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P35999

- PMIP_YEAST

UniProt

P35999 - PMIP_YEAST

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Protein

Mitochondrial intermediate peptidase

Gene
OCT1, MIP1, YKL134C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

Binds 1 zinc ion By similarity.

Enzyme regulationi

Stimulated by Fe2+.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi558 – 5581Zinc; catalytic By similarity
Active sitei559 – 5591 By similarity
Metal bindingi562 – 5621Zinc; catalytic By similarity
Metal bindingi565 – 5651Zinc; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: SGD

GO - Biological processi

  1. cellular iron ion homeostasis Source: SGD
  2. protein processing involved in protein targeting to mitochondrion Source: SGD
  3. protein stabilization Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YKL134C-MONOMER.

Protein family/group databases

MEROPSiM03.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial intermediate peptidase (EC:3.4.24.59)
Short name:
MIP
Gene namesi
Name:OCT1
Synonyms:MIP1
Ordered Locus Names:YKL134C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

SGDiS000001617. OCT1.

Subcellular locationi

Mitochondrion matrix 3 Publications

GO - Cellular componenti

  1. mitochondrial matrix Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311C → S or V: Affects protein stability, but has no effect on peptidase activity. 1 Publication
Mutagenesisi557 – 5571F → R: Affects protein stability. 1 Publication
Mutagenesisi558 – 5581H → R: Abolishes proteolytic activity. 1 Publication
Mutagenesisi559 – 5591E → D: Abolishes proteolytic activity. 1 Publication
Mutagenesisi561 – 5611G → L: Affects protein stability. 1 Publication
Mutagenesisi562 – 5621H → R: Abolishes proteolytic activity. 1 Publication
Mutagenesisi565 – 5651H → R: Temperature sensitive; abolishes proteolytic activity for RIP1, but not for COX4. 1 Publication
Mutagenesisi578 – 5781G → L: Temperature sensitive; abolishes proteolytic activity for RIP1, but not for COX4. 1 Publication
Mutagenesisi581 – 5811C → S or V: Affects protein stability, but has no effect on peptidase activity. 1 Publication
Mutagenesisi584 – 5841D → E: No effect. 1 Publication
Mutagenesisi587 – 5871E → D: Abolishes proteolytic activity. 1 Publication
Mutagenesisi589 – 5891P → L: No effect. 1 Publication
Mutagenesisi590 – 5901S → Y: Affects protein stability. 1 Publication
Mutagenesisi594 – 5941E → D: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737Mitochondrion Reviewed predictionAdd
BLAST
Chaini38 – 772735Mitochondrial intermediate peptidasePRO_0000028583Add
BLAST

Proteomic databases

MaxQBiP35999.
PaxDbiP35999.
PRIDEiP35999.

Expressioni

Gene expression databases

GenevestigatoriP35999.

Interactioni

Protein-protein interaction databases

BioGridi34002. 60 interactions.
DIPiDIP-2670N.
IntActiP35999. 1 interaction.
MINTiMINT-497669.
STRINGi4932.YKL134C.

Structurei

3D structure databases

ProteinModelPortaliP35999.
SMRiP35999. Positions 123-751.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
GeneTreeiENSGT00550000075047.
HOGENOMiHOG000076521.
KOiK01410.
OMAiLQVFYSA.
OrthoDBiEOG71GB4R.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35999-1 [UniParc]FASTAAdd to Basket

