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Protein

Mitochondrial-processing peptidase subunit beta

Gene

MAS1

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.

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi70 – 701ZincPROSITE-ProRule annotation1 Publication
Active sitei73 – 731Proton acceptor
Metal bindingi74 – 741ZincPROSITE-ProRule annotation1 Publication
Metal bindingi150 – 1501ZincPROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: Reactome

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16673.
YEAST:G3O-32293-MONOMER.
ReactomeiREACT_334110. Mitochondrial protein import.
SABIO-RKP10507.

Protein family/group databases

MEROPSiM16.980.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial-processing peptidase subunit beta (EC:3.4.24.64)
Alternative name(s):
Beta-MPP
PEP
Gene namesi
Name:MAS1
Synonyms:MIF1
Ordered Locus Names:YLR163C
ORF Names:L9632.10
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR163c.
SGDiS000004153. MAS1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731E → Q: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2020Mitochondrion1 PublicationAdd
BLAST
Chaini21 – 462442Mitochondrial-processing peptidase subunit betaPRO_0000026784Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei243 – 2431Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP10507.
PaxDbiP10507.
PeptideAtlasiP10507.
PRIDEiP10507.

Expressioni

Gene expression databases

GenevestigatoriP10507.

Interactioni

Subunit structurei

Heterodimer of alpha and beta subunits.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MAS2P119145EBI-11212,EBI-11205

Protein-protein interaction databases

BioGridi31436. 21 interactions.
DIPiDIP-2402N.
IntActiP10507. 14 interactions.
MINTiMINT-614379.
STRINGi4932.YLR163C.

Structurei

Secondary structure

1
462
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 304Combined sources
Beta strandi36 – 416Combined sources
Beta strandi46 – 5510Combined sources
Helixi58 – 603Combined sources
Turni63 – 675Combined sources
Helixi68 – 758Combined sources
Beta strandi78 – 825Combined sources
Helixi85 – 9410Combined sources
Beta strandi98 – 1036Combined sources
Beta strandi105 – 11511Combined sources
Helixi116 – 1183Combined sources
Helixi119 – 13113Combined sources
Helixi137 – 15418Combined sources
Helixi158 – 17013Combined sources
Turni171 – 1733Combined sources
Helixi175 – 1773Combined sources
Helixi184 – 1896Combined sources
Helixi192 – 20211Combined sources
Helixi205 – 2073Combined sources
Beta strandi208 – 2158Combined sources
Helixi218 – 22912Combined sources
Beta strandi254 – 2596Combined sources
Beta strandi264 – 27310Combined sources
Helixi282 – 29211Combined sources
Beta strandi294 – 2963Combined sources
Turni297 – 2993Combined sources
Beta strandi302 – 3054Combined sources
Helixi308 – 3147Combined sources
Beta strandi321 – 3299Combined sources
Beta strandi334 – 34310Combined sources
Turni344 – 3463Combined sources
Helixi349 – 36416Combined sources
Helixi370 – 38516Combined sources
Helixi391 – 40515Combined sources
Helixi411 – 4199Combined sources
Helixi423 – 43311Combined sources
Beta strandi434 – 4363Combined sources
Beta strandi439 – 4457Combined sources
Helixi447 – 4493Combined sources
Helixi453 – 4619Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HR6X-ray2.50B/D/F/H21-462[»]
1HR7X-ray2.55B/D/F/H21-462[»]
1HR8X-ray2.70B/D/F/H21-462[»]
1HR9X-ray3.01B/D/F/H21-462[»]
ProteinModelPortaliP10507.
SMRiP10507. Positions 23-462.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10507.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M16 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0612.
GeneTreeiENSGT00550000074701.
HOGENOMiHOG000242450.
InParanoidiP10507.
KOiK17732.
OMAiSTHKGEI.
OrthoDBiEOG7BW0TR.

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.

