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UniProtKB - Q10740 (LKHA4_YEAST)
Protein
Leucine aminopeptidase 2
Gene
LAP2
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA4 but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B4 as the product compared to the homologous mammalian enzyme (in vitro).
6 PublicationsMiscellaneous
Present with 5590 molecules/cell in log phase SD medium.1 Publication
Catalytic activityi
- EC:3.3.2.101 Publication
Cofactori
Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication
Activity regulationi
Inhibited by 3-(4-benzyloxyphenyl)-2-(R)-amino-1-propanethiol (thioamine) and N-hydroxy-N-(2-(S)-amino-3-(4-benzyloxyphenyl)propyl)-5-carboxypen-tanamide (hydroxamic acid). The aminopeptidase activity is stimulated by LTA4.2 Publications
Kineticsi
- KM=1.5 mM for Leu-p-nitroanilide3 Publications
- KM=1.8 mM for Met-p-nitroanilide3 Publications
- KM=2.0 mM for Ala-p-nitroanilide3 Publications
- Vmax=520 nmol/min/mg enzyme with Leu-p-nitroanilide as substrate3 Publications
- Vmax=360 nmol/min/mg enzyme with Met-p-nitroanilide as substrate3 Publications
- Vmax=170 nmol/min/mg enzyme with Ala-p-nitroanilide as substrate3 Publications
pH dependencei
Optimum pH is about 7.3.3 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 340 | Zinc; catalytic | 1 | |
Active sitei | 341 | Proton acceptor | 1 | |
Metal bindingi | 344 | Zinc; catalytic | 1 | |
Metal bindingi | 363 | Zinc; catalytic | 1 | |
Active sitei | 429 | Proton donor | 1 |
GO - Molecular functioni
- aminopeptidase activity Source: SGD
- epoxide hydrolase activity Source: SGD
- metallopeptidase activity Source: UniProtKB-KW
- zinc ion binding Source: UniProtKB
GO - Biological processi
- cellular lipid metabolic process Source: SGD
- peptide catabolic process Source: UniProtKB
- protein catabolic process Source: SGD
Keywordsi
Molecular function | Hydrolase, Metalloprotease, Protease |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
Reactomei | R-SCE-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX) R-SCE-6798695, Neutrophil degranulation R-SCE-9018676, Biosynthesis of D-series resolvins R-SCE-9018681, Biosynthesis of protectins R-SCE-9018896, Biosynthesis of E-series 18(S)-resolvins R-SCE-9020265, Biosynthesis of aspirin-triggered D-series resolvins R-SCE-9023661, Biosynthesis of E-series 18(R)-resolvins |
SABIO-RKi | Q10740 |
Protein family/group databases
MEROPSi | M01.034 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:LAP21 Publication Ordered Locus Names:YNL045W ORF Names:N2535 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000004990, LAP2 |
VEuPathDBi | FungiDB:YNL045W |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 244 | Y → F: Reduces strongly the substrate affinity. 1 Publication | 1 | |
Mutagenesisi | 316 | E → A, Q or D: Abolishes the aminopeptidase activity. 1 Publication | 1 | |
Mutagenesisi | 340 | H → Q: Abolishes the epoxide hydrolase and aminopeptidase activities. 1 Publication | 1 | |
Mutagenesisi | 341 | E → Q: Abolishes aminopeptidase activity. No effect on the epoxide hydrolase activity. 1 Publication | 1 | |
Mutagenesisi | 344 | H → Q: Abolishes the epoxide hydrolase and aminopeptidase activities. 1 Publication | 1 | |
Mutagenesisi | 363 | E → Q: Abolishes the epoxide hydrolase activity. 1 Publication | 1 | |
