Entry sw: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   02-NOV-2016, entry version 101.
DE   RecName: Full=Putative tRNA pseudouridine synthase Pus10;
DE            EC=5.4.99.-;
DE   AltName: Full=Coiled-coil domain-containing protein 139;
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; Synonyms=Ccdc139;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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
RC   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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Pseudouridylate synthases catalyze pseudouridination of
CC       structural RNAs, including transfer, ribosomal, and splicing RNAs.
CC       PUS10 catalyzes the formation of the universal psi55 in the GC
CC       loop of transfer RNAs (Probable). Modulator of TRAIL-induced cell
CC       death via activation of procaspase 8 and BID cleavage. Required
CC       for the progression of the apoptotic signal through intrinsic
CC       mitochondrial cell death (By similarity). {ECO:0000250,
CC       ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY: tRNA uridine = tRNA pseudouridine.
CC   -!- PTM: Proteolytically cleaved during TRAIL-induced cell death.
CC       Cleaved, in vitro, either by caspase-3 or caspase-8 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase Pus10 family.
CC       {ECO:0000305}.
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; AL805916; CAI24204.1; -; Genomic_DNA.
DR   EMBL; AL672049; CAI24204.1; JOINED; Genomic_DNA.
DR   EMBL; BX255874; CAI24204.1; JOINED; Genomic_DNA.
DR   EMBL; BX255874; CAI26149.1; -; Genomic_DNA.
DR   EMBL; AL672049; CAI26149.1; JOINED; Genomic_DNA.
DR   EMBL; AL805916; CAI26149.1; JOINED; Genomic_DNA.
DR   EMBL; AL672049; CAM16949.1; -; Genomic_DNA.
DR   EMBL; AL805916; CAM16949.1; JOINED; Genomic_DNA.
DR   EMBL; BX255874; CAM16949.1; JOINED; 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   UniGene; Mm.29536; -.
DR   ProteinModelPortal; Q9D3U0; -.
DR   SMR; Q9D3U0; -.
DR   STRING; 10090.ENSMUSP00000020520; -.
DR   iPTMnet; Q9D3U0; -.
DR   PhosphoSitePlus; Q9D3U0; -.
DR   EPD; Q9D3U0; -.
DR   MaxQB; Q9D3U0; -.
DR   PaxDb; Q9D3U0; -.
DR   PeptideAtlas; Q9D3U0; -.
DR   PRIDE; Q9D3U0; -.
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   eggNOG; KOG2364; Eukaryota.
DR   eggNOG; COG1258; LUCA.
DR   GeneTree; ENSGT00390000007529; -.
DR   HOGENOM; HOG000030855; -.
DR   HOVERGEN; HBG056180; -.
DR   InParanoid; Q9D3U0; -.
DR   KO; K07583; -.
DR   OMA; IKKVCQK; -.
DR   OrthoDB; EOG091G06K1; -.
DR   PhylomeDB; Q9D3U0; -.
DR   TreeFam; TF106109; -.
DR   ChiTaRS; Pus10; mouse.
DR   PRO; PR:Q9D3U0; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000020280; -.
DR   CleanEx; MM_PUS10; -.
DR   ExpressionAtlas; Q9D3U0; baseline and differential.
DR   Genevisible; Q9D3U0; MM.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IBA:GO_Central.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom.
DR   SUPFAM; SSF55120; SSF55120; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Complete proteome; Isomerase; Phosphoprotein;
KW   Reference proteome; tRNA processing.
FT   CHAIN         1    527       Putative tRNA pseudouridine synthase
FT                                Pus10.
FT                                /FTId=PRO_0000299023.
FT   REGION      302    315       RNA binding forefinger loop.
FT                                {ECO:0000255}.
FT   REGION      440    455       RNA binding thumb loop. {ECO:0000255}.
FT   COILED       42     87       {ECO:0000255}.
FT   ACT_SITE    342    342       Nucleophile. {ECO:0000255}.
FT   BINDING     412    412       Substrate. {ECO:0000255}.
FT   BINDING     483    483       Substrate. {ECO:0000255}.
FT   MOD_RES      82     82       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q3MIT2}.
FT   CONFLICT      7      7       E -> G (in Ref. 1; BAE26208).
FT                                {ECO:0000305}.
FT   CONFLICT     10     10       H -> R (in Ref. 1; BAE26208).
FT                                {ECO:0000305}.
FT   CONFLICT     26     26       L -> F (in Ref. 1; BAE26208).
FT                                {ECO:0000305}.
FT   CONFLICT    215    215       P -> S (in Ref. 1; BAB28439).
FT                                {ECO:0000305}.
FT   CONFLICT    218    218       A -> G (in Ref. 1; BAC26650).
FT                                {ECO:0000305}.
FT   CONFLICT    258    258       D -> G (in Ref. 1; BAB28439).
FT                                {ECO:0000305}.
FT   CONFLICT    268    268       N -> H (in Ref. 1; BAC26650).
FT                                {ECO:0000305}.
FT   CONFLICT    269    269       S -> L (in Ref. 1; BAB28439).
FT                                {ECO:0000305}.
FT   CONFLICT    289    289       A -> G (in Ref. 1; BAC26650).
FT                                {ECO:0000305}.
FT   CONFLICT    329    329       R -> K (in Ref. 1; BAE26208).
FT                                {ECO:0000305}.
FT   CONFLICT    487    487       F -> L (in Ref. 1; BAC25908).
FT                                {ECO:0000305}.
FT   CONFLICT    522    522       P -> T (in Ref. 1; BAC25908).
FT                                {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
//