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P36775

- LONM_YEAST

UniProt

P36775 - LONM_YEAST

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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

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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP36775.
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

        10         20         30         40         50
MLRTRTTKTL STVARTTRAI QYYRSIAKTA AVSQRRFAST LTVRDVENIK
60 70 80 90 100
PSHIIKSPTW QEFQHQLKDP RYMEHFAQLD AQFARHFMAT NSGKSILAKD
110 120 130 140 150
DSTSQKKDED VKIVPDEKDT DNDVEPTRDD EIVNKDQEGE ASKNSRSSAS
160 170 180 190 200
GGGQSSSSRS DSGDGSSKQK PPKDVPEVYP QMLALPIARR PLFPGFYKAV
210 220 230 240 250
VISDERVMKA IKEMLDRQQP YIGAFMLKNS EEDTDVITDK NDVYDVGVLA
260 270 280 290 300
QITSAFPSKD EKTGTETMTA LLYPHRRIKI DELFPPNEEK EKSKEQAKDT
310 320 330 340 350
DTETTVVEDA NNPEDQESTS PATPKLEDIV VERIPDSELQ HHKRVEATEE
360 370 380 390 400
ESEELDDIQE GEDINPTEFL KNYNVSLVNV LNLEDEPFDR KSPVINALTS
410 420 430 440 450
EILKVFKEIS QLNTMFREQI ATFSASIQSA TTNIFEEPAR LADFAAAVSA
460 470 480 490 500
GEEDELQDIL SSLNIEHRLE KSLLVLKKEL MNAELQNKIS KDVETKIQKR
510 520 530 540 550
QREYYLMEQL KGIKRELGID DGRDKLIDTY KERIKSLKLP DSVQKIFDDE
560 570 580 590 600
ITKLSTLETS MSEFGVIRNY LDWLTSIPWG KHSKEQYSIP RAKKILDEDH
610 620 630 640 650
YGMVDVKDRI LEFIAVGKLL GKVDGKIICF VGPPGVGKTS IGKSIARALN
660 670 680 690 700
RKFFRFSVGG MTDVAEIKGH RRTYIGALPG RVVQALKKCQ TQNPLILIDE
710 720 730 740 750
IDKIGHGGIH GDPSAALLEV LDPEQNNSFL DNYLDIPIDL SKVLFVCTAN
760 770 780 790 800
SLETIPRPLL DRMEVIELTG YVAEDKVKIA EQYLVPSAKK SAGLENSHVD
810 820 830 840 850
MTEDAITALM KYYCRESGVR NLKKHIEKIY RKAALQVVKK LSIEDSPTSS
860 870 880 890 900
ADSKPKESVS SEEKAENNAK SSSEKTKDNN SEKTSDDIEA LKTSEKINVS
910 920 930 940 950
ISQKNLKDYV GPPVYTTDRL YETTPPGVVM GLAWTNMGGC SLYVESVLEQ
960 970 980 990 1000
PLHNCKHPTF ERTGQLGDVM KESSRLAYSF AKMYLAQKFP ENRFFEKASI
1010 1020 1030 1040 1050
HLHCPEGATP KDGPSAGVTM ATSFLSLALN KSIDPTVAMT GELTLTGKVL
1060 1070 1080 1090 1100
RIGGLREKAV AAKRSGAKTI IFPKDNLNDW EELPDNVKEG LEPLAADWYN
1110 1120 1130
DIFQKLFKDV NTKEGNSVWK AEFEILDAKK EKD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi P36775.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 132 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