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Protein

Mitochondrial inner membrane protease subunit 2

Gene

IMP2

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

Catalytic component of the mitochondrial inner membrane peptidase (IMP) complex. IMP catalyzes the removal of signal peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. The two catalytic IMP subunits seem to have non-overlapping substrate specificities. IMP2 substrates include nuclear encoded CYB2, mitochondrially encoded COX2 and cytochrome c1. Required for the stability of IMP1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei41 – 411By similarity
Active sitei91 – 911By similarity

GO - Molecular functioni

  • endopeptidase activity Source: SGD
  • serine-type peptidase activity Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protease

Enzyme and pathway databases

BioCyciYEAST:G3O-32740-MONOMER.

Protein family/group databases

MEROPSiS26.012.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial inner membrane protease subunit 2 (EC:3.4.21.-)
Gene namesi
Name:IMP2
Ordered Locus Names:YMR035W
ORF Names:YM9973.09
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR035W.
SGDiS000004638. IMP2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei134 – 15219HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411S → A or T: Abolishes enzymatic activity. 1 Publication
Mutagenesisi91 – 911K → H or R: Abolishes enzymatic activity. 1 Publication
Mutagenesisi95 – 951G → D: Reduces processing of CYB2 and presence of IMP1 and SOM1 in the IMP complex. 1 Publication
Mutagenesisi123 – 1231G → S: Reduces processing of cytochrome c1; no effect on presence of IMP1 and SOM1 in the IMP complex. 1 Publication
Mutagenesisi124 – 1241D → N or Y: Abolishes enzymatic activity. 1 Publication
Mutagenesisi131 – 1311D → N or E: Abolishes enzymatic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 177177Mitochondrial inner membrane protease subunit 2PRO_0000109538Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

MaxQBiP46972.

Interactioni

Subunit structurei

Component of the mitochondrial inner membrane peptidase (IMP) complex which at least consists of IMP1, IMP2 and SOM1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MDM30Q059302EBI-9231,EBI-31799

Protein-protein interaction databases

BioGridi35207. 41 interactions.
DIPiDIP-1941N.
IntActiP46972. 3 interactions.
MINTiMINT-391123.

Structurei

3D structure databases

ProteinModelPortaliP46972.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S26 family. IMP2 subfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00550000075044.
HOGENOMiHOG000003673.
InParanoidiP46972.
KOiK09648.
OMAiVLLEKFC.
OrthoDBiEOG7H4F5X.

Family and domain databases

Gene3Di2.10.109.10. 1 hit.
InterProiIPR000223. Pept_S26A_signal_pept_1.
IPR019758. Pept_S26A_signal_pept_1_CS.
IPR019756. Pept_S26A_signal_pept_1_Ser-AS.
IPR028360. Peptidase_S24/S26_b-rbn.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
[Graphical view]
PANTHERiPTHR12383. PTHR12383. 1 hit.
PfamiPF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSiPR00727. LEADERPTASE.
SUPFAMiSSF51306. SSF51306. 1 hit.
PROSITEiPS00501. SPASE_I_1. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRAGSSKRF LRNTLIAISW VPVLLTINNN VVHIAQVKGT SMQPTLNPQT
60 70 80 90 100
ETLATDWVLL WKFGVKNPSN LSRDDIILFK APTNPRKVYC KRVKGLPFDT
110 120 130 140 150
IDTKFPYPKP QVNLPRGHIW VEGDNYFHSI DSNTFGPISS GLVIGKAITI
160 170
VWPPSRWGTD LKLSTGRDCI SKRAILE
Length:177
Mass (Da):19,930
Last modified:November 1, 1995 - v1
Checksum:i2335F334D8E9A552
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49213 Genomic DNA. Translation: CAA89151.1.
AY692994 Genomic DNA. Translation: AAT93013.1.
BK006946 Genomic DNA. Translation: DAA09934.1.
PIRiS53952.
RefSeqiNP_013749.1. NM_001182532.1.

Genome annotation databases

EnsemblFungiiYMR035W; YMR035W; YMR035W.
GeneIDi855051.
KEGGisce:YMR035W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49213 Genomic DNA. Translation: CAA89151.1.
AY692994 Genomic DNA. Translation: AAT93013.1.
BK006946 Genomic DNA. Translation: DAA09934.1.
PIRiS53952.
RefSeqiNP_013749.1. NM_001182532.1.

3D structure databases

ProteinModelPortaliP46972.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35207. 41 interactions.
DIPiDIP-1941N.
IntActiP46972. 3 interactions.
MINTiMINT-391123.

Protein family/group databases

MEROPSiS26.012.

Proteomic databases

MaxQBiP46972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR035W; YMR035W; YMR035W.
GeneIDi855051.
KEGGisce:YMR035W.

Organism-specific databases

EuPathDBiFungiDB:YMR035W.
SGDiS000004638. IMP2.

Phylogenomic databases

GeneTreeiENSGT00550000075044.
HOGENOMiHOG000003673.
InParanoidiP46972.
KOiK09648.
OMAiVLLEKFC.
OrthoDBiEOG7H4F5X.

Enzyme and pathway databases

BioCyciYEAST:G3O-32740-MONOMER.

Miscellaneous databases

PROiP46972.

Family and domain databases

Gene3Di2.10.109.10. 1 hit.
InterProiIPR000223. Pept_S26A_signal_pept_1.
IPR019758. Pept_S26A_signal_pept_1_CS.
IPR019756. Pept_S26A_signal_pept_1_Ser-AS.
IPR028360. Peptidase_S24/S26_b-rbn.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
[Graphical view]
PANTHERiPTHR12383. PTHR12383. 1 hit.
PfamiPF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSiPR00727. LEADERPTASE.
SUPFAMiSSF51306. SSF51306. 1 hit.
PROSITEiPS00501. SPASE_I_1. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A mitochondrial protease with two catalytic subunits of nonoverlapping specificities."
    Nunnari J., Fox T.D., Walter P.
    Science 262:1997-2004(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. 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. "Purified inner membrane protease I of yeast mitochondria is a heterodimer."
    Schneider A., Oppliger W., Jenoe P.
    J. Biol. Chem. 269:8635-8638(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 51-62, SUBUNIT.
  6. "Signal peptides having standard and nonstandard cleavage sites can be processed by Imp1p of the mitochondrial inner membrane protease."
    Chen X., Van Valkenburgh C., Fang H., Green N.
    J. Biol. Chem. 274:37750-37754(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-41; LYS-91; ASP-124 AND ASP-131.
  7. "The mitochondrial IMP peptidase of yeast: functional analysis of domains and identification of Gut2 as a new natural substrate."
    Esser K., Jan P.S., Pratje E., Michaelis G.
    Mol. Genet. Genomics 271:616-626(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-95 AND GLY-123.

Entry informationi

Entry nameiIMP2_YEAST
AccessioniPrimary (citable) accession number: P46972
Secondary accession number(s): D6VZL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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