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P36775

- LONM_YEAST

UniProt

P36775 - LONM_YEAST

Protein

Lon protease homolog, mitochondrial

Gene

PIM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner. Endogenous substrates include ACO2, ILV1, ILV2, LSC1, LYS4 and several oxidized proteins.8 PublicationsUniRule annotation

    Kineticsi

    1. KM=40 µM for ATP for ATPase activity1 Publication

    pH dependencei

    Optimum pH is 7.9.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1015 – 10151UniRule annotation
    Active sitei1058 – 10581UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi632 – 6398ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. ATP-dependent peptidase activity Source: SGD
    3. sequence-specific DNA binding Source: UniProtKB-HAMAP
    4. serine-type endopeptidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular response to oxidative stress Source: UniProtKB-HAMAP
    3. chaperone-mediated protein complex assembly Source: SGD
    4. misfolded or incompletely synthesized protein catabolic process Source: SGD
    5. oxidation-dependent protein catabolic process Source: UniProtKB-HAMAP
    6. regulation of mitochondrial DNA replication Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28925-MONOMER.

    Protein family/group databases

    MEROPSiS16.010.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lon protease homolog, mitochondrialUniRule annotation (EC:3.4.21.-UniRule annotation)
    Gene namesi
    Name:PIM1UniRule annotation
    Synonyms:LON
    Ordered Locus Names:YBL022C
    ORF Names:YBL0440
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBL022c.
    SGDiS000000118. PIM1.

    Subcellular locationi

    Mitochondrion matrix 3 PublicationsUniRule annotation

    GO - Cellular componenti

    1. mitochondrial matrix Source: SGD

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi638 – 6381K → N: Abolishes ATP-binding. 2 Publications
    Mutagenesisi1015 – 10151S → A: Abolishes peptidase activity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3737MitochondrionUniRule annotationAdd
    BLAST
    Propeptidei38 – 9861Removed in mature form; by autocatalysis2 PublicationsUniRule annotationPRO_0000395761Add
    BLAST
    Chaini99 – 11331035Lon protease homolog, mitochondrialPRO_0000026733Add
    BLAST

    Proteomic databases

    MaxQBiP36775.
    PaxDbiP36775.
    PeptideAtlasiP36775.

    Expressioni

    Gene expression databases

    GenevestigatoriP36775.

    Interactioni

    Subunit structurei

    Homoheptamer. Organized in a ring with a central cavity. Oligomerization is independent of its proteolytic activity and the autocatalytic maturation of its subunits.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi32676. 71 interactions.
    DIPiDIP-6629N.
    IntActiP36775. 13 interactions.
    MINTiMINT-626645.

