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Protein

Mitochondrial-processing peptidase subunit alpha

Gene

Pmpca

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Protein family/group databases

MEROPSiM16.985.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial-processing peptidase subunit alpha (EC:3.4.24.64)
Alternative name(s):
Alpha-MPP
P-55
Gene namesi
Name:Pmpca
Synonyms:Inpp5e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1918568. Pmpca.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionBy similarityAdd
BLAST
Chaini34 – 524491Mitochondrial-processing peptidase subunit alphaPRO_0000026768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631N6-succinyllysineCombined sources
Modified residuei298 – 2981N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9DC61.
MaxQBiQ9DC61.
PaxDbiQ9DC61.
PRIDEiQ9DC61.

PTM databases

iPTMnetiQ9DC61.
SwissPalmiQ9DC61.

Expressioni

Gene expression databases

BgeeiQ9DC61.
CleanExiMM_INPP5E.
MM_PMPCA.
ExpressionAtlasiQ9DC61. baseline and differential.
GenevisibleiQ9DC61. MM.

Interactioni

Subunit structurei

Heterodimer of alpha and beta subunits.By similarity

Protein-protein interaction databases

BioGridi211772. 1 interaction.
IntActiQ9DC61. 3 interactions.
MINTiMINT-1841068.
STRINGi10090.ENSMUSP00000075762.

Structurei

3D structure databases

ProteinModelPortaliQ9DC61.
SMRiQ9DC61. Positions 67-486.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M16 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2067. Eukaryota.
COG0612. LUCA.
GeneTreeiENSGT00550000074666.
HOGENOMiHOG000206848.
HOVERGENiHBG106890.
InParanoidiQ9DC61.
KOiK01412.
OMAiEFILMAG.
OrthoDBiEOG76HQ1Q.
PhylomeDBiQ9DC61.
TreeFamiTF105031.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 2 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9DC61-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATAVWAAAR LLRGSAVLCA RPRFGSPAHR RFSSGATYPN IPLSSPLPGV
60 70 80 90 100
PKPIFATVDG QEKFETKVTT LDNGLRVASQ NKFGQFCTVG ILINSGSRYE
110 120 130 140 150
AKYLSGIAHF LEKLAFSSTA RFDSKDEILL TLEKHGGICD CQTSRDTTMY
160 170 180 190 200
AVSADSKGLD TVVDLLADVV LHPRLTDEEI EMTRMAVQFE LEDLNMRPDP
210 220 230 240 250
EPLLTEMIHE AAFRENTVGL HRFCPVENIA KIDREVLHSY LKNYYTPDRM
260 270 280 290 300
VLAGVGVEHE HLVECARKYL VGAEPAWGAP GTVDVDRSVA QYTGGIIKVE
310 320 330 340 350
RDMSNVSLGP TPIPELTHIM VGLESCSFLE DDFIPFAVLN MMMGGGGSFS
360 370 380 390 400
AGGPGKGMFS RLYLNVLNRH HWMYNATSYH HSYEDTGLLC IHASADPRQV
410 420 430 440 450
REMVEIITKE FILMGRTVDL VELERAKTQL MSMLMMNLES RPVIFEDVGR
460 470 480 490 500
QVLATHSRKL PHELCTLIRN VKPEDIKRVA SKMLRGKPAV AALGDLTDLP
510 520
TYEHIQAALS SRNGHLPRSY RLFR
Length:524
Mass (Da):58,279
Last modified:June 1, 2001 - v1
Checksum:iAD15AE6C97E95F9A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15804.1.
RefSeqiNP_775272.1. NM_173180.3.
UniGeneiMm.250359.
Mm.330070.

Genome annotation databases

EnsembliENSMUST00000076431; ENSMUSP00000075762; ENSMUSG00000026926.
GeneIDi66865.
KEGGimmu:66865.
UCSCiuc008ive.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15804.1.
RefSeqiNP_775272.1. NM_173180.3.
UniGeneiMm.250359.
Mm.330070.

3D structure databases

ProteinModelPortaliQ9DC61.
SMRiQ9DC61. Positions 67-486.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211772. 1 interaction.
IntActiQ9DC61. 3 interactions.
MINTiMINT-1841068.
STRINGi10090.ENSMUSP00000075762.

Protein family/group databases

MEROPSiM16.985.

PTM databases

iPTMnetiQ9DC61.
SwissPalmiQ9DC61.

Proteomic databases

EPDiQ9DC61.
MaxQBiQ9DC61.
PaxDbiQ9DC61.
PRIDEiQ9DC61.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000076431; ENSMUSP00000075762; ENSMUSG00000026926.
GeneIDi66865.
KEGGimmu:66865.
UCSCiuc008ive.1. mouse.

Organism-specific databases

CTDi23203.
MGIiMGI:1918568. Pmpca.

Phylogenomic databases

eggNOGiKOG2067. Eukaryota.
COG0612. LUCA.
GeneTreeiENSGT00550000074666.
HOGENOMiHOG000206848.
HOVERGENiHBG106890.
InParanoidiQ9DC61.
KOiK01412.
OMAiEFILMAG.
OrthoDBiEOG76HQ1Q.
PhylomeDBiQ9DC61.
TreeFamiTF105031.

Miscellaneous databases

ChiTaRSiPmpca. mouse.
PROiQ9DC61.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DC61.
CleanExiMM_INPP5E.
MM_PMPCA.
ExpressionAtlasiQ9DC61. baseline and differential.
GenevisibleiQ9DC61. MM.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 2 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMPPA_MOUSE
AccessioniPrimary (citable) accession number: Q9DC61
Secondary accession number(s): Q3TF19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.