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Reviewed, UniProtKB/Swiss-Prot Q9DC61 (MPPA_MOUSE)

Last modified June 16, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
    Mitochondrial-processing peptidase subunit alpha
    EC=3.4.24.64
Alternative name(s):
    Alpha-MPP
    P-55
Gene names
Name: Pmpca
Synonyms: Inpp5e
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Cleaves presequences (transit peptides) from mitochondrial protein precursors By similarity.

Catalytic activity

Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.

Subunit structure

Heterodimer of alpha and beta subunits By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the peptidase M16 family.

Caution

Does not seem to have a protease activity as it lack the zinc-binding site.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion By similarity
Chain34 – 524491Mitochondrial-processing peptidase subunit alpha
PRO_0000026768

Sequences

Sequence LengthMass (Da)Tools
Q9DC61-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: AD15AE6C97E95F9A

FASTA52458,279
        10         20         30         40         50         60 
MATAVWAAAR LLRGSAVLCA RPRFGSPAHR RFSSGATYPN IPLSSPLPGV PKPIFATVDG 

        70         80         90        100        110        120 
QEKFETKVTT LDNGLRVASQ NKFGQFCTVG ILINSGSRYE AKYLSGIAHF LEKLAFSSTA 

       130        140        150        160        170        180 
RFDSKDEILL TLEKHGGICD CQTSRDTTMY AVSADSKGLD TVVDLLADVV LHPRLTDEEI 

       190        200        210        220        230        240 
EMTRMAVQFE LEDLNMRPDP EPLLTEMIHE AAFRENTVGL HRFCPVENIA KIDREVLHSY 

       250        260        270        280        290        300 
LKNYYTPDRM VLAGVGVEHE HLVECARKYL VGAEPAWGAP GTVDVDRSVA QYTGGIIKVE 

       310        320        330        340        350        360 
RDMSNVSLGP TPIPELTHIM VGLESCSFLE DDFIPFAVLN MMMGGGGSFS AGGPGKGMFS 

       370        380        390        400        410        420 
RLYLNVLNRH HWMYNATSYH HSYEDTGLLC IHASADPRQV REMVEIITKE FILMGRTVDL 

       430        440        450        460        470        480 
VELERAKTQL MSMLMMNLES RPVIFEDVGR QVLATHSRKL PHELCTLIRN VKPEDIKRVA 

       490        500        510        520 
SKMLRGKPAV AALGDLTDLP TYEHIQAALS SRNGHLPRSY RLFR 

« Hide

References

« Hide 'large scale' 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: Heart and Lung.
[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: Kidney.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 250-267; 288-298; 362-369 AND 417-425, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.

Cross-references

Sequence databases

AK004549 mRNA. Translation: BAB23363.1.
AK147110 mRNA. Translation: BAE27682.1.
AK169325 mRNA. Translation: BAE41079.1.
AK169342 mRNA. Translation: BAE41094.1.
BC010810 mRNA. Translation: AAH10810.1.
IPIIPI00120199.
RefSeqNP_775272.1.
UniGeneMm.250359

3D structure databases

HSSPHSSP built from PDB template 1HR6 based on UniProtKB P11914.
ModBaseSearch...

Protein family/group databases

MEROPSM16.971.

Proteomic databases

PRIDEQ9DC61.

Genome annotation databases

EnsemblENSMUSG00000026926. Mus musculus. [Contig view]
GeneID66865.
KEGGmmu:66865.

Organism-specific databases

MGIMGI:1918568. Pmpca.

Phylogenomic databases

HOGENOMQ9DC61.
HOVERGENQ9DC61.
OMAQ9DC61. YRGNTVG.

Enzyme and pathway databases

BRENDA3.4.24.64. 244.

Gene expression databases

BgeeQ9DC61.
CleanExMM_INPP5E.
MM_PMPCA.
GermOnlineENSMUSG00000026926. Mus musculus.

Family and domain databases

InterProIPR011237. Pept_M16_core.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
Gene3DG3DSA:3.30.830.10. Pept_M16_core. 2 hits.
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
PROSITEPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio322859.
SOURCESearch...

Entry information

Entry nameMPPA_MOUSE
AccessionPrimary (citable) accession number: Q9DC61
Secondary accession number(s): Q3TF19
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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