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P35999 (PMIP_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 123. 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 intermediate peptidase

Short name=MIP
EC=3.4.24.59
Gene names
Name:OCT1
Synonyms:MIP1
Ordered Locus Names:YKL134C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length772 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane. Cleaves precursor proteins of respiratory components, including subunits of the electron transport chain and tricarboxylic acid cycle enzymes, and components of the mitochondrial genetic machinery, including ribosomal proteins, translation factors, and proteins required for mitochondrial DNA metabolism. Ref.1 Ref.4

Catalytic activity

Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.

Cofactor

Binds 1 zinc ion By similarity.

Enzyme regulation

Stimulated by Fe2+. Ref.6

Subcellular location

Mitochondrion matrix Ref.5 Ref.7 Ref.9.

Miscellaneous

Present with 2690 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase M3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Mitochondrion Potential
Chain38 – 772735Mitochondrial intermediate peptidase
PRO_0000028583

Sites

Active site5591 By similarity
Metal binding5581Zinc; catalytic By similarity
Metal binding5621Zinc; catalytic By similarity
Metal binding5651Zinc; catalytic By similarity

Experimental info

Mutagenesis1311C → S or V: Affects protein stability, but has no effect on peptidase activity. Ref.5
Mutagenesis5571F → R: Affects protein stability. Ref.5
Mutagenesis5581H → R: Abolishes proteolytic activity. Ref.5
Mutagenesis5591E → D: Abolishes proteolytic activity. Ref.5
Mutagenesis5611G → L: Affects protein stability. Ref.5
Mutagenesis5621H → R: Abolishes proteolytic activity. Ref.5
Mutagenesis5651H → R: Temperature sensitive; abolishes proteolytic activity for RIP1, but not for COX4. Ref.5
Mutagenesis5781G → L: Temperature sensitive; abolishes proteolytic activity for RIP1, but not for COX4. Ref.5
Mutagenesis5811C → S or V: Affects protein stability, but has no effect on peptidase activity. Ref.5
Mutagenesis5841D → E: No effect. Ref.5
Mutagenesis5871E → D: Abolishes proteolytic activity. Ref.5
Mutagenesis5891P → L: No effect. Ref.5
Mutagenesis5901S → Y: Affects protein stability. Ref.5
Mutagenesis5941E → D: No effect. Ref.5
Sequence conflict343 – 3508MAKNPKDV → WQDRRC in CAA81975. Ref.2
Sequence conflict694 – 7029YGATYYSYL → SGQLITATY in CAA81975. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P35999 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 1C19A0655FAAE7CA

FASTA77288,183
        10         20         30         40         50         60 
MLRTIILKAG SNASIPSPSR QNKLLRFFAT AGAVSRTSPG SIKKIFDDNS YWRNINGQDA 

        70         80         90        100        110        120 
NNSKISQYLF KKNKTGLFKN PYLTSPDGLR KFSQVSLQQA QELLDKMRND FSESGKLTYI 

       130        140        150        160        170        180 
MNLDRLSDTL CRVIDLCEFI RSTHPDDAFV RAAQDCHEQM FEFMNVLNTD VSLCNILKSV 

       190        200        210        220        230        240 
LNNPEVSSKL SAEELKVGKI LLDDFEKSGI YMNPDVREKF IQLSQEISLV GQEFINHTDY 

       250        260        270        280        290        300 
PGSNSVKIPC KDLDNSKVST FLLKQLNKDV KGQNYKVPTF GYAAYALLKS CENEMVRKKL 

       310        320        330        340        350        360 
WTALHSCSDK QVKRLSHLIK LRAILANLMH KTSYAEYQLE GKMAKNPKDV QDFILTLMNN 

       370        380        390        400        410        420 
TIEKTANELK FIAELKAKDL KKPLTTNTDE ILKLVRPWDR DYYTGKYFQL NPSNSPNAKE 

       430        440        450        460        470        480 
ISYYFTLGNV IQGLSDLFQQ IYGIRLEPAI TDEGETWSPD VRRLNVISEE EGIIGIIYCD 

       490        500        510        520        530        540 
LFERNGKTSN PAHFTVCCSR QIYPSETDFS TIQVGENPDG TYFQLPVISL VCNFSPILIA 

       550        560        570        580        590        600 
SKKSLCFLQL SEVETLFHEM GHAMHSMLGR THMQNISGTR CATDFVELPS ILMEHFAKDI 

       610        620        630        640        650        660 
RILTKIGKHY GTGETIQADM LQRFMKSTNF LQNCETYSQA KMAMLDQSFH DEKIISDIDN 

       670        680        690        700        710        720 
FDVVENYQAL ERRLKVLVDD QSNWCGRFGH LFGYGATYYS YLFDRTIASK IWYALFEDDP 

       730        740        750        760        770 
YSRKNGDKFK KHLLKWGGLK DPWKCIADVL ECPMLEKGGS DAMEFIAQSH KS 

« Hide

References

« Hide 'large scale' references
[1]"MIP1, a new yeast gene homologous to the rat mitochondrial intermediate peptidase gene, is required for oxidative metabolism in Saccharomyces cerevisiae."
Isaya G., Miklos D., Rollins R.A.
Mol. Cell. Biol. 14:5603-5616(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 343-350 AND 694-702.
Strain: ATCC 204508 / S288c.
[4]"Prediction and identification of new natural substrates of the yeast mitochondrial intermediate peptidase."
Branda S.S., Isaya G.
J. Biol. Chem. 270:27366-27373(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Mutations in a putative zinc-binding domain inactivate the mitochondrial intermediate peptidase."
Chew A., Rollins R.A., Sakati W.R., Isaya G.
Biochem. Biophys. Res. Commun. 226:822-829(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-131; PHE-557; HIS-558; GLE-559; GLY-561; HIS-562; HIS-565; GLY-578; CYS-581; ASP-584; GLU-587; PRO-589; SER-590 AND GLU-594, SUBCELLULAR LOCATION.
[6]"Mitochondrial intermediate peptidase and the yeast frataxin homolog together maintain mitochondrial iron homeostasis in Saccharomyces cerevisiae."
Branda S.S., Yang Z.Y., Chew A., Isaya G.
Hum. Mol. Genet. 8:1099-1110(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10243 Genomic DNA. Translation: AAA21278.1.
Z28134 Genomic DNA. Translation: CAA81975.1.
BK006944 Genomic DNA. Translation: DAA09028.2.
PIRS37963.
RefSeqNP_012788.2. NM_001179700.2.

3D structure databases

ProteinModelPortalP35999.
SMRP35999. Positions 71-767.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34002. 60 interactions.
DIPDIP-2670N.
IntActP35999. 1 interaction.
MINTMINT-497669.
STRING4932.YKL134C.

Protein family/group databases

MEROPSM03.006.

Proteomic databases

PaxDbP35999.
PRIDEP35999.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL134C; YKL134C; YKL134C.
GeneID853724.
KEGGsce:YKL134C.

Organism-specific databases

SGDS000001617. OCT1.

Phylogenomic databases

eggNOGCOG0339.
GeneTreeENSGT00550000075047.
HOGENOMHOG000076521.
KOK01410.
OMALQVFYSA.
OrthoDBEOG71GB4R.

Enzyme and pathway databases

BioCycYEAST:YKL134C-MONOMER.

Gene expression databases

GenevestigatorP35999.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio974752.
PROP35999.

Entry information

Entry namePMIP_YEAST
AccessionPrimary (citable) accession number: P35999
Secondary accession number(s): D6VX62, P51980
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: 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