« Hide

MLRTIILKAG SNASIPSPSR QNKLLRFFAT AGAVSRTSPG SIKKIFDDNS    50
YWRNINGQDA NNSKISQYLF KKNKTGLFKN PYLTSPDGLR KFSQVSLQQA 100
QELLDKMRND FSESGKLTYI MNLDRLSDTL CRVIDLCEFI RSTHPDDAFV 150
RAAQDCHEQM FEFMNVLNTD VSLCNILKSV LNNPEVSSKL SAEELKVGKI 200
LLDDFEKSGI YMNPDVREKF IQLSQEISLV GQEFINHTDY PGSNSVKIPC 250
KDLDNSKVST FLLKQLNKDV KGQNYKVPTF GYAAYALLKS CENEMVRKKL 300
WTALHSCSDK QVKRLSHLIK LRAILANLMH KTSYAEYQLE GKMAKNPKDV 350
QDFILTLMNN TIEKTANELK FIAELKAKDL KKPLTTNTDE ILKLVRPWDR 400
DYYTGKYFQL NPSNSPNAKE ISYYFTLGNV IQGLSDLFQQ IYGIRLEPAI 450
TDEGETWSPD VRRLNVISEE EGIIGIIYCD LFERNGKTSN PAHFTVCCSR 500
QIYPSETDFS TIQVGENPDG TYFQLPVISL VCNFSPILIA SKKSLCFLQL 550
SEVETLFHEM GHAMHSMLGR THMQNISGTR CATDFVELPS ILMEHFAKDI 600
RILTKIGKHY GTGETIQADM LQRFMKSTNF LQNCETYSQA KMAMLDQSFH 650
DEKIISDIDN FDVVENYQAL ERRLKVLVDD QSNWCGRFGH LFGYGATYYS 700
YLFDRTIASK IWYALFEDDP YSRKNGDKFK KHLLKWGGLK DPWKCIADVL 750
ECPMLEKGGS DAMEFIAQSH KS 772
Length:772
Mass (Da):88,183
Last modified:November 1, 1997 - v2
Checksum:i1C19A0655FAAE7CA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti343 – 3508MAKNPKDV → WQDRRC in CAA81975. 1 Publication
Sequence conflicti694 – 7029YGATYYSYL → SGQLITATY in CAA81975. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U10243 Genomic DNA. Translation: AAA21278.1.
Z28134 Genomic DNA. Translation: CAA81975.1.
BK006944 Genomic DNA. Translation: DAA09028.2.
PIRiS37963.
RefSeqiNP_012788.2. NM_001179700.2.

Genome annotation databases

EnsemblFungiiYKL134C; YKL134C; YKL134C.
GeneIDi853724.
KEGGisce:YKL134C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U10243 Genomic DNA. Translation: AAA21278.1 .
Z28134 Genomic DNA. Translation: CAA81975.1 .
BK006944 Genomic DNA. Translation: DAA09028.2 .
PIRi S37963.
RefSeqi NP_012788.2. NM_001179700.2.

3D structure databases

ProteinModelPortali P35999.
SMRi P35999. Positions 123-751.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34002. 60 interactions.
DIPi DIP-2670N.
IntActi P35999. 1 interaction.
MINTi MINT-497669.
STRINGi 4932.YKL134C.

Protein family/group databases

MEROPSi M03.006.

Proteomic databases

MaxQBi P35999.
PaxDbi P35999.
PRIDEi P35999.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKL134C ; YKL134C ; YKL134C .
GeneIDi 853724.
KEGGi sce:YKL134C.

Organism-specific databases

SGDi S000001617. OCT1.

Phylogenomic databases

eggNOGi COG0339.
GeneTreei ENSGT00550000075047.
HOGENOMi HOG000076521.
KOi K01410.
OMAi LQVFYSA.
OrthoDBi EOG71GB4R.

Enzyme and pathway databases

BioCyci YEAST:YKL134C-MONOMER.

Miscellaneous databases

NextBioi 974752.
PROi P35999.

Gene expression databases

Genevestigatori P35999.

Family and domain databases

Gene3Di 1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view ]
Pfami PF01432. Peptidase_M3. 1 hit.
[Graphical view ]
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. 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].

Entry informationi

Entry nameiPMIP_YEAST
AccessioniPrimary (citable) accession number: P35999
Secondary accession number(s): D6VX62, P51980
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3

Similar proteinsi