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P36775 (LONM_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. 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:
Lon protease homolog, mitochondrial

EC=3.4.21.-
Gene names
Name:PIM1
Synonyms:LON
Ordered Locus Names:YBL022C
ORF Names:YBL0440
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1133 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.15 Ref.17

Subunit structure

Homoheptamer. Organized in a ring with a central cavity. Oligomerization is independent of its proteolytic activity and the autocatalytic maturation of its subunits. Ref.8 Ref.12

Subcellular location

Mitochondrion matrix Ref.7 Ref.13 Ref.16.

Miscellaneous

Present with 14500 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase S16 family.

Contains 1 Lon domain.

Biophysicochemical properties

Kinetic parameters:

KM=40 µM for ATP for ATPase activity Ref.9

pH dependence:

Optimum pH is 7.9.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Mitochondrion Potential
Propeptide38 – 9861Removed in mature form; by autocatalysis HAMAP-Rule MF_03120
PRO_0000395761
Chain99 – 11331035Lon protease homolog, mitochondrial HAMAP-Rule MF_03120
PRO_0000026733

Regions

Domain183 – 478296Lon
Nucleotide binding632 – 6398ATP By similarity

Sites

Active site10151 By similarity
Active site10581 By similarity

Experimental info

Mutagenesis6381K → N: Abolishes ATP-binding. Ref.7 Ref.10
Mutagenesis10151S → A: Abolishes peptidase activity. Ref.7 Ref.10
Sequence conflict5091Q → R in AAA53625. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P36775 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 281CAB94579FFF09

FASTA1,133127,112
        10         20         30         40         50         60 
MLRTRTTKTL STVARTTRAI QYYRSIAKTA AVSQRRFAST LTVRDVENIK PSHIIKSPTW 

        70         80         90        100        110        120 
QEFQHQLKDP RYMEHFAQLD AQFARHFMAT NSGKSILAKD DSTSQKKDED VKIVPDEKDT 

       130        140        150        160        170        180 
DNDVEPTRDD EIVNKDQEGE ASKNSRSSAS GGGQSSSSRS DSGDGSSKQK PPKDVPEVYP 

       190        200        210        220        230        240 
QMLALPIARR PLFPGFYKAV VISDERVMKA IKEMLDRQQP YIGAFMLKNS EEDTDVITDK 

       250        260        270        280        290        300 
NDVYDVGVLA QITSAFPSKD EKTGTETMTA LLYPHRRIKI DELFPPNEEK EKSKEQAKDT 

       310        320        330        340        350        360 
DTETTVVEDA NNPEDQESTS PATPKLEDIV VERIPDSELQ HHKRVEATEE ESEELDDIQE 

       370        380        390        400        410        420 
GEDINPTEFL KNYNVSLVNV LNLEDEPFDR KSPVINALTS EILKVFKEIS QLNTMFREQI 

       430        440        450        460        470        480 
ATFSASIQSA TTNIFEEPAR LADFAAAVSA GEEDELQDIL SSLNIEHRLE KSLLVLKKEL 

       490        500        510        520        530        540 
MNAELQNKIS KDVETKIQKR QREYYLMEQL KGIKRELGID DGRDKLIDTY KERIKSLKLP 

       550        560        570        580        590        600 
DSVQKIFDDE ITKLSTLETS MSEFGVIRNY LDWLTSIPWG KHSKEQYSIP RAKKILDEDH 

       610        620        630        640        650        660 
YGMVDVKDRI LEFIAVGKLL GKVDGKIICF VGPPGVGKTS IGKSIARALN RKFFRFSVGG 

       670        680        690        700        710        720 
MTDVAEIKGH RRTYIGALPG RVVQALKKCQ TQNPLILIDE IDKIGHGGIH GDPSAALLEV 

       730        740        750        760        770        780 
LDPEQNNSFL DNYLDIPIDL SKVLFVCTAN SLETIPRPLL DRMEVIELTG YVAEDKVKIA 

       790        800        810        820        830        840 
EQYLVPSAKK SAGLENSHVD MTEDAITALM KYYCRESGVR NLKKHIEKIY RKAALQVVKK 

       850        860        870        880        890        900 
LSIEDSPTSS ADSKPKESVS SEEKAENNAK SSSEKTKDNN SEKTSDDIEA LKTSEKINVS 

       910        920        930        940        950        960 
ISQKNLKDYV GPPVYTTDRL YETTPPGVVM GLAWTNMGGC SLYVESVLEQ PLHNCKHPTF 

       970        980        990       1000       1010       1020 
ERTGQLGDVM KESSRLAYSF AKMYLAQKFP ENRFFEKASI HLHCPEGATP KDGPSAGVTM 

      1030       1040       1050       1060       1070       1080 
ATSFLSLALN KSIDPTVAMT GELTLTGKVL RIGGLREKAV AAKRSGAKTI IFPKDNLNDW 

      1090       1100       1110       1120       1130 
EELPDNVKEG LEPLAADWYN DIFQKLFKDV NTKEGNSVWK AEFEILDAKK EKD 

« Hide

References

« Hide 'large scale' references
[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]Erratum
Suzuki C.K., Suda K., Wang N., Schatz G.
Science 264:891-891(1994) [PubMed] [Europe PMC] [Abstract]
[4]"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. expand/collapse author list , 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.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]Erratum
Rep M., van Dijl J.M., Suda K., Schatz G., Grivell L.A., Suzuki C.K.
Science 275:741-741(1997)
[12]"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.
[13]"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].
[14]"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].
[15]"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.
[16]"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].
[17]"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.
[18]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS43938.
RefSeqNP_009531.1. NM_001178262.1.

3D structure databases

ProteinModelPortalP36775.
SMRP36775. Positions 391-518, 527-1109.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32676. 71 interactions.
DIPDIP-6629N.
IntActP36775. 13 interactions.
MINTMINT-626645.

Protein family/group databases

MEROPSS16.010.

Proteomic databases

PaxDbP36775.
PeptideAtlasP36775.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBL022C; YBL022C; YBL022C.
GeneID852259.
KEGGsce:YBL022C.

Organism-specific databases

CYGDYBL022c.
SGDS000000118. PIM1.

Phylogenomic databases

eggNOGCOG0466.
GeneTreeENSGT00530000063553.
HOGENOMHOG000261409.
KOK08675.
OMARSAENFG.
OrthoDBEOG7327X6.

Enzyme and pathway databases

BioCycYEAST:G3O-28925-MONOMER.

Gene expression databases

GenevestigatorP36775.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_03120. lonm_euk.
InterProIPR003593. 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]
PANTHERPTHR10046. PTHR10046. 1 hit.
PfamPF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR00763. lon. 1 hit.
PROSITEPS01046. LON_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio970847.
PROP36775.

Entry information

Entry nameLONM_YEAST
AccessionPrimary (citable) accession number: P36775
Secondary accession number(s): D6VPX8, P13435
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 129 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 II

Yeast (Saccharomyces cerevisiae) chromosome II: 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