LTA4H

Functionⁱ

Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity.7 Publications

Catalytic activityⁱ

H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
leukotriene A₄
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
leukotriene B₄
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
6 Publications
Manual assertion based on experiment inⁱ
- Ref.10
  "Leukotriene A4 hydrolase in the human B-lymphocytic cell line Raji: indications of catalytically divergent forms of the enzyme."
  Odlander B., Claesson H.E., Bergman T., Radmark O., Joernvall H., Haeggstrom J.Z.
  Arch. Biochem. Biophys. 287:167-174(1991) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 2-22, FUNCTION, CATALYTIC ACTIVITY.
- Ref.12
  "Leukotriene A4 hydrolase: mapping of a henicosapeptide involved in mechanism-based inactivation."
  Mueller M.J., Wetterholm A., Blomster M., Jornvall H., Samuelsson B., Haeggstrom J.Z.
  Proc. Natl. Acad. Sci. U.S.A. 92:8383-8387(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 366-386, ACTIVITY REGULATION, COVALENT MODIFICATION AT TYR-379, CATALYTIC ACTIVITY.
- Ref.26
  "Crystal structures of leukotriene A4 hydrolase in complex with captopril and two competitive tight-binding inhibitors."
  Thunnissen M.M., Andersson B., Samuelsson B., Wong C.H., Haeggstrom J.Z.
  FASEB J. 16:1648-1650(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH CAPTOPRIL AND ZINC IONS, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, ACTIVE SITE.
- Ref.28
  "Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375."
  Rudberg P.C., Tholander F., Thunnissen M.M., Samuelsson B., Haeggstrom J.Z.
  Proc. Natl. Acad. Sci. U.S.A. 99:4215-4220(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT ASN-376 IN COMPLEX WITH BESTATIN AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-135; HIS-140; ASP-372; ASP-374; ASP-376 AND GLU-385.
- Ref.29
  "Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates."
  Rudberg P.C., Tholander F., Andberg M., Thunnissen M.M., Haeggstrom J.Z.
  J. Biol. Chem. 279:27376-27382(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-564 IN COMPLEX WITH ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, MUTAGENESIS OF ARG-564 AND LYS-566.
- Ref.30
  "Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design."
  Tholander F., Muroya A., Roques B.P., Fournie-Zaluski M.C., Thunnissen M.M., Haeggstrom J.Z.
  Chem. Biol. 15:920-929(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF MUTANT GLN-297 IN COMPLEXES WITH SUBSTRATE TRIPEPTIDES AND ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, MUTAGENESIS OF GLU-297 AND ASP-376.
EC:3.3.2.6
6 Publications
Manual assertion based on experiment inⁱ
- Ref.10
  "Leukotriene A4 hydrolase in the human B-lymphocytic cell line Raji: indications of catalytically divergent forms of the enzyme."
  Odlander B., Claesson H.E., Bergman T., Radmark O., Joernvall H., Haeggstrom J.Z.
  Arch. Biochem. Biophys. 287:167-174(1991) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 2-22, FUNCTION, CATALYTIC ACTIVITY.
- Ref.12
  "Leukotriene A4 hydrolase: mapping of a henicosapeptide involved in mechanism-based inactivation."
  Mueller M.J., Wetterholm A., Blomster M., Jornvall H., Samuelsson B., Haeggstrom J.Z.
  Proc. Natl. Acad. Sci. U.S.A. 92:8383-8387(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 366-386, ACTIVITY REGULATION, COVALENT MODIFICATION AT TYR-379, CATALYTIC ACTIVITY.
- Ref.26
  "Crystal structures of leukotriene A4 hydrolase in complex with captopril and two competitive tight-binding inhibitors."
  Thunnissen M.M., Andersson B., Samuelsson B., Wong C.H., Haeggstrom J.Z.
  FASEB J. 16:1648-1650(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH CAPTOPRIL AND ZINC IONS, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, ACTIVE SITE.
- Ref.28
  "Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375."
  Rudberg P.C., Tholander F., Thunnissen M.M., Samuelsson B., Haeggstrom J.Z.
  Proc. Natl. Acad. Sci. U.S.A. 99:4215-4220(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT ASN-376 IN COMPLEX WITH BESTATIN AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-135; HIS-140; ASP-372; ASP-374; ASP-376 AND GLU-385.
- Ref.29
  "Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates."
  Rudberg P.C., Tholander F., Andberg M., Thunnissen M.M., Haeggstrom J.Z.
  J. Biol. Chem. 279:27376-27382(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-564 IN COMPLEX WITH ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, MUTAGENESIS OF ARG-564 AND LYS-566.
- Ref.30
  "Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design."
  Tholander F., Muroya A., Roques B.P., Fournie-Zaluski M.C., Thunnissen M.M., Haeggstrom J.Z.
  Chem. Biol. 15:920-929(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF MUTANT GLN-297 IN COMPLEXES WITH SUBSTRATE TRIPEPTIDES AND ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, MUTAGENESIS OF GLU-297 AND ASP-376.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
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H₂O
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+
leukotriene A₄
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=
leukotriene B₄
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Cofactorⁱ

