P56960 (EXOSX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Exosome component 10
EC=3.1.13.-

Alternative name(s):
Autoantigen PM/Scl 2 homolog
Polymyositis/scleroderma autoantigen 2 homolog

Gene names

Name:	Exosc10
Synonyms:	Pmscl2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	887 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Putative 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. EXOSC10 has 3'-5' exonuclease activity By similarity. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of SKIV2L2, C1D and MPP6 wth the RNA exosome involved in the maturation of 5.8S rRNA By similarity.
Subunit structure	Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Interacts with C1D and MPHOSPH6 By similarity. MPHOSPH6 By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus › nucleolus By similarity. Nucleus By similarity.
Sequence similarities	Contains 1 HRDC domain.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay rRNA processing
Cellular component	Cytoplasm Exosome Nucleus
Ligand	RNA-binding
Molecular function	Exonuclease Hydrolase Nuclease
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	CUT catabolic process Inferred from electronic annotation. Source: Compara dosage compensation by inactivation of X chromosome Inferred from mutant phenotype PubMed 16789828. Source: MGI histone mRNA catabolic process Inferred from sequence or structural similarity. Source: UniProtKB maturation of 5.8S rRNA Inferred from electronic annotation. Source: Compara nuclear polyadenylation-dependent rRNA catabolic process Inferred from electronic annotation. Source: Compara nuclear retention of unspliced pre-mRNA at the site of transcription Inferred from electronic annotation. Source: Compara nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB exosome (RNase complex) Inferred from sequence or structural similarity. Source: UniProtKB nuclear exosome (RNase complex) Inferred from electronic annotation. Source: InterPro nucleolus Inferred from sequence or structural similarity. Source: UniProtKB transcriptionally active chromatin Inferred from electronic annotation. Source: Compara
Molecular_function	3'-5' exonuclease activity Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW exoribonuclease activity Inferred from electronic annotation. Source: Compara nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 887	887	Exosome component 10		PRO_0000087134
Regions
	Domain	503 – 583	81	HRDC
Experimental info
	Sequence conflict	792	1	I → V in AAF01779. Ref.1
	Sequence conflict	792	1	I → V in AAF01781. Ref.1
	Sequence conflict	860	1	C → F in AAF01779. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P56960 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 173164944163620C	FASTA	887	100,942