    Structurei

    3D structure databases

    ProteinModelPortaliP36775.
    SMRiP36775. Positions 391-518, 527-1109.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini183 – 478296LonUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S16 family.UniRule annotation
    Contains 1 Lon domain.UniRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0466.
    GeneTreeiENSGT00530000063553.
    HOGENOMiHOG000261409.
    KOiK08675.
    OMAiKISHENY.
    OrthoDBiEOG7327X6.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_03120. lonm_euk.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR004815. Lon_bac/euk-typ.
    IPR027065. Lon_Prtase.
    IPR027503. Lonm_euk.
    IPR027417. P-loop_NTPase.
    IPR008269. Pept_S16_C.
    IPR003111. Pept_S16_N.
    IPR008268. Peptidase_S16_AS.
    IPR015947. PUA-like_domain.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    [Graphical view]
    PANTHERiPTHR10046. PTHR10046. 1 hit.
    PfamiPF00004. AAA. 1 hit.
    PF02190. LON. 1 hit.
    PF05362. Lon_C. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00464. LON. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF88697. SSF88697. 1 hit.
    TIGRFAMsiTIGR00763. lon. 1 hit.
    PROSITEiPS01046. LON_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P36775-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRTRTTKTL STVARTTRAI QYYRSIAKTA AVSQRRFAST LTVRDVENIK     50
    PSHIIKSPTW QEFQHQLKDP RYMEHFAQLD AQFARHFMAT NSGKSILAKD 100
    DSTSQKKDED VKIVPDEKDT DNDVEPTRDD EIVNKDQEGE ASKNSRSSAS 150
    GGGQSSSSRS DSGDGSSKQK PPKDVPEVYP QMLALPIARR PLFPGFYKAV 200
    VISDERVMKA IKEMLDRQQP YIGAFMLKNS EEDTDVITDK NDVYDVGVLA 250
    QITSAFPSKD EKTGTETMTA LLYPHRRIKI DELFPPNEEK EKSKEQAKDT 300
    DTETTVVEDA NNPEDQESTS PATPKLEDIV VERIPDSELQ HHKRVEATEE 350
    ESEELDDIQE GEDINPTEFL KNYNVSLVNV LNLEDEPFDR KSPVINALTS 400
    EILKVFKEIS QLNTMFREQI ATFSASIQSA TTNIFEEPAR LADFAAAVSA 450
    GEEDELQDIL SSLNIEHRLE KSLLVLKKEL MNAELQNKIS KDVETKIQKR 500
    QREYYLMEQL KGIKRELGID DGRDKLIDTY KERIKSLKLP DSVQKIFDDE 550
    ITKLSTLETS MSEFGVIRNY LDWLTSIPWG KHSKEQYSIP RAKKILDEDH 600
    YGMVDVKDRI LEFIAVGKLL GKVDGKIICF VGPPGVGKTS IGKSIARALN 650
    RKFFRFSVGG MTDVAEIKGH RRTYIGALPG RVVQALKKCQ TQNPLILIDE 700
    IDKIGHGGIH GDPSAALLEV LDPEQNNSFL DNYLDIPIDL SKVLFVCTAN 750
    SLETIPRPLL DRMEVIELTG YVAEDKVKIA EQYLVPSAKK SAGLENSHVD 800
    MTEDAITALM KYYCRESGVR NLKKHIEKIY RKAALQVVKK LSIEDSPTSS 850
    ADSKPKESVS SEEKAENNAK SSSEKTKDNN SEKTSDDIEA LKTSEKINVS 900
    ISQKNLKDYV GPPVYTTDRL YETTPPGVVM GLAWTNMGGC SLYVESVLEQ 950
    PLHNCKHPTF ERTGQLGDVM KESSRLAYSF AKMYLAQKFP ENRFFEKASI 1000
    HLHCPEGATP KDGPSAGVTM ATSFLSLALN KSIDPTVAMT GELTLTGKVL 1050
    RIGGLREKAV AAKRSGAKTI IFPKDNLNDW EELPDNVKEG LEPLAADWYN 1100
    DIFQKLFKDV NTKEGNSVWK AEFEILDAKK EKD 1133
    Length:1,133
    Mass (Da):127,112
    Last modified:October 1, 1994 - v2
    Checksum:i281CAB94579FFF09
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti509 – 5091Q → R in AAA53625. (PubMed:8146662)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74544 Genomic DNA. Translation: CAA52634.1.
    L28110 mRNA. Translation: AAA53625.1.
    Z35783 Genomic DNA. Translation: CAA84841.1.
    M20318 Genomic DNA. Translation: AAA53539.1.
    BK006936 Genomic DNA. Translation: DAA07098.1.
    PIRiS43938.
    RefSeqiNP_009531.1. NM_001178262.1.

    Genome annotation databases

    EnsemblFungiiYBL022C; YBL022C; YBL022C.
    GeneIDi852259.
    KEGGisce:YBL022C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74544 Genomic DNA. Translation: CAA52634.1 .
    L28110 mRNA. Translation: AAA53625.1 .
    Z35783 Genomic DNA. Translation: CAA84841.1 .
    M20318 Genomic DNA. Translation: AAA53539.1 .
    BK006936 Genomic DNA. Translation: DAA07098.1 .
    PIRi S43938.
    RefSeqi NP_009531.1. NM_001178262.1.

    3D structure databases

    ProteinModelPortali P36775.
    SMRi P36775. Positions 391-518, 527-1109.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32676. 71 interactions.
    DIPi DIP-6629N.
    IntActi P36775. 13 interactions.
    MINTi MINT-626645.

    Protein family/group databases

    MEROPSi S16.010.

    Proteomic databases

    MaxQBi P36775.
    PaxDbi P36775.
    PeptideAtlasi P36775.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBL022C ; YBL022C ; YBL022C .
    GeneIDi 852259.
    KEGGi sce:YBL022C.

    Organism-specific databases

    CYGDi YBL022c.
    SGDi S000000118. PIM1.

