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Entry version 193 (23 Feb 2022)
Sequence version 1 (01 Oct 1996)
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Protein

Leucine aminopeptidase 2

Gene

LAP2

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi340Zinc; catalytic1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei341Proton acceptor1
Metal bindingi344Zinc; catalytic1
Metal bindingi363Zinc; catalytic1
Active sitei429Proton donor1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
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-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q10740

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M01.034

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:LAP21 Publication
Ordered Locus Names:YNL045W
ORF Names:N2535
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XIV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000004990, LAP2

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YNL045W

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000951291 – 671Leucine aminopeptidase 2Add BLAST671

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q10740

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q10740

PRoteomics IDEntifications database

More...
PRIDEi
Q10740

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q10740

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
35779, 87 interactors

Database of interacting proteins

More...
DIPi
DIP-4371N

Protein interaction database and analysis system

More...
IntActi
Q10740, 6 interactors

Molecular INTeraction database

More...
MINTi
Q10740

STRING: functional protein association networks

More...
STRINGi
4932.YNL045W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q10740, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1671
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q10740

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q10740

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni184 – 186Substrate binding3
Regioni311 – 316Substrate binding6

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1047, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156375

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_014505_1_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q10740

Identification of Orthologs from Complete Genome Data

More...
OMAi
CTALQWM

Family and domain databases

Conserved Domains Database

More...
CDDi
cd09599, M1_LTA4H, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.390.10, 1 hit
1.25.40.320, 1 hit
2.60.40.1730, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

The PANTHER Classification System

More...
PANTHERi
PTHR45726, PTHR45726, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF09127, Leuk-A4-hydro_C, 1 hit
PF01433, Peptidase_M1, 1 hit
PF17900, Peptidase_M1_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00756, ALADIPTASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01263, Leuk-A4-hydro_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48371, SSF48371, 1 hit
SSF63737, SSF63737, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02411, leuko_A4_hydro, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00142, ZINC_PROTEASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i454E40F030BF28FA
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X94547 Genomic DNA Translation: CAA64237.1
Z71321 Genomic DNA Translation: CAA95912.1
BK006947 Genomic DNA Translation: DAA10500.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S61099

NCBI Reference Sequences

More...
RefSeqi
NP_014353.1, NM_001182884.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YNL045W_mRNA; YNL045W; YNL045W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855682

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YNL045W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
PIRiS61099
RefSeqiNP_014353.1, NM_001182884.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XPYX-ray2.73A40-671[»]
2XPZX-ray2.30A40-671[»]
2XQ0X-ray1.96A40-669[»]
SMRiQ10740
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi35779, 87 interactors
DIPiDIP-4371N
IntActiQ10740, 6 interactors
MINTiQ10740
STRINGi4932.YNL045W

Protein family/group databases

MEROPSiM01.034

PTM databases

iPTMnetiQ10740

Proteomic databases

MaxQBiQ10740
PaxDbiQ10740
PRIDEiQ10740

Genome annotation databases

EnsemblFungiiYNL045W_mRNA; YNL045W; YNL045W
GeneIDi855682
KEGGisce:YNL045W

Organism-specific databases

SGDiS000004990, LAP2
VEuPathDBiFungiDB:YNL045W

Phylogenomic databases

eggNOGiKOG1047, Eukaryota
GeneTreeiENSGT00940000156375
HOGENOMiCLU_014505_1_1_1
InParanoidiQ10740
OMAiCTALQWM

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ10740

Protein Ontology

More...
PROi
PR:Q10740
RNActiQ10740, protein

Family and domain databases

CDDicd09599, M1_LTA4H, 1 hit
Gene3Di1.10.390.10, 1 hit
1.25.40.320, 1 hit
2.60.40.1730, 1 hit
InterProiView 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
PANTHERiPTHR45726, PTHR45726, 1 hit
PfamiView protein in Pfam
PF09127, Leuk-A4-hydro_C, 1 hit
PF01433, Peptidase_M1, 1 hit
PF17900, Peptidase_M1_N, 1 hit
PRINTSiPR00756, ALADIPTASE
SMARTiView protein in SMART
SM01263, Leuk-A4-hydro_C, 1 hit
SUPFAMiSSF48371, SSF48371, 1 hit
SSF63737, SSF63737, 1 hit
TIGRFAMsiTIGR02411, leuko_A4_hydro, 1 hit
PROSITEiView protein in PROSITE
PS00142, ZINC_PROTEASE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLKHA4_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q10740
Secondary accession number(s): D6W1D4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated 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.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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