	10 20 30 40 50 60 MAPPSPREHQ SAPATSATKP DAEMVLPGFP DADSFVKFAL GSVVAVTKAS GGLPQFGDEY 70 80 90 100 110 120 DFYRSFPAFQ AFCETQGDRL LQCMSRVMQY HGCRSNIKDR SKVTELEDKF DLLVDTNDVI 130 140 150 160 170 180 LERVGMLLDE ASGVNKHQQP VLPAGLQVPK TIVSSWNRKA GEYGKKAKSE TFRLLHAKNI 190 200 210 220 230 240 VRPQLRFREK IDNSNTPFLP KIFVKPNARK PLPLALSKER RERPQDRPED LDVPPALADF 250 260 270 280 290 300 IHQQRTQQVE QDMFAHPYQY ELDHFTPPQS VLQRPKPQLY RAVGETPCHL VSSLDELVEL 310 320 330 340 350 360 NEKLLGCQEF AVDLEHHSYR SFLGLTCLMQ ISTRTEDFIV DTLELRSDMY ILNESLTDPA 370 380 390 400 410 420 IVKVFHGADS DIEWLQKDFG LYVVNMFDTH QAARLLNLAR HSLDHLLRLY CGVESNKQYQ 430 440 450 460 470 480 LADWRIRPLP EEMLSYARDD THYLLYIYDR MRLELWERGN HQPVQLQVVW QRSRDICLKK 490 500 510 520 530 540 FVKPIFTDES YLELYRKQKK HLNSQQLTAF QLLFAWRDKT ARREDESYGY VLPNHMMLKI 550 560 570 580 590 600 AEELPKEPQG IIACCNPVPP LVRQQINEMH LLIQQAREMP LLKSENAAGV RKSGPLPSAE 610 620 630 640 650 660 RLENDLFGPH DCSHAPPDNY QNTSTDGTLP LQKQPSLFTE GKEETSVDAG CLLATAVITL 670 680 690 700 710 720 FSEPNTEEGG KTPLTVAQKK AQNIMQSFEN PFRMFLPSLE HKAHISQAAK FDPSSKIYEI 730 740 750 760 770 780 SNRWKLASQV QVQKEPKEAT KKKVAEQTAA REEAKEEAAA GVLEQAIPVR QQAALENATK 790 800 810 820 830 840 KRERATSDLR TIEQKQEKKR LKSSKKAKDP DPPGKDFSPY DYSQSDFRAF AGDSKSKPSS 850 860 870 880 QFDPNKLAPS GKKGVGAKKC KQSVGNKSMS FAVGKSDRGF RHNWPKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and localization of mouse Pmscl1 and Pmscl2 genes." Bliskovski V., Liddell R., Ramsay E.S., Miller M.J., Mock B.A. Genomics 64:106-110(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: 129/SvJ and BALB/c.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 395-400, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF091392 mRNA. Translation: AAF01779.1. AF091505 , AF091506, AF092074, AF092075, AF092076, AF092077, AF092078, AF092079, AF092080, AF092081, AF092082, AF092083 Genomic DNA. Translation: AAF01781.1. AL606969, AL713995 Genomic DNA. Translation: CAM21195.1. AL713995, AL606969 Genomic DNA. Translation: CAM23945.1.
IPI	IPI00342382.
RefSeq	NP_057908.2. NM_016699.2.
UniGene	Mm.266635.
3D structure databases
ProteinModelPortal	P56960.
SMR	P56960. Positions 179-595.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4094804.
PTM databases
PhosphoSite	P56960.
Proteomic databases
PaxDb	P56960.
PRIDE	P56960.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000017408; ENSMUSP00000017408; ENSMUSG00000017264.
GeneID	50912.
KEGG	mmu:50912.
UCSC	uc008vut.2. mouse.
Organism-specific databases
CTD	5394.
MGI	MGI:1355322. Exosc10.
Phylogenomic databases
eggNOG	COG0349.
GeneTree	ENSGT00390000015408.
HOGENOM	HOG000001579.
HOVERGEN	HBG051524.
InParanoid	B1ARY9.
KO	K12591.
OMA	GNKSMSF.
OrthoDB	EOG4X6C7P.
Gene expression databases
ArrayExpress	P56960.
Bgee	P56960.
CleanEx	MM_EXOSC10.
Genevestigator	P56960.
GermOnline	ENSMUSG00000017264. Mus musculus.
Family and domain databases
InterPro	IPR002562. 3'-5'_exonuclease_dom. IPR012588. Exosome-assoc_fac_Rrp6_N. IPR010997. HRDC-like. IPR002121. HRDC_dom. IPR012337. RNaseH-like_dom. [Graphical view]
Pfam	PF01612. DNA_pol_A_exo1. 1 hit. PF00570. HRDC. 1 hit. PF08066. PMC2NT. 1 hit. [Graphical view]
SMART	SM00474. 35EXOc. 1 hit. SM00341. HRDC. 1 hit. [Graphical view]
SUPFAM	SSF47819. HRDC_like. 1 hit. SSF53098. RNaseH_fold. 1 hit.
PROSITE	PS50967. HRDC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EXOSC10. mouse.
NextBio	307899.
SOURCE	Search...

Entry information

Entry name

EXOSX_MOUSE

Accession

Primary (citable) accession number: P56960
Secondary accession number(s): B1ARY9, Q9QYS8, Q9R0B1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	July 27, 2011
Last modified:	May 29, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program