Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mitochondrial-processing peptidase subunit alpha

Gene

MAS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves presequences (transit peptides) from mitochondrial protein precursors. The cleavage sites typically contain an arginine at position -2 (in the N-terminal portion) from the scissible peptide bond in addition to other distal basic residues, and an aromatic residue at position +1.

Catalytic activityi

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

GO - Molecular functioni

  1. metal ion binding Source: InterPro
  2. metalloendopeptidase activity Source: InterPro

GO - Biological processi

  1. protein processing involved in protein targeting to mitochondrion Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16674.
YEAST:G3O-31085-MONOMER.
ReactomeiREACT_334110. Mitochondrial protein import.
SABIO-RKP11914.

Protein family/group databases

MEROPSiM16.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial-processing peptidase subunit alpha (EC:3.4.24.64)
Alternative name(s):
Alpha-MPP
Gene namesi
Name:MAS2
Synonyms:MIF2
Ordered Locus Names:YHR024C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VIII

Organism-specific databases

CYGDiYHR024c.
SGDiS000001066. MAS2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrial processing peptidase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1313Mitochondrion1 PublicationAdd
BLAST
Chaini14 – 482469Mitochondrial-processing peptidase subunit alphaPRO_0000026773Add
BLAST

Proteomic databases

MaxQBiP11914.
PaxDbiP11914.
PeptideAtlasiP11914.

Expressioni

Gene expression databases

GenevestigatoriP11914.

Interactioni

Subunit structurei

Heterodimer of alpha and beta subunits.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MAS1P105075EBI-11205,EBI-11212

Protein-protein interaction databases

BioGridi36455. 10 interactions.
DIPiDIP-2401N.
IntActiP11914. 6 interactions.
MINTiMINT-630854.
STRINGi4932.YHR024C.

Structurei

Secondary structure

1
482
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni15 – 184Combined sources
Beta strandi20 – 234Combined sources
Beta strandi29 – 346Combined sources
Beta strandi38 – 4710Combined sources
Helixi50 – 523Combined sources
Turni54 – 596Combined sources
Helixi60 – 667Combined sources
Turni67 – 693Combined sources
Beta strandi72 – 754Combined sources
Helixi77 – 8610Combined sources
Beta strandi91 – 955Combined sources
Beta strandi100 – 1067Combined sources
Helixi108 – 1103Combined sources
Helixi111 – 12313Combined sources
Helixi129 – 14618Combined sources
Helixi150 – 16213Combined sources
Turni163 – 1653Combined sources
Helixi167 – 1693Combined sources
Helixi176 – 1816Combined sources
Helixi184 – 19411Combined sources
Helixi197 – 1993Combined sources
Beta strandi200 – 2078Combined sources
Helixi209 – 22012Combined sources
Beta strandi240 – 2445Combined sources
Beta strandi251 – 2533Combined sources
Beta strandi257 – 2648Combined sources
Helixi273 – 28311Combined sources
Beta strandi285 – 2895Combined sources
Helixi301 – 3055Combined sources
Turni306 – 3094Combined sources
Beta strandi311 – 32212Combined sources
Beta strandi327 – 3359Combined sources
Helixi337 – 3426Combined sources
Helixi343 – 35210Combined sources
Turni353 – 3553Combined sources
Helixi364 – 38118Combined sources
Helixi385 – 39915Combined sources
Helixi405 – 4139Combined sources
Helixi417 – 42812Combined sources
Beta strandi443 – 4486Combined sources
Helixi450 – 4534Combined sources
Helixi456 – 4627Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HR6X-ray2.50A/C/E/G14-482[»]
1HR7X-ray2.55A/C/E/G14-482[»]
1HR8X-ray2.70A/C/E/G14-482[»]
1HR9X-ray3.01A/C/E/G14-482[»]
ProteinModelPortaliP11914.
SMRiP11914. Positions 14-470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11914.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M16 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0612.
GeneTreeiENSGT00550000074666.
HOGENOMiHOG000206848.
InParanoidiP11914.
KOiK01412.
OMAiGMECITA.
OrthoDBiEOG7N63XC.

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.

