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P28627 (IMP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial inner membrane protease subunit 1

EC=3.4.21.-
Gene names
Name:IMP1
Synonyms:PET2858
Ordered Locus Names:YMR150C
ORF Names:YM9375.20C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. IMP1 substrates include nuclear encoded CYB2, mitochondrially encoded COX2, NADH-cytochrome b5 reductase and GUT2. Ref.7

Subunit structure

Component of the mitochondrial inner membrane peptidase (IMP) complex which at least consists of IMP1, IMP2 and SOM1. Ref.5

Subcellular location

Mitochondrion inner membrane Probable.

Sequence similarities

Belongs to the peptidase S26 family. IMP1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 190189Mitochondrial inner membrane protease subunit 1
PRO_0000109537

Sites

Active site401 By similarity
Active site841 By similarity

Experimental info

Mutagenesis401S → A or T: Abolishes enzymatic activity. Ref.6
Mutagenesis841K → H or R: Abolishes enzymatic activity. Ref.6
Mutagenesis851R → A: Reduces enzymatic activity. Ref.6
Mutagenesis881G → D in pet ts2858; temperature-sensitive; abolishes processing of CYB2 and presence of SOM1 in the IMP complex. Ref.1 Ref.7
Mutagenesis1301G → S: Abolishes processing of CYB2 and COX2 and presence of SOM1 in the IMP complex. Ref.7
Mutagenesis1311D → E or N: Reduces enzymatic activity. Ref.6
Mutagenesis1311D → Y: Abolishes enzymatic activity. Ref.6
Mutagenesis1381D → N or E: Abolishes enzymatic activity. Ref.6
Sequence conflict1781I → V in AAS56741. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P28627 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 81B044C3B57DABB3

FASTA19021,433
        10         20         30         40         50         60 
MTVGTLPIWS KTFSYAIRSL CFLHIIHMYA YEFTETRGES MLPTLSATND YVHVLKNFQN 

        70         80         90        100        110        120 
GRGIKMGDCI VALKPTDPNH RICKRVTGMP GDLVLVDPST IVNYVGDVLV DEERFGTYIK 

       130        140        150        160        170        180 
VPEGHVWVTG DNLSHSLDSR TYNALPMGLI MGKIVAANNF DKPFWDGSIR NIWGFKWINN 

       190 
TFLDVQAKSN 

« Hide

References

« Hide 'large scale' references
[1]"Mitochondrial inner membrane protease 1 of Saccharomyces cerevisiae shows sequence similarity to the Escherichia coli leader peptidase."
Behrens M., Michaelis G., Pratje E.
Mol. Gen. Genet. 228:167-176(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-88.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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 2-16, 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-40; LYS-84; ARG-85; ASP-131 AND ASP-138.
[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-88 AND GLY-130.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S55518 Genomic DNA. Translation: AAB19704.1.
Z47071 Genomic DNA. Translation: CAA87365.1.
AY558415 Genomic DNA. Translation: AAS56741.1.
BK006946 Genomic DNA. Translation: DAA10046.1.
PIRS16817.
RefSeqNP_013870.1. NM_001182652.1.

3D structure databases

ProteinModelPortalP28627.
SMRP28627. Positions 48-159.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35326. 14 interactions.
DIPDIP-8328N.
IntActP28627. 2 interactions.
STRING4932.YMR150C.

Protein family/group databases

MEROPSS26.002.

Proteomic databases

PaxDbP28627.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR150C; YMR150C; YMR150C.
GeneID855182.
KEGGsce:YMR150C.

Organism-specific databases

SGDS000004758. IMP1.

Phylogenomic databases

eggNOGCOG0681.
GeneTreeENSGT00550000075025.
HOGENOMHOG000003673.
KOK09647.
OMAYNALPMG.
OrthoDBEOG70PC8B.

Enzyme and pathway databases

BioCycYEAST:G3O-32841-MONOMER.

Gene expression databases

GenevestigatorP28627.

Family and domain databases

Gene3D2.10.109.10. 1 hit.
InterProIPR026730. Mitochondrial_IMP1.
IPR000223. Pept_S26A_signal_pept_1.
IPR019757. Pept_S26A_signal_pept_1_Lys-AS.
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]
PANTHERPTHR12383. PTHR12383. 1 hit.
PTHR12383:SF2. PTHR12383:SF2. 1 hit.
PfamPF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSPR00727. LEADERPTASE.
SUPFAMSSF51306. SSF51306. 1 hit.
TIGRFAMsTIGR02227. sigpep_I_bact. 1 hit.
PROSITEPS00501. SPASE_I_1. 1 hit.
PS00760. SPASE_I_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio978638.
PROP28627.

Entry information

Entry nameIMP1_YEAST
AccessionPrimary (citable) accession number: P28627
Secondary accession number(s): D6VZX2, E9P8W1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries