MPPA_YEAST
ID MPPA_YEAST Reviewed; 482 AA.
AC P11914; D3DKX1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Mitochondrial-processing peptidase subunit alpha {ECO:0000303|PubMed:9299349};
DE AltName: Full=Alpha-MPP;
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000305};
DE AltName: Full=Matrix processing peptidase {ECO:0000303|PubMed:3061797};
DE Short=MPP;
DE AltName: Full=Mitochondrial assembly protein 2 {ECO:0000303|PubMed:3061808};
DE AltName: Full=Mitochondrial import function protein 2 {ECO:0000303|PubMed:3061797};
DE Flags: Precursor;
GN Name=MAS2 {ECO:0000303|PubMed:3061808};
GN Synonyms=MIF2 {ECO:0000303|PubMed:3061797};
GN OrderedLocusNames=YHR024C {ECO:0000312|SGD:S000001066};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MC3;
RX PubMed=3061797; DOI=10.1002/j.1460-2075.1988.tb03225.x;
RA Pollock R.A., Hartl F.-U., Cheng M.Y., Ostermann J., Horwich A.,
RA Neupert W.;
RT "The processing peptidase of yeast mitochondria: the two co-operating
RT components MPP and PEP are structurally related.";
RL EMBO J. 7:3493-3500(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3061808; DOI=10.1002/j.1460-2075.1988.tb03272.x;
RA Jensen R.E., Yaffe M.P.;
RT "Import of proteins into yeast mitochondria: the nuclear MAS2 gene encodes
RT a component of the processing protease that is homologous to the MAS1-
RT encoded subunit.";
RL EMBO J. 7:3863-3871(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PROTEIN SEQUENCE OF 14-22, AND SUBCELLULAR LOCATION.
RX PubMed=2007593; DOI=10.1016/s0021-9258(18)38134-1;
RA Yang M., Geli V., Oppliger W., Suda K., James P., Schatz G.;
RT "The MAS-encoded processing protease of yeast mitochondria. Interaction of
RT the purified enzyme with signal peptides and a purified precursor
RT protein.";
RL J. Biol. Chem. 266:6416-6423(1991).
RN [6]
RP FUNCTION, AND INTERACTION WITH MAS1.
RX PubMed=9299349; DOI=10.1006/jmbi.1997.1231;
RA Luciano P., Geoffroy S., Brandt A., Hernandez J.F., Geli V.;
RT "Functional cooperation of the mitochondrial processing peptidase
RT subunits.";
RL J. Mol. Biol. 272:213-225(1997).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 45-482 IN COMPLEX WITH MAS1 AND
RP SUBSTRATES.
RX PubMed=11470436; DOI=10.1016/s0969-2126(01)00621-9;
RA Taylor A.B., Smith B.S., Kitada S., Kojima K., Miyaura H., Otwinowski Z.,
RA Ito A., Deisenhofer J.;
RT "Crystal structures of mitochondrial processing peptidase reveal the mode
RT for specific cleavage of import signal sequences.";
RL Structure 9:615-625(2001).
CC -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC mitochondrial processing protease (MPP), which cleaves the
CC mitochondrial sequence off newly imported precursors proteins.
CC {ECO:0000269|PubMed:9299349}.
CC -!- SUBUNIT: Heterodimer of MAS2 (alpha) and MAS1 (beta) subunits, forming
CC the mitochondrial processing protease (MPP) in which MAS2 is involved
CC in substrate recognition and binding and MAS1 is the catalytic subunit.
CC {ECO:0000269|PubMed:11470436, ECO:0000269|PubMed:9299349}.
CC -!- INTERACTION:
CC P11914; P10507: MAS1; NbExp=4; IntAct=EBI-11205, EBI-11212;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:2007593}.
CC -!- MISCELLANEOUS: Present with 31400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the catalytic subunit
CC (PubMed:3061797). The low processing activity which was previously
CC observed with alpha-MPP which has been purified from a mitochondrial
CC extract is most likely due to contamination by the beta-subunit. Does
CC not seem to have a protease activity as it lack the zinc-binding site
CC (PubMed:9299349). {ECO:0000305, ECO:0000305|PubMed:3061797,
CC ECO:0000305|PubMed:9299349}.
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DR EMBL; X13455; CAA31804.1; -; Genomic_DNA.
DR EMBL; X14105; CAA32262.1; -; Genomic_DNA.
DR EMBL; U10399; AAB68877.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06715.1; -; Genomic_DNA.
DR PIR; S05738; ZPBY.
DR RefSeq; NP_011889.1; NM_001179154.1.
DR PDB; 1HR6; X-ray; 2.50 A; A/C/E/G=14-482.
DR PDB; 1HR7; X-ray; 2.55 A; A/C/E/G=14-482.
DR PDB; 1HR8; X-ray; 2.70 A; A/C/E/G=14-482.
DR PDB; 1HR9; X-ray; 3.01 A; A/C/E/G=14-482.
DR PDBsum; 1HR6; -.
DR PDBsum; 1HR7; -.
DR PDBsum; 1HR8; -.
DR PDBsum; 1HR9; -.
DR AlphaFoldDB; P11914; -.
DR SMR; P11914; -.
DR BioGRID; 36455; 280.
DR ComplexPortal; CPX-1630; Mitochondrial processing peptidase complex.
DR DIP; DIP-2401N; -.
DR IntAct; P11914; 8.
DR MINT; P11914; -.
DR STRING; 4932.YHR024C; -.
DR iPTMnet; P11914; -.
DR MaxQB; P11914; -.
DR PaxDb; P11914; -.
DR PRIDE; P11914; -.
DR EnsemblFungi; YHR024C_mRNA; YHR024C; YHR024C.
DR GeneID; 856419; -.
DR KEGG; sce:YHR024C; -.
DR SGD; S000001066; MAS2.
DR VEuPathDB; FungiDB:YHR024C; -.
DR eggNOG; KOG2067; Eukaryota.
DR GeneTree; ENSGT00940000156724; -.
DR HOGENOM; CLU_009902_5_2_1; -.
DR InParanoid; P11914; -.
DR OMA; LKYHHSP; -.
DR BioCyc; MetaCyc:G3O-31085-MON; -.
DR BioCyc; YEAST:G3O-31085-MON; -.
DR BRENDA; 3.4.24.64; 984.
DR Reactome; R-SCE-611105; Respiratory electron transport.
DR SABIO-RK; P11914; -.
DR EvolutionaryTrace; P11914; -.
DR PRO; PR:P11914; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P11914; protein.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0017087; C:mitochondrial processing peptidase complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0061133; F:endopeptidase activator activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IDA:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2007593"
FT CHAIN 14..482
FT /note="Mitochondrial-processing peptidase subunit alpha"
FT /id="PRO_0000026773"
FT CONFLICT 235
FT /note="A -> P (in Ref. 2; CAA32262)"
FT /evidence="ECO:0000305"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:1HR8"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:1HR6"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1HR6"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1HR6"
FT TURN 54..59
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:1HR6"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1HR6"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1HR7"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:1HR6"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1HR6"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 129..146
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:1HR6"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1HR6"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 209..220
FT /evidence="ECO:0007829|PDB:1HR6"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:1HR6"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:1HR6"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:1HR6"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:1HR6"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:1HR6"
FT STRAND 311..322
FT /evidence="ECO:0007829|PDB:1HR6"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 343..352
FT /evidence="ECO:0007829|PDB:1HR6"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 364..381
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 385..399
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 405..413
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 417..428
FT /evidence="ECO:0007829|PDB:1HR6"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:1HR6"
FT HELIX 456..462
FT /evidence="ECO:0007829|PDB:1HR6"
SQ SEQUENCE 482 AA; 53338 MW; 0FDCD157388A56C7 CRC64;
MLRNGVQRLY SNIARTDNFK LSSLANGLKV ATSNTPGHFS ALGLYIDAGS RFEGRNLKGC
THILDRLAFK STEHVEGRAM AETLELLGGN YQCTSSRENL MYQASVFNQD VGKMLQLMSE
TVRFPKITEQ ELQEQKLSAE YEIDEVWMKP ELVLPELLHT AAYSGETLGS PLICPRELIP
SISKYYLLDY RNKFYTPENT VAAFVGVPHE KALELTEKYL GDWQSTHPPI TKKVAQYTGG
ESCIPPAPVF GNLPELFHIQ IGFEGLPIDH PDIYALATLQ TLLGGGGSFS AGGPGKGMYS
RLYTHVLNQY YFVENCVAFN HSYSDSGIFG ISLSCIPQAA PQAVEVIAQQ MYNTFANKDL
RLTEDEVSRA KNQLKSSLLM NLESKLVELE DMGRQVLMHG RKIPVNEMIS KIEDLKPDDI
SRVAEMIFTG NVNNAGNGKG RATVVMQGDR GSFGDVENVL KAYGLGNSSS SKNDSPKKKG
WF