P11914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRNGVQRLY SNIARTDNFK LSSLANGLKV ATSNTPGHFS ALGLYIDAGS
60 70 80 90 100
RFEGRNLKGC THILDRLAFK STEHVEGRAM AETLELLGGN YQCTSSRENL
110 120 130 140 150
MYQASVFNQD VGKMLQLMSE TVRFPKITEQ ELQEQKLSAE YEIDEVWMKP
160 170 180 190 200
ELVLPELLHT AAYSGETLGS PLICPRELIP SISKYYLLDY RNKFYTPENT
210 220 230 240 250
VAAFVGVPHE KALELTEKYL GDWQSTHPPI TKKVAQYTGG ESCIPPAPVF
260 270 280 290 300
GNLPELFHIQ IGFEGLPIDH PDIYALATLQ TLLGGGGSFS AGGPGKGMYS
310 320 330 340 350
RLYTHVLNQY YFVENCVAFN HSYSDSGIFG ISLSCIPQAA PQAVEVIAQQ
360 370 380 390 400
MYNTFANKDL RLTEDEVSRA KNQLKSSLLM NLESKLVELE DMGRQVLMHG
410 420 430 440 450
RKIPVNEMIS KIEDLKPDDI SRVAEMIFTG NVNNAGNGKG RATVVMQGDR
460 470 480
GSFGDVENVL KAYGLGNSSS SKNDSPKKKG WF
Length:482
Mass (Da):53,338
Last modified:September 30, 1989 - v1
Checksum:i0FDCD157388A56C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti235 – 2351A → P in CAA32262 (PubMed:3061808).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13455 Genomic DNA. Translation: CAA31804.1.
X14105 Genomic DNA. Translation: CAA32262.1.
U10399 Genomic DNA. Translation: AAB68877.1.
BK006934 Genomic DNA. Translation: DAA06715.1.
PIRiS05738. ZPBY.
RefSeqiNP_011889.1. NM_001179154.1.

Genome annotation databases

EnsemblFungiiYHR024C; YHR024C; YHR024C.
GeneIDi856419.
KEGGisce:YHR024C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13455 Genomic DNA. Translation: CAA31804.1.
X14105 Genomic DNA. Translation: CAA32262.1.
U10399 Genomic DNA. Translation: AAB68877.1.
BK006934 Genomic DNA. Translation: DAA06715.1.
PIRiS05738. ZPBY.
RefSeqiNP_011889.1. NM_001179154.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HR6X-ray2.50A/C/E/G14-482[»]
1HR7X-ray2.55A/C/E/G14-482[»]
1HR8X-ray2.70A/C/E/G14-482[»]
1HR9X-ray3.01A/C/E/G14-482[»]
ProteinModelPortaliP11914.
SMRiP11914. Positions 14-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36455. 10 interactions.
DIPiDIP-2401N.
IntActiP11914. 6 interactions.
MINTiMINT-630854.
STRINGi4932.YHR024C.

Protein family/group databases

MEROPSiM16.971.

Proteomic databases

MaxQBiP11914.
PaxDbiP11914.
PeptideAtlasiP11914.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR024C; YHR024C; YHR024C.
GeneIDi856419.
KEGGisce:YHR024C.

Organism-specific databases

CYGDiYHR024c.
SGDiS000001066. MAS2.

Phylogenomic databases

eggNOGiCOG0612.
GeneTreeiENSGT00550000074666.
HOGENOMiHOG000206848.
InParanoidiP11914.
KOiK01412.
OMAiGMECITA.
OrthoDBiEOG7N63XC.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16674.
YEAST:G3O-31085-MONOMER.
ReactomeiREACT_334110. Mitochondrial protein import.
SABIO-RKP11914.

Miscellaneous databases

EvolutionaryTraceiP11914.
NextBioi981985.
PROiP11914.

Gene expression databases

GenevestigatoriP11914.

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 processing peptidase of yeast mitochondria: the two co-operating components MPP and PEP are structurally related."
    Pollock R.A., Hartl F.-U., Cheng M.Y., Ostermann J., Horwich A., Neupert W.
    EMBO J. 7:3493-3500(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MC3.
  2. "Import of proteins into yeast mitochondria: the nuclear MAS2 gene encodes a component of the processing protease that is homologous to the MAS1-encoded subunit."
    Jensen R.E., Yaffe M.P.
    EMBO J. 7:3863-3871(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "The MAS-encoded processing protease of yeast mitochondria. Interaction of the purified enzyme with signal peptides and a purified precursor protein."
    Yang M., Geli V., Oppliger W., Suda K., James P., Schatz G.
    J. Biol. Chem. 266:6416-6423(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 14-22.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences."
    Taylor A.B., Smith B.S., Kitada S., Kojima K., Miyaura H., Otwinowski Z., Ito A., Deisenhofer J.
    Structure 9:615-625(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 45-482 IN COMPLEX WITH SUBSTRATES.

Entry informationi

Entry nameiMPPA_YEAST
AccessioniPrimary (citable) accession number: P11914
Secondary accession number(s): D3DKX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1989
Last sequence update: September 30, 1989
Last modified: March 31, 2015
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 31400 molecules/cell in log phase SD medium.1 Publication

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

External Data

Dasty 3

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 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.