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P35999

- PMIP_YEAST

UniProt

P35999 - PMIP_YEAST

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Protein

Mitochondrial intermediate peptidase

Gene

OCT1

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; catalyticPROSITE-ProRule annotation
Active sitei559 – 5591PROSITE-ProRule annotation
Metal bindingi562 – 5621Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi565 – 5651Zinc; catalyticPROSITE-ProRule annotation

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 – 3737MitochondrionSequence AnalysisAdd
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
GeneTreeiENSGT00550000075047.
HOGENOMiHOG000076521.
InParanoidiP35999.
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

        10         20         30         40         50
MLRTIILKAG SNASIPSPSR QNKLLRFFAT AGAVSRTSPG SIKKIFDDNS
60 70 80 90 100
YWRNINGQDA NNSKISQYLF KKNKTGLFKN PYLTSPDGLR KFSQVSLQQA
110 120 130 140 150
QELLDKMRND FSESGKLTYI MNLDRLSDTL CRVIDLCEFI RSTHPDDAFV
160 170 180 190 200
RAAQDCHEQM FEFMNVLNTD VSLCNILKSV LNNPEVSSKL SAEELKVGKI
210 220 230 240 250
LLDDFEKSGI YMNPDVREKF IQLSQEISLV GQEFINHTDY PGSNSVKIPC
260 270 280 290 300
KDLDNSKVST FLLKQLNKDV KGQNYKVPTF GYAAYALLKS CENEMVRKKL
310 320 330 340 350
WTALHSCSDK QVKRLSHLIK LRAILANLMH KTSYAEYQLE GKMAKNPKDV
360 370 380 390 400
QDFILTLMNN TIEKTANELK FIAELKAKDL KKPLTTNTDE ILKLVRPWDR
410 420 430 440 450
DYYTGKYFQL NPSNSPNAKE ISYYFTLGNV IQGLSDLFQQ IYGIRLEPAI
460 470 480 490 500
TDEGETWSPD VRRLNVISEE EGIIGIIYCD LFERNGKTSN PAHFTVCCSR
510 520 530 540 550
QIYPSETDFS TIQVGENPDG TYFQLPVISL VCNFSPILIA SKKSLCFLQL
560 570 580 590 600
SEVETLFHEM GHAMHSMLGR THMQNISGTR CATDFVELPS ILMEHFAKDI
610 620 630 640 650
RILTKIGKHY GTGETIQADM LQRFMKSTNF LQNCETYSQA KMAMLDQSFH
660 670 680 690 700
DEKIISDIDN FDVVENYQAL ERRLKVLVDD QSNWCGRFGH LFGYGATYYS
710 720 730 740 750
YLFDRTIASK IWYALFEDDP YSRKNGDKFK KHLLKWGGLK DPWKCIADVL
760 770
ECPMLEKGGS DAMEFIAQSH KS
Length:772
Mass (Da):88,183
Last modified:November 1, 1997 - v2
Checksum:i1C19A0655FAAE7CA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti343 – 3508MAKNPKDV → WQDRRC in CAA81975. (PubMed:8196765)Curated
Sequence conflicti694 – 7029YGATYYSYL → SGQLITATY in CAA81975. (PubMed:8196765)Curated

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.
InParanoidi P35999.
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: October 29, 2014
This is version 127 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.1 Publication

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