Mutagenesisi | 424 | F → Y: Increases the aminopeptidase activity and decreases the epoxide hydrolase activity. 1 Publication | 1 | |
Mutagenesisi | 429 | Y → F: Abolishes the aminopeptidase activity and decreases the epoxide hydrolase activity. 1 Publication | 1 | |
Mutagenesisi | 627 | R → K or A: Abolishes the aminopeptidase activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000095129 | 1 – 671 | Leucine aminopeptidase 2Add BLAST | 671 |
Proteomic databases
MaxQBi | Q10740 |
PaxDbi | Q10740 |
PRIDEi | Q10740 |
PTM databases
iPTMneti | Q10740 |
Interactioni
Protein-protein interaction databases
BioGRIDi | 35779, 87 interactors |
DIPi | DIP-4371N |
IntActi | Q10740, 6 interactors |
MINTi | Q10740 |
STRINGi | 4932.YNL045W |
Miscellaneous databases
RNActi | Q10740, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q10740 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q10740 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 184 – 186 | Substrate binding | 3 | |
Regioni | 311 – 316 | Substrate binding | 6 |
Sequence similaritiesi
Belongs to the peptidase M1 family.Curated
Phylogenomic databases
eggNOGi | KOG1047, Eukaryota |
GeneTreei | ENSGT00940000156375 |
HOGENOMi | CLU_014505_1_1_1 |
InParanoidi | Q10740 |
OMAi | CTALQWM |
Family and domain databases
CDDi | cd09599, M1_LTA4H, 1 hit |
Gene3Di | 1.10.390.10, 1 hit 1.25.40.320, 1 hit 2.60.40.1730, 1 hit |
InterProi | View protein in InterPro IPR045357, Aminopeptidase_N-like_N IPR042097, Aminopeptidase_N-like_N_sf IPR016024, ARM-type_fold IPR012777, LTA4H IPR038502, M1_LTA-4_hydro/amino_C_sf IPR034015, M1_LTA4H IPR001930, Peptidase_M1 IPR015211, Peptidase_M1_C IPR014782, Peptidase_M1_dom IPR027268, Peptidase_M4/M1_CTD_sf |
PANTHERi | PTHR45726, PTHR45726, 1 hit |
Pfami | View protein in Pfam PF09127, Leuk-A4-hydro_C, 1 hit PF01433, Peptidase_M1, 1 hit PF17900, Peptidase_M1_N, 1 hit |
PRINTSi | PR00756, ALADIPTASE |
SMARTi | View protein in SMART SM01263, Leuk-A4-hydro_C, 1 hit |
SUPFAMi | SSF48371, SSF48371, 1 hit SSF63737, SSF63737, 1 hit |
TIGRFAMsi | TIGR02411, leuko_A4_hydro, 1 hit |
PROSITEi | View protein in PROSITE PS00142, ZINC_PROTEASE, 1 hit |
i Sequence
Sequence statusi: Complete.
Q10740-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MFLLPFVIRH SSSIYLPTLR FRGLLTVISR NIHISTPHKM LPLSIEQRRP
60 70 80 90 100
SRSPEYDQST LSNYKDFAVL HTDLNLSVSF EKSAISGSVT FQLKKLHEGK
110 120 130 140 150
NKSDELHLDT SYLDVQEVHI DGSKADFQIE QRKEPLGSRL VINNASCNDN
160 170 180 190 200
FTLNIQFRTT DKCTALQWLN SKQTKGGKPY VFSQLEAIHA RSLFPCFDTP
210 220 230 240 250
SVKSTFTASI ESPLPVVFSG IRIEDTSKDT NIYRFEQKVP IPAYLIGIAS
260 270 280 290 300
GDLSSAPIGP RSTVYTEPFR LKDCQWEFEN DVEKFIQTAE KIIFEYEWGT
310 320 330 340 350
YDILVNVDSY PYGGMESPNM TFATPTLIAH DRSNIDVIAH ELAHSWSGNL
360 370 380 390 400
VTNCSWNHFW LNEGWTVYLE RRIIGAIHGE PTRHFSALIG WSDLQNSIDS
410 420 430 440 450
MKDPERFSTL VQNLNDNTDP DDAFSTVPYE KGFNLLFHLE TILGGKAEFD
460 470 480 490 500
PFIRHYFKKF AKKSLDTFQF LDTLYEFYPE KKEILDSVDW ETWLYKPGMP
510 520 530 540 550
PRPHFITALA DNVYQLADKW VEMAQHLKTT EDFRSEFNAI DIKDFNSNQL
560 570 580 590 600
VLFLETLTQN GHSNKKPKDF DWAKFPVASR ALLDIYQDNI VKSQNAEVVF
610 620 630 640 650
KMFKFQIFAK LQEEYKHLAD WLGTVGRMKF VRPGYRLLNS VDRRLALATF
660 670
DKFKDTYHPI CKALVKQDLG L
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X94547 Genomic DNA Translation: CAA64237.1 Z71321 Genomic DNA Translation: CAA95912.1 BK006947 Genomic DNA Translation: DAA10500.1 |
