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Reviewed, UniProtKB/Swiss-Prot Q8JZY4 (MRRP3_MOUSE)

Last modified December 15, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Mitochondrial ribonuclease P protein 3
      Short name=Mitochondrial RNase P protein 3
Gene names
Name: Kiaa0391
Synonyms: Mrpp3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length584 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/RG9MTD1, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends By similarity.

Subunit structure

Interacts with MRPP1/RG9MTD1 and MRPP2/HSD17B10 By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence caution

The sequence BAD32220.1 differs from that shown. Reason: Miscellaneous discrepancy. Partial sequence.

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Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentMitochondrion
   DomainTransit peptide
Gene Ontology (GO)
   Biological processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Mitochondrion Potential
Chain44 – 584541Mitochondrial ribonuclease P protein 3
PRO_0000360397

Experimental info

Sequence conflict4301L → V in BAC27278. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q8JZY4-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: BB68EF585649A3BD

FASTA58466,857
        10         20         30         40         50         60 
MTFYLSGFRS IPKLWKSNPY FELGPATSST PFFLCAIGNQ QRWFSVKPTT PPNSKALNLL 

        70         80         90        100        110        120 
DTKARTHRKG NDNNGQVSSD PHYFAAGAAK KRSHIGANPQ NQGHALPVRS SVQLPTKPLN 

       130        140        150        160        170        180 
SAEWDKLKED FKGKASFEDF IISQMARNCC SVDVAKSLLA WVAAKNNGIV GYNLLVKYLY 

       190        200        210        220        230        240 
LCVFHKQTSE VIDVYEIMKA KYKSLESGGY TLLIRGLIHS DRWRESLLLL EDIKKVMVPS 

       250        260        270        280        290        300 
KKNYGDCIQG ALLHQDVNTA WNLYQELIGH NLIPPLETLK AFFDYGKDIN DDHYSDKLLD 

       310        320        330        340        350        360 
ILLYLRNNQL YPGESFAHSI KTWFESIPGR QWKGQFTTIQ KSGQCSGCGR TIEPIHLSPE 

       370        380        390        400        410        420 
EYEFLKEKIM RDVIDGGDQY KKTTPQELKR FESFVNSCPP FDIVIDGLNV AKMFPKGRES 

       430        440        450        460        470        480 
QNLLGVVSQL AQQNLQLLVL GRKHMLRPSS QWRKEEMEQV RKQAHCFFAD NISEDDPFLL 

       490        500        510        520        530        540 
YATLNSGNHC KFITKDLLRD HKACLPDART QRLFFKWQQG HQLAIMKGFQ KSKLTFQHIL 

       550        560        570        580 
SYDTVVQRTG DSWHIPYDED LVQRSSCEVP TKWLCLQRKT PDPC

« Hide

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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: Bone marrow, Embryo, Forelimb and Stomach.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
Tissue: Mammary gland.
[4]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed: 15368895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 327-584.
Tissue: Splenocyte.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AK003589 mRNA. Translation: BAB22879.1.
AK008749 mRNA. Translation: BAB25874.1. Different initiation.
AK031144 mRNA. Translation: BAC27278.1.
AK151976 mRNA. Translation: BAE30844.1.
AK152028 mRNA. Translation: BAE30887.1.
CH466526 Genomic DNA. Translation: EDL36732.1.
BC034876 mRNA. Translation: AAH34876.1.
AK172942 mRNA. Translation: BAD32220.1. Sequence problems.
IPIIPI00172345.
RefSeqNP_079649.1.
UniGeneMm.383213

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ8JZY4.

Proteomic databases

PRIDEQ8JZY4.

Genome annotation databases

EnsemblENSMUST00000021411; ENSMUSP00000021411; ENSMUSG00000021023; Mus musculus. [Genome view]
GeneID66132.
KEGGmmu:66132.
UCSCuc007nop.1. mouse.

Organism-specific databases

MGIMGI:1913382. 1110008L16Rik.
RougeSearch...

Phylogenomic databases

HOGENOMHBG444588.
HOVERGENQ8JZY4.
InParanoidQ8JZY4.
OMAQTSEVID.
OrthoDBEOG944P5Q.

Gene expression databases

ArrayExpressQ8JZY4.
BgeeQ8JZY4.
GenevestigatorQ8JZY4.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio320728.
SOURCESearch...

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Entry information

Entry nameMRRP3_MOUSE
AccessionPrimary (citable) accession number: Q8JZY4
Secondary accession number(s): Q6A076 expand/collapse secondary AC list , Q8BSN8, Q9CTH1, Q9D7W9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: October 1, 2002
Last modified: December 15, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents