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Q9DB28 (POP5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease P/MRP protein subunit POP5

EC=3.1.26.5
Gene names
Name:Pop5
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length169 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP By similarity.

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.

Subunit structure

Component of nuclear RNase P and RNase MRP ribonucleoproteins. RNase P consists of a RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. RNase MRP consists of a RNA moiety and at least 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38, RPP40, POP5 and RPP21 By similarity.

Subcellular location

Nucleusnucleolus By similarity.

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 2 family.

Sequence caution

The sequence BAB28294.1 differs from that shown. Reason: Frameshift at position 44.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentNucleus
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtRNA processing

Inferred from direct assay. Source: MGI

   Cellular componentnucleolar ribonuclease P complex

Inferred from direct assay. Source: MGI

   Molecular functionribonuclease P activity

Inferred from direct assay. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 169169Ribonuclease P/MRP protein subunit POP5
PRO_0000239008

Experimental info

Sequence conflict21V → R in BAB28751. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9DB28 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 8334DECD7665A48D

FASTA16919,285
        10         20         30         40         50         60 
MVRFKHRYLL CELVSEDARC RLSLDDRVLG GLVRDTIARV HGAFGAAACS VGFAVRYLNA 

        70         80         90        100        110        120 
YTGVVLLRCR KDFYQLVWSA LPFITYLENK GHRYPCFFNT LHVGGTIRTC QKFLIQYNRR 

       130        140        150        160 
QLLILLQNCT DEGEREAIKK SVSRSCLLDR EPVEELSDSA GEEVAEAME 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum and Embryo.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK005290 mRNA. Translation: BAB23935.1.
AK012523 mRNA. Translation: BAB28294.1. Frameshift.
AK013257 mRNA. Translation: BAB28751.1.
BC022670 mRNA. Translation: AAH22670.1.
IPIIPI00756093.
RefSeqNP_080674.1. NM_026398.4.
UniGeneMm.24636.

3D structure databases

ProteinModelPortalQ9DB28.
SMRQ9DB28. Positions 1-120.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9DB28.

PTM databases

PhosphoSiteQ9DB28.

Proteomic databases

PRIDEQ9DB28.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081497; ENSMUSP00000080215; ENSMUSG00000060152.
ENSMUST00000135455; ENSMUSP00000118408; ENSMUSG00000060152.
GeneID117109.
KEGGmmu:117109.
UCSCuc008zdi.1. mouse.

Organism-specific databases

CTD51367.
MGIMGI:2151221. Pop5.

Phylogenomic databases

eggNOGroNOG16661.
GeneTreeENSGT00390000012331.
HOGENOMHBG713344.
HOVERGENHBG082157.
InParanoidQ9DB28.
OMACEVVSDD.
OrthoDBEOG49W2GX.

Gene expression databases

ArrayExpressQ9DB28.
BgeeQ9DB28.
GenevestigatorQ9DB28.
GermOnlineENSMUSG00000060152. Mus musculus.

Family and domain databases

InterProIPR016819. RNase_P/MRP_POP5.
IPR002759. RNase_P/MRP_subunit.
[Graphical view]
KOK03537.
PfamPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
PIRSFPIRSF023803. Ribonuclease_P_prd. 1 hit.
ProtoNetSearch...

Other

NextBio369498.
SOURCESearch...

Entry information

Entry namePOP5_MOUSE
AccessionPrimary (citable) accession number: Q9DB28
Secondary accession number(s): Q9CSC3, Q9CSL4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2001
Last modified: November 16, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families