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Protein

Leucine aminopeptidase 2

Gene

LAP2

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

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 Publications

Miscellaneous

Present with 5590 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

An epoxide + H2O = a glycol.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Enzyme 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

  1. KM=1.5 mM for Leu-p-nitroanilide3 Publications
  2. KM=1.8 mM for Met-p-nitroanilide3 Publications
  3. KM=2.0 mM for Ala-p-nitroanilide3 Publications
  1. Vmax=520 nmol/min/mg enzyme with Leu-p-nitroanilide as substrate3 Publications
  2. Vmax=360 nmol/min/mg enzyme with Met-p-nitroanilide as substrate3 Publications
  3. 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 keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi340Zinc; catalytic1
Active sitei341Proton acceptor1
Metal bindingi344Zinc; catalytic1
Metal bindingi363Zinc; catalytic1
Active sitei429Proton donor1

GO - Molecular functioni

  • aminopeptidase activity Source: SGD
  • epoxide hydrolase activity Source: SGD
  • leukotriene-A4 hydrolase activity Source: UniProtKB-EC
  • metalloaminopeptidase activity Source: GO_Central
  • peptide binding Source: GO_Central
  • 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 functionHydrolase, Metalloprotease, Protease
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YNL045W-MONOMER
ReactomeiR-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-RKiQ10740

Protein family/group databases

MEROPSiM01.034

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine aminopeptidase 21 Publication (EC:3.4.11.-1 Publication)
Alternative name(s):
Epoxide hydrolase1 Publication (EC:3.3.2.101 Publication)
Leucyl aminopeptidase yscIV
Short name:
AP IV
Leukotriene A-4 hydrolase homolog1 Publication
Short name:
LTA-4 hydrolase
Gene namesi
Name:LAP21 Publication
Ordered Locus Names:YNL045W
ORF Names:N2535
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL045W
SGDiS000004990 LAP2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi244Y → F: Reduces strongly the substrate affinity. 1 Publication1
Mutagenesisi316E → A, Q or D: Abolishes the aminopeptidase activity. 1 Publication1
Mutagenesisi340H → Q: Abolishes the epoxide hydrolase and aminopeptidase activities. 1 Publication1
Mutagenesisi341E → Q: Abolishes aminopeptidase activity. No effect on the epoxide hydrolase activity. 1 Publication1
Mutagenesisi344H → Q: Abolishes the epoxide hydrolase and aminopeptidase activities. 1 Publication1
Mutagenesisi363E → Q: Abolishes the epoxide hydrolase activity. 1 Publication1
Mutagenesisi424F → Y: Increases the aminopeptidase activity and decreases the epoxide hydrolase activity. 1 Publication1
Mutagenesisi429Y → F: Abolishes the aminopeptidase activity and decreases the epoxide hydrolase activity. 1 Publication1
Mutagenesisi627R → K or A: Abolishes the aminopeptidase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000951291 – 671Leucine aminopeptidase 2Add BLAST671

Proteomic databases

MaxQBiQ10740
PaxDbiQ10740
PRIDEiQ10740

PTM databases

iPTMnetiQ10740

Interactioni

Protein-protein interaction databases

BioGridi35779, 83 interactors
DIPiDIP-4371N
IntActiQ10740, 6 interactors
MINTiQ10740
STRINGi4932.YNL045W

