PUS7_MOUSE
ID PUS7_MOUSE Reviewed; 660 AA.
AC Q91VU7; B7ZNL8; F7AC41; Q3TUC7; Q3UQN6; Q69Z76;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Pseudouridylate synthase 7 homolog {ECO:0000305};
DE EC=5.4.99.- {ECO:0000250|UniProtKB:Q96PZ0};
GN Name=Pus7 {ECO:0000312|MGI:MGI:1925947};
GN Synonyms=Kiaa1897 {ECO:0000303|PubMed:15368895};
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 1).
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Heart;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain;
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: Pseudouridylate synthase that catalyzes pseudouridylation of
CC RNAs. Acts as a regulator of protein synthesis in embryonic stem cells
CC by mediating pseudouridylation of RNA fragments derived from tRNAs
CC (tRFs): pseudouridylated tRFs inhibit translation by targeting the
CC translation initiation complex. Also catalyzes pseudouridylation of
CC mRNAs: mediates pseudouridylation of mRNAs with the consensus sequence
CC 5'-UGUAG-3'. Acts as a regulator of pre-mRNA splicing by mediating
CC pseudouridylation of pre-mRNAs at locations associated with
CC alternatively spliced regions. Pseudouridylation of pre-mRNAs near
CC splice sites directly regulates mRNA splicing and mRNA 3'-end
CC processing. In addition to mRNAs and tRNAs, binds other types of RNAs,
CC such as snRNAs, Y RNAs and vault RNAs, suggesting that it can catalyze
CC pseudouridylation of many RNA types. {ECO:0000250|UniProtKB:Q96PZ0}.
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:Q96PZ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(13) in tRNA = pseudouridine(13) in tRNA;
CC Xref=Rhea:RHEA:42540, Rhea:RHEA-COMP:10105, Rhea:RHEA-COMP:10106,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:Q96PZ0};
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:Q96PZ0};
CC -!- SUBUNIT: Interacts with SIRT1. {ECO:0000250|UniProtKB:Q96PZ0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96PZ0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91VU7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91VU7-2; Sequence=VSP_059623;
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruD family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32568.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE25003.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK173290; BAD32568.1; ALT_INIT; mRNA.
DR EMBL; AK142271; BAE25003.1; ALT_INIT; mRNA.
DR EMBL; AK160849; BAE36044.1; -; mRNA.
DR EMBL; AC117614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008544; AAH08544.2; -; mRNA.
DR EMBL; BC138533; AAI38534.1; -; mRNA.
DR EMBL; BC145316; AAI45317.1; -; mRNA.
DR CCDS; CCDS51431.1; -. [Q91VU7-1]
DR CCDS; CCDS80219.1; -. [Q91VU7-2]
DR RefSeq; NP_001276709.1; NM_001289780.1. [Q91VU7-2]
DR RefSeq; NP_001276710.1; NM_001289781.1. [Q91VU7-1]
DR RefSeq; NP_848490.2; NM_178403.5. [Q91VU7-1]
DR AlphaFoldDB; Q91VU7; -.
DR SMR; Q91VU7; -.
DR STRING; 10090.ENSMUSP00000113801; -.
DR iPTMnet; Q91VU7; -.
DR PhosphoSitePlus; Q91VU7; -.
DR EPD; Q91VU7; -.
DR MaxQB; Q91VU7; -.
DR PaxDb; Q91VU7; -.
DR PRIDE; Q91VU7; -.
DR ProteomicsDB; 340938; -. [Q91VU7-1]
DR ProteomicsDB; 342885; -.
DR Antibodypedia; 17076; 133 antibodies from 17 providers.
DR DNASU; 78697; -.
DR Ensembl; ENSMUST00000119946; ENSMUSP00000113801; ENSMUSG00000057541. [Q91VU7-1]
DR Ensembl; ENSMUST00000131992; ENSMUSP00000123129; ENSMUSG00000057541. [Q91VU7-1]
DR Ensembl; ENSMUST00000148618; ENSMUSP00000114588; ENSMUSG00000057541. [Q91VU7-2]
DR GeneID; 78697; -.
