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Entry version 151 (07 Apr 2021)
Sequence version 3 (02 Dec 2020)
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Protein

Leukotriene A-4 hydrolase

Gene

Lta4h

Organism
Rattus norvegicus (Rat)
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

Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities (By similarity). Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the proinflammatory mediator leukotriene B4 (LTB4) (PubMed:1544505). Has also aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides. In addition to its proinflammatory EH activity, may also counteract inflammation by its aminopeptidase activity, which inactivates by cleavage another neutrophil attractant, the tripeptide Pro-Gly-Pro (PGP), a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP9) and prolylendopeptidase (PREPL). Involved also in the biosynthesis of resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, two lipid mediators that show potent anti-inflammatory and pro-resolving actions (By similarity).By similarity1 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+By similarityNote: Binds 1 zinc ion per subunit.By similarity

<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 bestatin (By similarity). Inhibited by captopril (PubMed:1544505). The epoxide hydrolase activity is restrained by suicide inactivation that involves binding of LTA4 to Tyr-379. 4-(4-benzylphenyl)thiazol-2-amine (ARM1) selectively inhibits the epoxide hydrolase activity (By similarity).By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: leukotriene B4 biosynthesis

This protein is involved in the pathway leukotriene B4 biosynthesis, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway leukotriene B4 biosynthesis and in Lipid metabolism.

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 bindingi296Zinc; catalyticBy similarity1
<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 sitei297Proton acceptorBy similarity1
Metal bindingi300Zinc; catalyticBy similarity1
Metal bindingi319Zinc; catalyticBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei376Essential for epoxide hydrolase activity, but not for aminopeptidase activityBy similarity1
Sitei379Covalently modified during suicide inhibition by leukotrienesBy similarity1
Active sitei384Proton donorBy similarity1

<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
Biological processLeukotriene biosynthesis
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.3.2.6, 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-RNO-6798695, Neutrophil degranulation
R-RNO-9018676, Biosynthesis of D-series resolvins
R-RNO-9018681, Biosynthesis of protectins
R-RNO-9018896, Biosynthesis of E-series 18(S)-resolvins
R-RNO-9020265, Biosynthesis of aspirin-triggered D-series resolvins
R-RNO-9023661, Biosynthesis of E-series 18(R)-resolvins

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00878

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M01.004

<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:
Leukotriene A-4 hydrolase (EC:3.3.2.61 Publication)
Short name:
LTA-4 hydrolase
Alternative name(s):
Leukotriene A(4) hydrolase
Tripeptide aminopeptidase LTA4HCurated (EC:3.4.11.4By similarity)
<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:Lta4h
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 7

Organism-specific databases

Rat genome database

More...
RGDi
1311333, Lta4h

<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

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2400

<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_00000951261 – 611Leukotriene A-4 hydrolaseAdd BLAST611

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei73N6-acetyllysineBy similarity1
Modified residuei337N6-acetyllysineBy similarity1
Modified residuei414N6-acetyllysineBy similarity1
Modified residuei416PhosphoserineBy similarity1
Modified residuei573N6-acetyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Ser-416 inhibits leukotriene-A4 hydrolase activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P30349

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

More...
PaxDbi
P30349

PeptideAtlas

More...
PeptideAtlasi
P30349

PRoteomics IDEntifications database

More...
PRIDEi
P30349

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P30349

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P30349

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000004494, Expressed in lung and 8 other tissues

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

By similarity

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P30349, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000005930

<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

3D structure databases

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

More...
SMRi
P30349

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Regioni135 – 137Substrate bindingBy similarity3
Regioni267 – 272Substrate bindingBy similarity6
Regioni564 – 566Substrate bindingBy similarity3

<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
COG0308, LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156375

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_014505_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P30349

Identification of Orthologs from Complete Genome Data

More...
OMAi
NSNFRMK

Database of Orthologous Groups

More...
OrthoDBi
775595at2759

TreeFam database of animal gene trees

More...
TreeFami
TF300758

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
IPR042097, Aminopeptidase_N-like_N
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

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.