PIRi | S61099 |
RefSeqi | NP_014353.1, NM_001182884.1 |
Genome annotation databases
EnsemblFungii | YNL045W_mRNA; YNL045W; YNL045W |
GeneIDi | 855682 |
KEGGi | sce:YNL045W |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X94547 Genomic DNA Translation: CAA64237.1 Z71321 Genomic DNA Translation: CAA95912.1 BK006947 Genomic DNA Translation: DAA10500.1 |
PIRi | S61099 |
RefSeqi | NP_014353.1, NM_001182884.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2XPY | X-ray | 2.73 | A | 40-671 | [»] | |
2XPZ | X-ray | 2.30 | A | 40-671 | [»] | |
2XQ0 | X-ray | 1.96 | A | 40-669 | [»] | |
SMRi | Q10740 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 35779, 87 interactors |
DIPi | DIP-4371N |
IntActi | Q10740, 6 interactors |
MINTi | Q10740 |
STRINGi | 4932.YNL045W |
Protein family/group databases
MEROPSi | M01.034 |
PTM databases
iPTMneti | Q10740 |
Proteomic databases
MaxQBi | Q10740 |
PaxDbi | Q10740 |
PRIDEi | Q10740 |
Genome annotation databases
EnsemblFungii | YNL045W_mRNA; YNL045W; YNL045W |
GeneIDi | 855682 |
KEGGi | sce:YNL045W |
Organism-specific databases
SGDi | S000004990, LAP2 |
VEuPathDBi | FungiDB:YNL045W |
Phylogenomic databases
eggNOGi | KOG1047, Eukaryota |
GeneTreei | ENSGT00940000156375 |
HOGENOMi | CLU_014505_1_1_1 |
InParanoidi | Q10740 |
OMAi | CTALQWM |
Enzyme and pathway databases
Reactomei | R-SCE-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX) R-SCE-6798695, Neutrophil degranulation R-SCE-9018676, Biosynthesis of D-series resolvins R-SCE-9018681, Biosynthesis of protectins R-SCE-9018896, Biosynthesis of E-series 18(S)-resolvins R-SCE-9020265, Biosynthesis of aspirin-triggered D-series resolvins R-SCE-9023661, Biosynthesis of E-series 18(R)-resolvins |
SABIO-RKi | Q10740 |
Miscellaneous databases
EvolutionaryTracei | Q10740 |
PROi | PR:Q10740 |
RNActi | Q10740, protein |
Family and domain databases
CDDi | cd09599, M1_LTA4H, 1 hit |
Gene3Di | 1.10.390.10, 1 hit 1.25.40.320, 1 hit 2.60.40.1730, 1 hit |
InterProi | View protein in InterPro IPR045357, Aminopeptidase_N-like_N IPR042097, Aminopeptidase_N-like_N_sf IPR016024, ARM-type_fold IPR012777, LTA4H IPR038502, M1_LTA-4_hydro/amino_C_sf IPR034015, M1_LTA4H IPR001930, Peptidase_M1 IPR015211, Peptidase_M1_C IPR014782, Peptidase_M1_dom IPR027268, Peptidase_M4/M1_CTD_sf |
PANTHERi | PTHR45726, PTHR45726, 1 hit |
Pfami | View protein in Pfam PF09127, Leuk-A4-hydro_C, 1 hit PF01433, Peptidase_M1, 1 hit PF17900, Peptidase_M1_N, 1 hit |
PRINTSi | PR00756, ALADIPTASE |
SMARTi | View protein in SMART SM01263, Leuk-A4-hydro_C, 1 hit |
SUPFAMi | SSF48371, SSF48371, 1 hit SSF63737, SSF63737, 1 hit |
TIGRFAMsi | TIGR02411, leuko_A4_hydro, 1 hit |
PROSITEi | View protein in PROSITE PS00142, ZINC_PROTEASE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | LKHA4_YEAST | |
Accessioni | Q10740Primary (citable) accession number: Q10740 Secondary accession number(s): D6W1D4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | October 1, 1996 | |
Last modified: | February 23, 2022 | |
This is version 193 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome XIV
Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names - Peptidase families
Classification of peptidase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families