P10507-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSRTASKFR NTRRLLSTIS SQIPGTRTSK LPNGLTIATE YIPNTSSATV
60 70 80 90 100
GIFVDAGSRA ENVKNNGTAH FLEHLAFKGT QNRSQQGIEL EIENIGSHLN
110 120 130 140 150
AYTSRENTVY YAKSLQEDIP KAVDILSDIL TKSVLDNSAI ERERDVIIRE
160 170 180 190 200
SEEVDKMYDE VVFDHLHEIT YKDQPLGRTI LGPIKNIKSI TRTDLKDYIT
210 220 230 240 250
KNYKGDRMVL AGAGAVDHEK LVQYAQKYFG HVPKSESPVP LGSPRGPLPV
260 270 280 290 300
FCRGERFIKE NTLPTTHIAI ALEGVSWSAP DYFVALATQA IVGNWDRAIG
310 320 330 340 350
TGTNSPSPLA VAASQNGSLA NSYMSFSTSY ADSGLWGMYI VTDSNEHNVQ
360 370 380 390 400
LIVNEILKEW KRIKSGKISD AEVNRAKAQL KAALLLSLDG STAIVEDIGR
410 420 430 440 450
QVVTTGKRLS PEEVFEQVDK ITKDDIIMWA NYRLQNKPVS MVALGNTSTV
460
PNVSYIEEKL NQ
Length:462
Mass (Da):51,084
Last modified:July 1, 1989 - v1
Checksum:i084CE63C495EDFC4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07649 Genomic DNA. Translation: CAA30489.1.
U51921 Genomic DNA. Translation: AAB67487.1.
AY693198 Genomic DNA. Translation: AAT93217.1.
BK006945 Genomic DNA. Translation: DAA09485.1.
PIRiS00552.
RefSeqiNP_013264.1. NM_001182050.1.

Genome annotation databases

EnsemblFungiiYLR163C; YLR163C; YLR163C.
GeneIDi850860.
KEGGisce:YLR163C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07649 Genomic DNA. Translation: CAA30489.1.
U51921 Genomic DNA. Translation: AAB67487.1.
AY693198 Genomic DNA. Translation: AAT93217.1.
BK006945 Genomic DNA. Translation: DAA09485.1.
PIRiS00552.
RefSeqiNP_013264.1. NM_001182050.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HR6X-ray2.50B/D/F/H21-462[»]
1HR7X-ray2.55B/D/F/H21-462[»]
1HR8X-ray2.70B/D/F/H21-462[»]
1HR9X-ray3.01B/D/F/H21-462[»]
ProteinModelPortaliP10507.
SMRiP10507. Positions 23-462.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31436. 21 interactions.
DIPiDIP-2402N.
IntActiP10507. 14 interactions.
MINTiMINT-614379.
STRINGi4932.YLR163C.

Protein family/group databases

MEROPSiM16.980.

Proteomic databases

MaxQBiP10507.
PaxDbiP10507.
PeptideAtlasiP10507.
PRIDEiP10507.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR163C; YLR163C; YLR163C.
GeneIDi850860.
KEGGisce:YLR163C.

Organism-specific databases

CYGDiYLR163c.
SGDiS000004153. MAS1.

Phylogenomic databases

eggNOGiCOG0612.
GeneTreeiENSGT00550000074701.
HOGENOMiHOG000242450.
InParanoidiP10507.
KOiK17732.
OMAiSTHKGEI.
OrthoDBiEOG7BW0TR.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16673.
YEAST:G3O-32293-MONOMER.
ReactomeiREACT_334110. Mitochondrial protein import.
SABIO-RKP10507.

Miscellaneous databases

EvolutionaryTraceiP10507.
NextBioi967179.
PROiP10507.

Gene expression databases

GenevestigatoriP10507.

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. "MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease."
    Witte C., Jensen R.E., Yaffe M.P., Schatz G.
    EMBO J. 7:1439-1447(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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 21-32.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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 21-462 IN COMPLEX WITH ZINC AND SUBSTRATES, MUTAGENESIS OF GLU-73.

Entry informationi

Entry nameiMPPB_YEAST
AccessioniPrimary (citable) accession number: P10507
Secondary accession number(s): D6VYG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 1, 2015
This is version 156 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 1360 molecules/cell in log phase SD medium.1 Publication

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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.