P30349-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPEVADTCSL ASPASVCRTQ HLHLRCSVDF ARRALTGTAA LTVQSQEDNL
60 70 80 90 100
RSLTLDTKDL TIEKVVINGQ EVKYTLGESQ GYKGSPMEIS LPIALSKNQE
110 120 130 140 150
VVIEISFETS PKSSALQWLT PEQTSGKQHP YLFSQCQAIH CRAILPCQDT
160 170 180 190 200
PSVKLTYTAE VSVPKELVAL MSAIRDGEAP DPEDPSRKIY RFNQRVPIPC
210 220 230 240 250
YLIALVVGAL ESRQIGPRTL VWSEKEQVEK SAYEFSETES MLKIAEDLGG
260 270 280 290 300
PYVWGQYDLL VLPPSFPYGG MENPCLTFVT PTLLAGDKSL SNVIAHEISH
310 320 330 340 350
SWTGNLVTNK TWDHFWLNEG HTVYLERHIC GRLFGEKFRH FHALGGWGEL
360 370 380 390 400
QNTIKTFGES HPFTKLVVDL KDVDPDVAYS SIPYEKGFAL LFYLEQLLGG
410 420 430 440 450
PEVFLGFLKA YVEKFSYQSV TTDDWKSFLY AHFKDKVDLL NQVDWNAWLY
460 470 480 490 500
APGLPPVKPN YDVTLTNACI ALSQRWVTAK EEDLNSFSIE DLKDLSSHQL
510 520 530 540 550
NEFLAQVLQK APLPLGHIKR MQEVYNFNAI NNSEIRFRWL RLCIQSKWEE
560 570 580 590 600
AIPLALKMAT EQGRMKFTRP LFKDLAAFDK SHDQAVRTYQ EHKACMHPVT
610
AMLVGKDLKV D
Length:611
Mass (Da):69,089
Last modified:December 2, 2020 - v3
<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:i350BDE2683C223C9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti5A → E in AAB21778 (PubMed:1544505).Curated1
Sequence conflicti52S → T in AAB21778 (PubMed:1544505).Curated1
Sequence conflicti136 – 137CQ → WE in AAB21778 (PubMed:1544505).Curated2
Sequence conflicti151Missing in AAB21778 (PubMed:1544505).Curated1
Sequence conflicti510K → R in AAB21778 (PubMed:1544505).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
S87522 mRNA Translation: AAB21778.1
AABR07056638 Genomic DNA No translation available.
BC099819 mRNA Translation: AAH99819.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S20444

NCBI Reference Sequences

More...
RefSeqi
NP_001025202.1, NM_001030031.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000005930; ENSRNOP00000005930; ENSRNOG00000004494

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
299732

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:299732

UCSC genome browser

More...
UCSCi
RGD:1311333, rat

<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
S87522 mRNA Translation: AAB21778.1
AABR07056638 Genomic DNA No translation available.
BC099819 mRNA Translation: AAH99819.1
PIRiS20444
RefSeqiNP_001025202.1, NM_001030031.1

3D structure databases

SMRiP30349
ModBaseiSearch...

Protein-protein interaction databases

IntActiP30349, 2 interactors
STRINGi10116.ENSRNOP00000005930

Chemistry databases

ChEMBLiCHEMBL2400

Protein family/group databases

MEROPSiM01.004

PTM databases

iPTMnetiP30349
PhosphoSitePlusiP30349

Proteomic databases

jPOSTiP30349
PaxDbiP30349
PeptideAtlasiP30349
PRIDEiP30349

Genome annotation databases

EnsembliENSRNOT00000005930; ENSRNOP00000005930; ENSRNOG00000004494
GeneIDi299732
KEGGirno:299732
UCSCiRGD:1311333, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4048
RGDi1311333, Lta4h

Phylogenomic databases

eggNOGiKOG1047, Eukaryota
COG0308, LUCA
GeneTreeiENSGT00940000156375
HOGENOMiCLU_014505_0_0_1
InParanoidiP30349
OMAiNSNFRMK
OrthoDBi775595at2759
TreeFamiTF300758

Enzyme and pathway databases

UniPathwayiUPA00878
BRENDAi3.3.2.6, 5301
ReactomeiR-RNO-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-RNO-6798695, Neutrophil degranulation
R-RNO-9018676, Biosynthesis of D-series resolvins
R-RNO-9018681, Biosynthesis of protectins
R-RNO-9018896, Biosynthesis of E-series 18(S)-resolvins
R-RNO-9020265, Biosynthesis of aspirin-triggered D-series resolvins
R-RNO-9023661, Biosynthesis of E-series 18(R)-resolvins

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P30349

Gene expression databases

BgeeiENSRNOG00000004494, Expressed in lung and 8 other tissues

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
IPR042097, Aminopeptidase_N-like_N
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
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_RAT
<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: P30349
Secondary accession number(s): Q499P2
<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: April 1, 1993
Last sequence update: December 2, 2020
Last modified: April 7, 2021
This is version 151 of the entry and version 3 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 programChordata 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

Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
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