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Q8JZY4 (MRRP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 › Mus

Protein attributes

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

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 BAB25874.1 differs from that shown. Reason: Erroneous initiation.

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

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentMitochondrion
   DomainTransit peptide
   Technical termComplete proteome
Reference proteome
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...

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

Sequences

Sequence LengthMass (Da)Tools
Q8JZY4 [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

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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. NM_025373.1.
UniGeneMm.383213.

3D structure databases

ProteinModelPortalQ8JZY4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8JZY4.

PTM databases

PhosphoSiteQ8JZY4.

Proteomic databases

PRIDEQ8JZY4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021411; ENSMUSP00000021411; ENSMUSG00000021023.
GeneID66132.
KEGGmmu:66132.
UCSCuc007noo.2. mouse.

Organism-specific databases

MGIMGI:1913382. 1110008L16Rik.
RougeSearch...

Phylogenomic databases

eggNOGroNOG12234.
GeneTreeENSGT00390000002201.
HOGENOMHBG444588.
HOVERGENHBG099441.
InParanoidQ8JZY4.
OMAQKSGQCS.
OrthoDBEOG4DBTFD.

Gene expression databases

ArrayExpressQ8JZY4.
BgeeQ8JZY4.
GenevestigatorQ8JZY4.

Family and domain databases

ProtoNetSearch...

Other

NextBio320728.
SOURCESearch...

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: September 21, 2011
This is version 65 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents