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Exosome complex component RRP45 (Autoantigen PM/Scl 1) (Exosome component 9) (P75 polymyositis-scleroderma overlap syndrome-associated autoantigen) (Polymyositis/scleroderma autoantigen 1) (Polymyositis/scleroderma autoantigen 75 kDa) (PM/Scl-75)

 EXOS9_MOUSE             Reviewed;         438 AA.
Q9JHI7; Q9CSZ2;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 136.
RecName: Full=Exosome complex component RRP45;
AltName: Full=Autoantigen PM/Scl 1;
AltName: Full=Exosome component 9;
AltName: Full=P75 polymyositis-scleroderma overlap syndrome-associated autoantigen;
AltName: Full=Polymyositis/scleroderma autoantigen 1;
AltName: Full=Polymyositis/scleroderma autoantigen 75 kDa;
Short=PM/Scl-75;
Name=Exosc9; Synonyms=Pmscl1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Brain, and Spleen;
PubMed=10708524; DOI=10.1006/geno.2000.6118;
Bliskovski V., Liddell R., Ramsay E.S., Miller M.J., Mock B.A.;
"Structure and localization of mouse Pmscl1 and Pmscl2 genes.";
Genomics 64:106-110(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-395.
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393 AND SER-395, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Liver, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Non-catalytic component of the RNA exosome complex which
has 3'->5' exoribonuclease activity and participates in a
multitude of cellular RNA processing and degradation events. In
the nucleus, the RNA exosome complex is involved in proper
maturation of stable RNA species such as rRNA, snRNA and snoRNA,
in the elimination of RNA processing by-products and non-coding
'pervasive' transcripts, such as antisense RNA species and
promoter-upstream transcripts (PROMPTs), and of mRNAs with
processing defects, thereby limiting or excluding their export to
the cytoplasm. The RNA exosome may be involved in Ig class switch
recombination (CSR) and/or Ig variable region somatic
hypermutation (SHM) by targeting AICDA deamination activity to
transcribed dsDNA substrates. In the cytoplasm, the RNA exosome
complex is involved in general mRNA turnover and specifically
degrades inherently unstable mRNAs containing AU-rich elements
(AREs) within their 3' untranslated regions, and in RNA
surveillance pathways, preventing translation of aberrant mRNAs.
It seems to be involved in degradation of histone mRNA. The
catalytic inactive RNA exosome core complex of 9 subunits (Exo-9)
is proposed to play a pivotal role in the binding and presentation
of RNA for ribonucleolysis, and to serve as a scaffold for the
association with catalytic subunits and accessory proteins or
complexes. EXOSC9 binds to ARE-containing RNAs (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Component of the RNA exosome complex. Specifically part
of the catalytically inactive RNA exosome core (Exo-9) complex
which is believed to associate with catalytic subunits EXOSC10,
and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome
complex forms. Exo-9 is formed by a hexameric ring of RNase PH
domain-containing subunits specifically containing the
heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and
peripheral S1 domain-containing components EXOSC1, EXOSC2 and
EXOSC3 located on the top of the ring structure. Interacts (via C-
terminus region) with SETX (via N-terminus domain); the
interaction enhances SETX sumoylation (By similarity).
{ECO:0000250|UniProtKB:Q06265}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
{ECO:0000250|UniProtKB:Q06265}. Nucleus
{ECO:0000250|UniProtKB:Q06265}. Nucleus, nucleoplasm
{ECO:0000250|UniProtKB:Q06265}. Note=Colocalizes with SETX in
nuclear foci upon induction of transcription-related DNA damage at
the S phase (By similarity). {ECO:0000250|UniProtKB:Q06265}.
-!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF152841; AAF73218.1; -; mRNA.
EMBL; AF152842; AAF73219.1; -; mRNA.
EMBL; BC005622; AAH05622.1; -; mRNA.
EMBL; BC052156; AAH52156.1; -; mRNA.
EMBL; AK011636; BAB27749.1; -; mRNA.
CCDS; CCDS17312.1; -.
RefSeq; NP_062266.1; NM_019393.2.
UniGene; Mm.116711; -.
ProteinModelPortal; Q9JHI7; -.
SMR; Q9JHI7; -.
IntAct; Q9JHI7; 1.
STRING; 10090.ENSMUSP00000029269; -.
iPTMnet; Q9JHI7; -.
PhosphoSitePlus; Q9JHI7; -.
EPD; Q9JHI7; -.
MaxQB; Q9JHI7; -.
PaxDb; Q9JHI7; -.
PeptideAtlas; Q9JHI7; -.
PRIDE; Q9JHI7; -.
Ensembl; ENSMUST00000029269; ENSMUSP00000029269; ENSMUSG00000027714.
GeneID; 50911; -.
KEGG; mmu:50911; -.
UCSC; uc008ozm.1; mouse.
CTD; 5393; -.
MGI; MGI:1355319; Exosc9.
eggNOG; KOG1614; Eukaryota.
eggNOG; COG2123; LUCA.
GeneTree; ENSGT00530000063093; -.
HOGENOM; HOG000229504; -.
HOVERGEN; HBG051523; -.
InParanoid; Q9JHI7; -.
KO; K03678; -.
OMA; MFMNSNL; -.
OrthoDB; EOG091G08FZ; -.
PhylomeDB; Q9JHI7; -.
TreeFam; TF300092; -.
Reactome; R-MMU-429958; mRNA decay by 3' to 5' exoribonuclease.
Reactome; R-MMU-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-MMU-450604; KSRP (KHSRP) binds and destabilizes mRNA.
Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
PRO; PR:Q9JHI7; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027714; -.
CleanEx; MM_EXOSC9; -.
ExpressionAtlas; Q9JHI7; baseline and differential.
Genevisible; Q9JHI7; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
GO; GO:0000178; C:exosome (RNase complex); ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
GO; GO:0000176; C:nuclear exosome (RNase complex); ISO:MGI.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0017091; F:AU-rich element binding; ISO:MGI.
GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IEA:Ensembl.
GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; ISO:MGI.
GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
GO; GO:0071028; P:nuclear mRNA surveillance; ISO:MGI.
GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IBA:GO_Central.
GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; ISO:MGI.
GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; ISO:MGI.
GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0034473; P:U1 snRNA 3'-end processing; IBA:GO_Central.
GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
GO; GO:0034476; P:U5 snRNA 3'-end processing; IBA:GO_Central.
CDD; cd11368; RNase_PH_RRP45; 1.
Gene3D; 3.30.230.70; -; 1.
InterPro; IPR001247; ExoRNase_PH_dom1.
InterPro; IPR015847; ExoRNase_PH_dom2.
InterPro; IPR036345; ExoRNase_PH_dom2_sf.
InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR033100; Rrp45.
Pfam; PF01138; RNase_PH; 1.
Pfam; PF03725; RNase_PH_C; 1.
SUPFAM; SSF54211; SSF54211; 2.
SUPFAM; SSF55666; SSF55666; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Exonuclease; Exosome;
Hydrolase; Isopeptide bond; Nuclease; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; rRNA processing; Ubl conjugation.
CHAIN 1 438 Exosome complex component RRP45.
/FTId=PRO_0000139972.
MOD_RES 65 65 Phosphoserine.
{ECO:0000250|UniProtKB:Q06265}.
MOD_RES 297 297 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q06265}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000250|UniProtKB:Q06265}.
MOD_RES 346 346 Phosphoserine.
{ECO:0000250|UniProtKB:Q06265}.
MOD_RES 393 393 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q06265}.
CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q06265}.
SEQUENCE 438 AA; 48937 MW; 7AAE63DBF12F5149 CRC64;
MKETPLSNCE RRFLLRAIEE KKRLDGRQTY DYRNIRISFG TDYGCCIVEL GKTRVLGQVS
CELVSPKLNR ATEGILFFNL ELSQMAAPAF EPGRQSDLLV KLNRLLERCL RNSKCIDTES
LCVVAGEKVW QIRVDLHLLN HDGNIIDAAS IAAIVALCHF RRPDVSVQGE EVTLYTPEER
DPVPLSIHHM PICVSFAFFQ QGTYLLVDPN EREERVMDGL LVIAMNKHRE ICTIQSSGGI
MLLKDQVFRC SKIAGVKVAE ITELIQKALE NDQRVRKEGG KFGFAESIAN QRITAFKMET
APIDTSNIEE RAEEIIAEAE PPPEVVSQPV LWTPGTAQIG DGIENSWGDL EDSEKEEEEE
EGGIDEAVIL DDTKMDTGEV SDIGSQGAPI VLSDSEEEEM IILEPEKNPK KIRAQTSANQ
KAPSKGQGKR KKKKRTAN


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