Reviewed, UniProtKB/Swiss-Prot P11914 (MPPA_YEAST)

Names and origin

Protein names

Recommended name:
    Mitochondrial-processing peptidase subunit alpha
    EC=3.4.24.64
Alternative name(s):
    Alpha-MPP

Gene names

Name:	MAS2
Synonyms:	MIF2
Ordered Locus Names:	YHR024C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 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.
Subcellular location	Mitochondrion matrix.
Miscellaneous	Present with 31400 molecules/cell in log phase SD medium. Ref.5
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 component	Mitochondrion
Domain	Transit peptide
Molecular function	Hydrolase Metalloprotease Protease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	mitochondrial protein processing during import Ref.2 Inferred from mutant phenotype. Source: SGD proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial processing peptidase complex Inferred from direct assay. Source: SGD
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MSH1	P25846	1	EBI-11205,EBI-11347

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 13

13

Mitochondrion Ref.4

Chain

14 – 482

469

Mitochondrial-processing peptidase subunit alpha

PRO_0000026773

Amino acid modifications

Modified residue

226

1

Phosphothreonine Ref.6

Modified residue

231

1

Phosphothreonine Ref.6

Experimental info

Sequence conflict

235

1

A → P in CAA32262. Ref.2

Secondary structure

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482

Helix Strand Turn

Details...

Beta strand

20 – 23

4

Beta strand

29 – 34

6

Beta strand

38 – 47

10

Helix

50 – 52

3

Turn

54 – 59

6

Helix

60 – 66

7

Turn

67 – 69

3

Helix

77 – 86

10

Beta strand

91 – 95

5

Beta strand

100 – 106

7

Helix

108 – 110

3

Helix

111 – 123

13

Helix

129 – 146

18

Helix

150 – 162

13

Turn

163 – 165

3

Helix

167 – 169

3

Helix

176 – 181

6

Helix

184 – 194

11

Helix

197 – 199

3

Beta strand

200 – 207

8

Helix

209 – 220

12

Beta strand

240 – 244

5

Beta strand

251 – 253

3

Beta strand

257 – 264

8

Helix

273 – 283

11

Beta strand

285 – 289

5

Helix

301 – 305

5

Turn

306 – 309

4

Beta strand

311 – 322

12

Beta strand

327 – 335

9

Helix

337 – 342

6

Helix

343 – 352

10

Turn

353 – 355

3

Helix

364 – 381

18

Helix

385 – 399

15

Helix

405 – 413

9

Helix

417 – 428

12

Beta strand

443 – 448

6

Helix

450 – 453

4

Helix

456 – 462

7

Sequences

	Sequence		Length	Mass (Da)
	P11914-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 0FDCD157388A56C7	FASTA	482	53,338
	10 20 30 40 50 60 MLRNGVQRLY SNIARTDNFK LSSLANGLKV ATSNTPGHFS ALGLYIDAGS RFEGRNLKGC 70 80 90 100 110 120 THILDRLAFK STEHVEGRAM AETLELLGGN YQCTSSRENL MYQASVFNQD VGKMLQLMSE 130 140 150 160 170 180 TVRFPKITEQ ELQEQKLSAE YEIDEVWMKP ELVLPELLHT AAYSGETLGS PLICPRELIP 190 200 210 220 230 240 SISKYYLLDY RNKFYTPENT VAAFVGVPHE KALELTEKYL GDWQSTHPPI TKKVAQYTGG 250 260 270 280 290 300 ESCIPPAPVF GNLPELFHIQ IGFEGLPIDH PDIYALATLQ TLLGGGGSFS AGGPGKGMYS 310 320 330 340 350 360 RLYTHVLNQY YFVENCVAFN HSYSDSGIFG ISLSCIPQAA PQAVEVIAQQ MYNTFANKDL 370 380 390 400 410 420 RLTEDEVSRA KNQLKSSLLM NLESKLVELE DMGRQVLMHG RKIPVNEMIS KIEDLKPDDI 430 440 450 460 470 480 SRVAEMIFTG NVNNAGNGKG RATVVMQGDR GSFGDVENVL KAYGLGNSSS SKNDSPKKKG WF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(1988) [PubMed: 3061797] [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(1988) [PubMed: 3061808] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M. Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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(1991) [PubMed: 2007593] [Abstract] Cited for: PROTEIN SEQUENCE OF 14-22.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"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(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-226 AND THR-231, MASS SPECTROMETRY.
[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(2001) [PubMed: 11470436] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 45-482 IN COMPLEX WITH SUBSTRATES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X13455 Genomic DNA. Translation: CAA31804.1.
X14105 Genomic DNA. Translation: CAA32262.1.
U10399 Genomic DNA. Translation: AAB68877.1.

PIR

ZPBY. S05738.

RefSeq

NP_011889.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HR6	X-ray	2.50	A/C/E/G	14-482	[»]
1HR7	X-ray	2.55	A/C/E/G	14-482	[»]
1HR8	X-ray	2.70	A/C/E/G	14-482	[»]
1HR9	X-ray	3.01	A/C/E/G	14-482	[»]

SMR

P11914. Positions 14-470.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2401N.

IntAct

P11914. 9 interactions.

Protein family/group databases

MEROPS

M16.971.

Proteomic databases

PeptideAtlas

P11914.

PRIDE

P11914.

Genome annotation databases

Ensembl

YHR024C. Saccharomyces cerevisiae. [Contig view]

GeneID

856419.

GenomeReviews

Gene locus YHR024C in contig U00093_GR.

KEGG

sce:YHR024C.

NMPDR

fig|4932.3.peg.3035.

Organism-specific databases

CYGD

YHR024c.

SGD

S000001066. MAS2.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P11914.

OMA

P11914. YRGNTVG.

Enzyme and pathway databases

BRENDA

3.4.24.64. 250.

Gene expression databases

ArrayExpress

P11914.

GermOnline

YHR024C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011237. Pept_M16_core.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]

Gene3D

G3DSA:3.30.830.10. Pept_M16_core. 2 hits.

Pfam

PF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]

PROSITE

PS00143. INSULINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

981985.

Entry information

Entry name

MPPA_YEAST

Accession

Primary (citable) accession number: P11914

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	June 16, 2009
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)