Structurei

Secondary structure

1671
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 48Combined sources6
Beta strandi51 – 54Combined sources4
Helixi64 – 66Combined sources3
Beta strandi67 – 79Combined sources13
Turni80 – 83Combined sources4
Beta strandi84 – 95Combined sources12
Beta strandi99 – 101Combined sources3
Beta strandi105 – 109Combined sources5
Beta strandi111 – 120Combined sources10
Beta strandi127 – 129Combined sources3
Turni134 – 136Combined sources3
Beta strandi140 – 143Combined sources4
Beta strandi147 – 159Combined sources13
Beta strandi164 – 169Combined sources6
Turni171 – 173Combined sources3
Beta strandi175 – 178Combined sources4
Beta strandi180 – 183Combined sources4
Turni186 – 189Combined sources4
Helixi190 – 192Combined sources3
Beta strandi204 – 211Combined sources8
Beta strandi216 – 222Combined sources7
Beta strandi232 – 241Combined sources10
Helixi243 – 245Combined sources3
Beta strandi248 – 252Combined sources5
Beta strandi254 – 259Combined sources6
Beta strandi262 – 266Combined sources5
Helixi268 – 278Combined sources11
Turni279 – 281Combined sources3
Helixi282 – 292Combined sources11
Beta strandi297 – 299Combined sources3
Beta strandi303 – 305Combined sources3
Beta strandi312 – 315Combined sources4
Beta strandi321 – 323Combined sources3
Helixi325 – 327Combined sources3
Beta strandi330 – 332Combined sources3
Helixi336 – 344Combined sources9
Turni348 – 350Combined sources3
Beta strandi351 – 355Combined sources5
Helixi356 – 359Combined sources4
Helixi360 – 378Combined sources19
Helixi380 – 399Combined sources20
Beta strandi401 – 403Combined sources3
Helixi404 – 407Combined sources4
Beta strandi409 – 411Combined sources3
Beta strandi416 – 418Combined sources3
Helixi420 – 423Combined sources4
Helixi427 – 442Combined sources16
Helixi446 – 459Combined sources14
Turni460 – 462Combined sources3
Beta strandi463 – 465Combined sources3
Helixi467 – 477Combined sources11
Helixi479 – 481Combined sources3
Helixi482 – 486Combined sources5
Helixi490 – 495Combined sources6
Helixi508 – 523Combined sources16
Turni524 – 526Combined sources3
Helixi530 – 536Combined sources7
Helixi539 – 542Combined sources4
Helixi547 – 558Combined sources12
Beta strandi562 – 565Combined sources4
Helixi572 – 574Combined sources3
Helixi576 – 585Combined sources10
Helixi587 – 591Combined sources5
Helixi596 – 608Combined sources13
Helixi612 – 614Combined sources3
Helixi615 – 621Combined sources7
Turni622 – 624Combined sources3
Helixi628 – 639Combined sources12
Helixi643 – 653Combined sources11
Helixi654 – 656Combined sources3
Helixi659 – 668Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XPYX-ray2.73A40-671[»]
2XPZX-ray2.30A40-671[»]
2XQ0X-ray1.96A40-669[»]
ProteinModelPortaliQ10740
SMRiQ10740
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ10740

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni184 – 186Substrate binding3
Regioni311 – 316Substrate binding6

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000063003
HOGENOMiHOG000293296
InParanoidiQ10740
KOiK01254
OMAiNFEHFWL
OrthoDBiEOG092C0ZZE

Family and domain databases

CDDicd09599 M1_LTA4H, 1 hit
Gene3Di1.10.390.10, 1 hit
1.25.40.320, 1 hit
InterProiView protein in InterPro
IPR016024 ARM-type_fold
IPR012777 Leukotriene_A4_hydrolase
IPR038502 M1_LTA-4_hydro/amino_C_sf
IPR034015 M1_LTA4H
IPR001930 Peptidase_M1
IPR015211 Peptidase_M1_C
IPR014782 Peptidase_M1_N
IPR027268 Peptidase_M4/M1_CTD_sf
PANTHERiPTHR11533 PTHR11533, 1 hit
PfamiView protein in Pfam
PF09127 Leuk-A4-hydro_C, 1 hit
PF01433 Peptidase_M1, 1 hit
PRINTSiPR00756 ALADIPTASE
SMARTiView protein in SMART
SM01263 Leuk-A4-hydro_C, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit
TIGRFAMsiTIGR02411 leuko_A4_hydro, 1 hit
PROSITEiView protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

Sequencei

Sequence statusi: Complete.

Q10740-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:671
Mass (Da):77,353
Last modified:October 1, 1996 - v1
Checksum:i454E40F030BF28FA
GO

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
PIRiS61099
RefSeqiNP_014353.1, NM_001182884.1

Genome annotation databases

EnsemblFungiiYNL045W; YNL045W; YNL045W
GeneIDi855682
KEGGisce:YNL045W

Similar proteinsi

Entry informationi

Entry nameiLKHA4_YEAST
AccessioniPrimary (citable) accession number: Q10740
Secondary accession number(s): D6W1D4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 173 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

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