    Phylogenomic databases

    eggNOGi COG0466.
    GeneTreei ENSGT00530000063553.
    HOGENOMi HOG000261409.
    KOi K08675.
    OMAi KISHENY.
    OrthoDBi EOG7327X6.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28925-MONOMER.

    Miscellaneous databases

    NextBioi 970847.
    PROi P36775.

    Gene expression databases

    Genevestigatori P36775.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPi MF_03120. lonm_euk.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR004815. Lon_bac/euk-typ.
    IPR027065. Lon_Prtase.
    IPR027503. Lonm_euk.
    IPR027417. P-loop_NTPase.
    IPR008269. Pept_S16_C.
    IPR003111. Pept_S16_N.
    IPR008268. Peptidase_S16_AS.
    IPR015947. PUA-like_domain.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    [Graphical view ]
    PANTHERi PTHR10046. PTHR10046. 1 hit.
    Pfami PF00004. AAA. 1 hit.
    PF02190. LON. 1 hit.
    PF05362. Lon_C. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    SM00464. LON. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF88697. SSF88697. 1 hit.
    TIGRFAMsi TIGR00763. lon. 1 hit.
    PROSITEi PS01046. LON_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae."
      van Dyck L., Pearce D.A., Sherman F.
      J. Biol. Chem. 269:238-242(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: ATCC 204508 / S288c.
    2. "Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration."
      Suzuki C.K., Suda K., Wang N., Schatz G.
      Science 264:273-276(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    3. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "The HAP3 regulatory locus of Saccharomyces cerevisiae encodes divergent overlapping transcripts."
      Hahn S., Pinkham J., Wei R., Miller R., Guarente L.
      Mol. Cell. Biol. 8:655-663(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-216.
      Strain: ATCC MYA-3516 / BWG1-7A.
    6. "Autocatalytic processing of the ATP-dependent PIM1 protease: crucial function of a pro-region for sorting to mitochondria."
      Wagner I., van Dyck L., Savel'ev A.S., Neupert W., Langer T.
      EMBO J. 16:7317-7325(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, MUTAGENESIS OF LYS-638 AND SER-1015, AUTOCATALYTIC PROCESSING, SUBCELLULAR LOCATION.
    7. "The ATPase and protease domains of yeast mitochondrial Lon: roles in proteolysis and respiration-dependent growth."
      van Dijl J.M., Kutejova E., Suda K., Perecko D., Schatz G., Suzuki C.K.
      Proc. Natl. Acad. Sci. U.S.A. 95:10584-10589(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBUNIT.
    8. "Yeast mitochondrial ATP-dependent protease: purification and comparison with the homologous rat enzyme and the bacterial ATP-dependent protease La."
      Kutejova E., Durcova G., Surovkova E., Kuzela S.
      FEBS Lett. 329:47-50(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon."
      Rep M., van Dijl J.M., Suda K., Schatz G., Grivell L.A., Suzuki C.K.
      Science 274:103-106(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-638 AND SER-1015.
    10. "Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits."
      Stahlberg H., Kutejova E., Suda K., Wolpensinger B., Lustig A., Schatz G., Engel A., Suzuki C.K.
      Proc. Natl. Acad. Sci. U.S.A. 96:6787-6790(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. "Cleavage site selection within a folded substrate by the ATP-dependent lon protease."
      Ondrovicova G., Liu T., Singh K., Tian B., Li H., Gakh O., Perecko D., Janata J., Granot Z., Orly J., Kutejova E., Suzuki C.K.
      J. Biol. Chem. 280:25103-25110(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "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].
    15. "Proteomic analysis of mitochondrial protein turnover: identification of novel substrate proteins of the matrix protease pim1."
      Major T., von Janowsky B., Ruppert T., Mogk A., Voos W.
      Mol. Cell. Biol. 26:762-776(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBSTRATE.
    16. "Identification of novel oxidized protein substrates and physiological partners of the mitochondrial ATP-dependent Lon-like protease Pim1."
      Bayot A., Gareil M., Rogowska-Wrzesinska A., Roepstorff P., Friguet B., Bulteau A.L.
      J. Biol. Chem. 285:11445-11457(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE.

    Entry informationi

    Entry nameiLONM_YEAST
    AccessioniPrimary (citable) accession number: P36775
    Secondary accession number(s): D6VPX8, P13435
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 131 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 14500 molecules/cell in log phase SD medium.1 Publication

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

    External Data

    Dasty 3