AND THR-422, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Pseudouridylate synthase that catalyzes pseudouridylation of
CC tRNAs and mRNAs. Acts on positions 27/28 in the anticodon stem and also
CC positions 34 and 36 in the anticodon of an intron containing tRNA. Also
CC catalyzes pseudouridylation of mRNAs: mediates pseudouridylation of
CC mRNAs with the consensus sequence 5'-UGUAG-3'. Acts as a regulator of
CC pre-mRNA splicing by mediating pseudouridylation of pre-mRNAs at
CC locations associated with alternatively spliced regions.
CC Pseudouridylation of pre-mRNAs near splice sites directly regulates
CC mRNA splicing and mRNA 3'-end processing. Involved in regulation of
CC nuclear receptor activity through pseudouridylation of SRA1 mRNA.
CC {ECO:0000250|UniProtKB:Q9Y606}.
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:0000250|UniProtKB:Q9Y606};
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:0000250|UniProtKB:Q9Y606};
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 (By similarity). {ECO:0000250|UniProtKB:Q9WU56,
CC ECO:0000250|UniProtKB:Q9Y606}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y606}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y606}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9Y606}.
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000305}.
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DR EMBL; AC095390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001020734.1; NM_001025563.1.
DR AlphaFoldDB; Q4KM92; -.
DR SMR; Q4KM92; -.
DR STRING; 10116.ENSRNOP00000053623; -.
DR iPTMnet; Q4KM92; -.
DR PhosphoSitePlus; Q4KM92; -.
DR jPOST; Q4KM92; -.
DR PaxDb; Q4KM92; -.
DR Ensembl; ENSRNOT00000056780; ENSRNOP00000053623; ENSRNOG00000037500.
DR GeneID; 304567; -.
DR KEGG; rno:304567; -.
DR UCSC; RGD:1311871; rat.
DR CTD; 80324; -.
DR RGD; 1311871; Pus1.
DR eggNOG; KOG2553; Eukaryota.
DR GeneTree; ENSGT00950000183160; -.
DR HOGENOM; CLU_021971_3_0_1; -.
DR InParanoid; Q4KM92; -.
DR OMA; AVMIGYC; -.
DR OrthoDB; 710785at2759; -.
DR PhylomeDB; Q4KM92; -.
DR PRO; PR:Q4KM92; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000037500; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; Q4KM92; baseline and differential.
DR Genevisible; Q4KM92; RN.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:RGD.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISS:UniProtKB.
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; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; ISO:RGD.
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 Cytoplasm; Isomerase; Mitochondrion; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Transit peptide;
KW tRNA processing.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..423
FT /note="Pseudouridylate synthase 1 homolog"
FT /id="PRO_0000248245"
FT REGION 32..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..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:22673903"
FT MOD_RES 422
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 423 AA; 47515 MW; BCF4780D9D439520 CRC64;
MGFPRLWAAL LRAWGRWTAR PGPRVPGLPP MAGNKVPPAL PSHQPDRKGR GGWVWEETEH
PAKRVKGGED EEPPRKLPKR KIVLLMAYSG KGYHGMQRNL GSSQFRTIED DLVSALVQAG
CIPENHGTDM RKMSFQRCAR TDKGVSAAGQ VVSLKVWLID DILDKINSHL PSHIRILGLK
RVTGGFNSKN KCDARTYCYM LPTFAFAHKD RDVQDESYRL SAETLQQVNR LLGCYKGTHN
FHNFTSQKGP REPSARRYIL EMYCEEPFVR EGLEFAVIKV KGQSFMMHQI RKMVGLVVAI
VKGYAPESVL ERSWGEEKVD VPKAPGLGLV LERVHFEKYN QRFGSDGLHE PLDWAQEEGK
VTAFKEQYIY PTIVSTERDE RSMAQWLNTL PIHNFSGTAL GADDTGAKVP SSLEGSEGDG
DTD
