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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

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Enzyme and pathway databases

BioCyciMetaCyc:G3O-31085-MONOMER.
YEAST:G3O-31085-MONOMER.
ReactomeiR-SCE-1268020. 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
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR024C.
SGDiS000001066. MAS2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 13Mitochondrion1 PublicationAdd BLAST13
ChainiPRO_000002677314 – 482Mitochondrial-processing peptidase subunit alphaAdd BLAST469

Proteomic databases

MaxQBiP11914.
PRIDEiP11914.

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. 12 interactors.
DIPiDIP-2401N.
IntActiP11914. 6 interactors.
MINTiMINT-630854.

Structurei

Secondary structure

1482
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni15 – 18Combined sources4
Beta strandi20 – 23Combined sources4
Beta strandi29 – 34Combined sources6
Beta strandi38 – 47Combined sources10
Helixi50 – 52Combined sources3
Turni54 – 59Combined sources6
Helixi60 – 66Combined sources7
Turni67 – 69Combined sources3
Beta strandi72 – 75Combined sources4
Helixi77 – 86Combined sources10
Beta strandi91 – 95Combined sources5
Beta strandi100 – 106Combined sources7
Helixi108 – 110Combined sources3
Helixi111 – 123Combined sources13
Helixi129 – 146Combined sources18
Helixi150 – 162Combined sources13
Turni163 – 165Combined sources3
Helixi167 – 169Combined sources3
Helixi176 – 181Combined sources6
Helixi184 – 194Combined sources11
Helixi197 – 199Combined sources3
Beta strandi200 – 207Combined sources8
Helixi209 – 220Combined sources12
Beta strandi240 – 244Combined sources5
Beta strandi251 – 253Combined sources3
Beta strandi257 – 264Combined sources8
Helixi273 – 283Combined sources11
Beta strandi285 – 289Combined sources5
Helixi301 – 305Combined sources5
Turni306 – 309Combined sources4
Beta strandi311 – 322Combined sources12
Beta strandi327 – 335Combined sources9
Helixi337 – 342Combined sources6
Helixi343 – 352Combined sources10
Turni353 – 355Combined sources3
Helixi364 – 381Combined sources18
Helixi385 – 399Combined sources15
Helixi405 – 413Combined sources9
Helixi417 – 428Combined sources12
Beta strandi443 – 448Combined sources6
Helixi450 – 453Combined sources4
Helixi456 – 462Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11914.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M16 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00550000074666.
HOGENOMiHOG000206848.
InParanoidiP11914.
KOiK01412.
OMAiNDPEGME.
OrthoDBiEOG092C25X9.

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:October 1, 1989 - v1
Checksum:i0FDCD157388A56C7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti235A → P in CAA32262 (PubMed:3061808).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36455. 12 interactors.
DIPiDIP-2401N.
IntActiP11914. 6 interactors.
MINTiMINT-630854.

Protein family/group databases

MEROPSiM16.971.

Proteomic databases

MaxQBiP11914.
PRIDEiP11914.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YHR024C.
SGDiS000001066. MAS2.

Phylogenomic databases

GeneTreeiENSGT00550000074666.
HOGENOMiHOG000206848.
InParanoidiP11914.
KOiK01412.
OMAiNDPEGME.
OrthoDBiEOG092C25X9.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-31085-MONOMER.
YEAST:G3O-31085-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.
SABIO-RKP11914.

Miscellaneous databases

EvolutionaryTraceiP11914.
PROiP11914.

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...

Entry informationi

Entry nameiMPPA_YEAST
AccessioniPrimary (citable) accession number: P11914
Secondary accession number(s): D3DKX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 2, 2016
This is version 168 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

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.