DR KEGG; mmu:78697; -.
DR UCSC; uc008wqo.2; mouse. [Q91VU7-1]
DR UCSC; uc012dsw.2; mouse.
DR CTD; 54517; -.
DR MGI; MGI:1925947; Pus7.
DR VEuPathDB; HostDB:ENSMUSG00000057541; -.
DR eggNOG; KOG2339; Eukaryota.
DR GeneTree; ENSGT00530000063554; -.
DR HOGENOM; CLU_005281_0_1_1; -.
DR InParanoid; Q91VU7; -.
DR OMA; ERGYFNY; -.
DR OrthoDB; 955294at2759; -.
DR PhylomeDB; Q91VU7; -.
DR TreeFam; TF314278; -.
DR BioGRID-ORCS; 78697; 15 hits in 73 CRISPR screens.
DR ChiTaRS; Pus7; mouse.
DR PRO; PR:Q91VU7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR Bgee; ENSMUSG00000057541; Expressed in ureteric bud tip and 246 other tissues.
DR ExpressionAtlas; Q91VU7; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0001522; P:pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; ISS:UniProtKB.
DR GO; GO:2000380; P:regulation of mesoderm development; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; ISS:UniProtKB.
DR Gene3D; 3.30.2350.20; -; 2.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001656; PsdUridine_synth_TruD.
DR InterPro; IPR020119; PsdUridine_synth_TruD_CS.
DR InterPro; IPR011760; PsdUridine_synth_TruD_insert.
DR InterPro; IPR042214; TruD_catalytic.
DR PANTHER; PTHR13326; PTHR13326; 1.
DR Pfam; PF01142; TruD; 1.
DR PIRSF; PIRSF037016; Pseudouridin_synth_euk_prd; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00094; tRNA_TruD_broad; 1.
DR PROSITE; PS50984; TRUD; 1.
DR PROSITE; PS01268; UPF0024; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Isomerase; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; tRNA processing.
FT CHAIN 1..660
FT /note="Pseudouridylate synthase 7 homolog"
FT /id="PRO_0000444609"
FT DOMAIN 369..579
FT /note="TRUD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00342"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 293
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96PZ0"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PZ0"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PZ0"
FT VAR_SEQ 243
FT /note="N -> KVRAAAD (in isoform 2)"
FT /id="VSP_059623"
SQ SEQUENCE 660 AA; 74793 MW; 4D5DA7CC63142E86 CRC64;
MEMTSTSLKR GCLVVEDNDS VTPHDETKKQ KVSEGCLTSS QDGVENDGLH RSENEPGPPE
AESTVKDDEN SSAQVQEEEE EEEEEDGLSE AGEEEEAESF ADMMKHGLTE LDVGICKFVS
SHHGFSGILK ERYSDFVVHE IGKDGRISHL DDLSVPVDEE DPPEDALTVL TAEDRQQLEE
LQLFKNKETS VAIEVIEDTK EKRTVIHQAI KSLFPGLETK TEDREGRKYI VAYHAAGKKA
LANPRKHSWP KSRGSYCHFV LYKENKDTMD AINVLSKYLR VKPNIFSYMG TKDKRAITVQ
EIAVLKISAQ RLAHLNKCLM NLKLGNFSYQ KTPLKLGALQ GNHFTVVLRN ITGTDEQVQQ
AMQSLRETGF INYYGMQRFG TTAVPTYQVG RAILQNSWTE VMDLILKPRS GAEKGYLVKC
REEWAKTKDP ASALKKLPVK RCVEGQLLRG LSRYGMKNIV SAFGIIPRNN RLMYIHSYQS
YVWNTMVSRR IEEYGLRPVP GDLVLKGATP TYIEEDDVDN YSIHDVVMPL PGFDVIYPKH
KISEAYREML AADNLDIDNM RHTIRDYSLS GAYRRIIIRP QSVSWEVVAY DDPKIPLFNT
DVDNLEGKPP PVFASEGKYR ALKMDFSLPP STYATMAIRE VLKMDTSIKN QTQLNTSWLR
