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Protein

Cysteine proteinase 1, mitochondrial

Gene

LAP3

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

Functioni

The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities.2 Publications

Catalytic activityi

Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred.

Enzyme regulationi

Inhibited by E64, a specific inhibitor of cysteine proteases, N-ethylmaleimide, iodacetamide, and mercury and zinc ions.2 Publications

Kineticsi

N-terminal acetylation of lysine-4-methyl-7-coumarylamide (Ac-Lys-AMC) reduces the catalytic efficiency 50-fold towards this substrate.

  1. KM=12.8 µM for arginine-4-methyl-7-coumarylamide3 Publications
  2. KM=0.33 mM for glutamine-beta-naphthylamide3 Publications
  3. KM=228 µM for lysine-4-methyl-7-coumarylamide3 Publications
  1. Vmax=2.56 µmol/h/mg enzyme for arginine-4-methyl-7-coumarylamide3 Publications
  2. Vmax=370 nmol/min/mg enzyme for glutamine-beta-naphthylamide3 Publications

pH dependencei

Optimum pH is 7.5.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1021
Active sitei3981
Active sitei4211

GO - Molecular functioni

  • aminopeptidase activity Source: GO_Central
  • cysteine-type endopeptidase activity Source: InterPro
  • cysteine-type peptidase activity Source: SGD
  • double-stranded DNA binding Source: SGD
  • mRNA binding Source: SGD
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: SGD
  • single-stranded DNA binding Source: SGD

GO - Biological processi

  • homocysteine catabolic process Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • response to antibiotic Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33237-MONOMER.
BRENDAi3.4.22.40. 984.
ReactomeiR-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SABIO-RKQ01532.

Protein family/group databases

MEROPSiC01.085.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine proteinase 1, mitochondrial (EC:3.4.22.40)
Alternative name(s):
Bleomycin hydrolase
Short name:
BLM hydrolase
Homocysteine-thiolactonase
Short name:
HTLase
Short name:
Hcy-thiolactonase
Leucine aminopeptidase 3
Y3
Gene namesi
Name:LAP3
Synonyms:BLH1, GAL6, YCP1
Ordered Locus Names:YNL239W
ORF Names:N1118
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL239W.
SGDiS000005183. LAP3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi102C → A: Abolishes peptidase activity, which also hinders autocatalytic processing of the enzyme to the mature form. 1 Publication1
Mutagenesisi271 – 274KDKK → ADAA in GAL6DB; disrupts nucleic acid-binding activity, but retains normal peptidase activity. 1 Publication4
Mutagenesisi398H → A: Abolishes Hcy-thiolactonase activity. 1 Publication1
Mutagenesisi479G → A: Results in the abnormal cleavage of 3 C-terminal residues instead of only 1 during autocatalytic processing. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 30MitochondrionSequence analysisAdd BLAST30
ChainiPRO_000005055431 – 482Cysteine proteinase 1, mitochondrialAdd BLAST452
PropeptideiPRO_0000292865483Removed in mature form; by autocatalysis1 Publication1

Post-translational modificationi

The N-terminus of isoform Cytoplasmic is blocked.

Proteomic databases

PeptideAtlasiQ01532.
PRIDEiQ01532.

Interactioni

Subunit structurei

Homohexamer. Binds to nucleic acids. Binds single-stranded DNA and RNA with higher affinity than double-stranded DNA.1 Publication

Protein-protein interaction databases

BioGridi35600. 15 interactors.
DIPiDIP-2941N.
IntActiQ01532. 11 interactors.
MINTiMINT-513897.

Structurei

Secondary structure

1483
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 47Combined sources12
Helixi50 – 59Combined sources10
Helixi64 – 68Combined sources5
Helixi71 – 77Combined sources7
Beta strandi83 – 85Combined sources3
Beta strandi98 – 100Combined sources3
Helixi102 – 118Combined sources17
Helixi128 – 149Combined sources22
Turni150 – 152Combined sources3
Helixi158 – 165Combined sources8
Helixi174 – 184Combined sources11
Helixi189 – 191Combined sources3
Helixi197 – 200Combined sources4
Helixi203 – 226Combined sources24
Beta strandi229 – 231Combined sources3
Helixi232 – 252Combined sources21
Beta strandi264 – 269Combined sources6
Beta strandi275 – 280Combined sources6
Helixi282 – 288Combined sources7
Beta strandi296 – 301Combined sources6
Beta strandi311 – 314Combined sources4
Beta strandi326 – 330Combined sources5
Helixi333 – 345Combined sources13
Beta strandi350 – 354Combined sources5
Turni356 – 359Combined sources4
Turni362 – 365Combined sources4
Helixi374 – 377Combined sources4
Helixi385 – 390Combined sources6
Beta strandi398 – 407Combined sources10
Turni409 – 411Combined sources3
Beta strandi414 – 420Combined sources7
Turni425 – 428Combined sources4
Beta strandi432 – 436Combined sources5
Helixi437 – 443Combined sources7
Beta strandi444 – 450Combined sources7
Helixi451 – 453Combined sources3
Helixi456 – 463Combined sources8
Beta strandi470 – 472Combined sources3
Helixi477 – 479Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A6RX-ray2.05A32-483[»]
1GCBX-ray2.20A30-483[»]
2DZYX-ray2.57A30-482[»]
2DZZX-ray2.15A30-482[»]
2E00X-ray2.00A30-482[»]
2E01X-ray1.73A30-482[»]
2E02X-ray2.20A30-482[»]
2E03X-ray2.13A30-482[»]
3GCBX-ray1.87A30-482[»]
ProteinModelPortaliQ01532.
SMRiQ01532.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01532.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000064089.
InParanoidiQ01532.
KOiK01372.
OMAiMNTQLRH.
OrthoDBiEOG092C1SX8.

Family and domain databases

CDDicd00585. Peptidase_C1B. 1 hit.
InterProiIPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR004134. Peptidase_C1B.
[Graphical view]
PANTHERiPTHR10363. PTHR10363. 1 hit.
PfamiPF03051. Peptidase_C1_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005700. PepC. 1 hit.
PROSITEiPS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Mitochondrial (identifier: Q01532-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLPTSVSRSL YLKTFRSHLL RAPQIVLKRM SSSIDISKIN SWNKEFQSDL
60 70 80 90 100
THQLATTVLK NYNADDALLN KTRLQKQDNR VFNTVVSTDS TPVTNQKSSG
110 120 130 140 150
RCWLFAATNQ LRLNVLSELN LKEFELSQAY LFFYDKLEKA NYFLDQIVSS
160 170 180 190 200
ADQDIDSRLV QYLLAAPTED GGQYSMFLNL VKKYGLIPKD LYGDLPYSTT
210 220 230 240 250
ASRKWNSLLT TKLREFAETL RTALKERSAD DSIIVTLREQ MQREIFRLMS
260 270 280 290 300
LFMDIPPVQP NEQFTWEYVD KDKKIHTIKS TPLEFASKYA KLDPSTPVSL
310 320 330 340 350
INDPRHPYGK LIKIDRLGNV LGGDAVIYLN VDNETLSKLV VKRLQNNKAV
360 370 380 390 400
FFGSHTPKFM DKKTGVMDIE LWNYPAIGYN LPQQKASRIR YHESLMTHAM
410 420 430 440 450
LITGCHVDET SKLPLRYRVE NSWGKDSGKD GLYVMTQKYF EEYCFQIVVD
460 470 480
INELPKELAS KFTSGKEEPI VLPIWDPMGA LAK
Length:483
Mass (Da):55,483
Last modified:June 26, 2007 - v3
Checksum:iBF92A6049F98DD3D
GO
Isoform Cytoplasmic (identifier: Q01532-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Note: Produced by alternative initiation at Met-30 of isoform Mitochondrial.
Show »
Length:454
Mass (Da):52,089
Checksum:i2F4B6236AEE3BABF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti187I → M in CAA48878 (PubMed:8424954).Curated1

Mass spectrometryi

Molecular mass is 51830 Da from positions 31 - 482. Determined by ESI. 1 Publication

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0264531 – 29Missing in isoform Cytoplasmic. CuratedAdd BLAST29

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97910 Genomic DNA. Translation: AAA35231.1.
X69124 Genomic DNA. Translation: CAA48878.1.
X68228 Genomic DNA. Translation: CAA48309.1.
Z71515 Genomic DNA. Translation: CAA96144.1.
Z69381 Genomic DNA. Translation: CAA93359.1.
U74299 Genomic DNA. Translation: AAB18260.1.
BK006947 Genomic DNA. Translation: DAA10320.1.
PIRiA46093. S25606.
RefSeqiNP_014160.2. NM_001183077.1. [Q01532-2]

Genome annotation databases

GeneIDi855482.
KEGGisce:YNL239W.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97910 Genomic DNA. Translation: AAA35231.1.
X69124 Genomic DNA. Translation: CAA48878.1.
X68228 Genomic DNA. Translation: CAA48309.1.
Z71515 Genomic DNA. Translation: CAA96144.1.
Z69381 Genomic DNA. Translation: CAA93359.1.
U74299 Genomic DNA. Translation: AAB18260.1.
BK006947 Genomic DNA. Translation: DAA10320.1.
PIRiA46093. S25606.
RefSeqiNP_014160.2. NM_001183077.1. [Q01532-2]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A6RX-ray2.05A32-483[»]
1GCBX-ray2.20A30-483[»]
2DZYX-ray2.57A30-482[»]
2DZZX-ray2.15A30-482[»]
2E00X-ray2.00A30-482[»]
2E01X-ray1.73A30-482[»]
2E02X-ray2.20A30-482[»]
2E03X-ray2.13A30-482[»]
3GCBX-ray1.87A30-482[»]
ProteinModelPortaliQ01532.
SMRiQ01532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35600. 15 interactors.
DIPiDIP-2941N.
IntActiQ01532. 11 interactors.
MINTiMINT-513897.

Protein family/group databases

MEROPSiC01.085.

Proteomic databases

PeptideAtlasiQ01532.
PRIDEiQ01532.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi855482.
KEGGisce:YNL239W.

Organism-specific databases

EuPathDBiFungiDB:YNL239W.
SGDiS000005183. LAP3.

Phylogenomic databases

HOGENOMiHOG000064089.
InParanoidiQ01532.
KOiK01372.
OMAiMNTQLRH.
OrthoDBiEOG092C1SX8.

Enzyme and pathway databases

BioCyciYEAST:G3O-33237-MONOMER.
BRENDAi3.4.22.40. 984.
ReactomeiR-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SABIO-RKQ01532.

Miscellaneous databases

EvolutionaryTraceiQ01532.
PROiQ01532.

Family and domain databases

CDDicd00585. Peptidase_C1B. 1 hit.
InterProiIPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR004134. Peptidase_C1B.
[Graphical view]
PANTHERiPTHR10363. PTHR10363. 1 hit.
PfamiPF03051. Peptidase_C1_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005700. PepC. 1 hit.
PROSITEiPS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBLH1_YEAST
AccessioniPrimary (citable) accession number: Q01532
Secondary accession number(s): D6W0V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 26, 2007
Last modified: November 2, 2016
This is version 164 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 521 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.