Zn²⁺3 PublicationsNote: Binds 1 zinc ion per subunit.3 Publications

Activity regulationⁱ

Inhibited by bestatin. Subject to suicide inhibition by leukotriene A4, due to the formation of a covalent adduct at Tyr-379.1 Publication

Pathwayⁱ: leukotriene B4 biosynthesis

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

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	296	Zinc; catalyticCombined sources7 Publications	1
Active siteⁱ	297	Proton acceptorCombined sources1 Publication1 Publication	1
Metal bindingⁱ	300	Zinc; catalyticCombined sources7 Publications	1
Metal bindingⁱ	319	Zinc; catalyticCombined sources7 Publications	1
Siteⁱ	376	Essential for epoxide hydrolase activity, but not for aminopeptidase activity	1
Siteⁱ	379	Covalently modified during suicide inhibition by leukotrienes	1
Active siteⁱ	384	Proton donorCombined sources1 Publication1 Publication	1

GO - Molecular functionⁱ

aminopeptidase activity
Source: UniProtKB
Inferred from direct assayⁱ
epoxide hydrolase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 15078870
leukotriene-A4 hydrolase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 15078870
- 9774412
metalloaminopeptidase activity
Source: CAFA
Inferred from mutant phenotypeⁱ
- 11675384
peptidase activity
Source: ProtInc
Traceable author statementⁱ
- 1881903
RNA binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 22658674
zinc ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 15078870
- 18804029

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular lipid metabolic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cellular protein metabolic process
Source: CAFA
Inferred from mutant phenotypeⁱ
- 11675384
leukotriene biosynthetic process
Source: UniProtKB
Inferred from direct assayⁱ
- 15078870
- 9774412
leukotriene metabolic process Source: Reactome
long-chain fatty acid biosynthetic process Source: Reactome
neutrophil degranulation Source: Reactome
peptide catabolic process
Source: UniProtKB
Inferred from direct assayⁱ

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Metalloprotease, Protease
Biological process	Leukotriene biosynthesis
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS03372-MONOMER
BRENDAⁱ	3.3.2.6 2681
Reactomeⁱ	R-HSA-2142691 Synthesis of Leukotrienes (LT) and Eoxins (EX) R-HSA-6798695 Neutrophil degranulation R-HSA-9018676 Biosynthesis of D-series resolvins R-HSA-9018681 Biosynthesis of protectins R-HSA-9018896 Biosynthesis of E-series 18(S)-resolvins R-HSA-9020265 Biosynthesis of aspirin-triggered D-series resolvins R-HSA-9023661 Biosynthesis of E-series 18(R)-resolvins
SABIO-RKⁱ	P09960
UniPathwayⁱ	UPA00878

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	M01.004
MoonProtⁱ	P09960

Chemistry databases

SwissLipidsⁱ	SLP:000001118

SwissLipidsⁱ

SLP:000001118

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Leukotriene A-4 hydrolase (EC:3.3.2.6) Short name: LTA-4 hydrolase Alternative name(s): Leukotriene A(4) hydrolase
Gene namesⁱ	Name:LTA4H Synonyms:LTA4
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 12

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000111144.9
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:6710 LTA4H
MIMⁱ	151570 gene
neXtProtⁱ	NX_P09960

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	135	Q → A or L: Srongly increased epoxide hydrolase activity. 1 Publication	1
Mutagenesisⁱ	135	Q → A: Strongly reduced aminopeptidase activity. Strongly decreased affinity for leukotriene. Abolishes epoxide hydrolase activity. 1 Publication	1
Mutagenesisⁱ	137	Q → A: No loss of activity. 1 Publication	1
Mutagenesisⁱ	137	Q → L: Aminopeptidase activity strongly impaired, but keeps LTA4 activity. 1 Publication	1
Mutagenesisⁱ	137	Q → N: Aminopeptidase activity almost absent, but keeps LTA4 activity. 1 Publication	1
Mutagenesisⁱ	140	H → Q: Aminopeptidase activity almost absent, but keeps LTA4 activity. 1 Publication	1
Mutagenesisⁱ	269	G → A: No loss of activity. 1 Publication	1
Mutagenesisⁱ	270	G → A: No loss of activity. 1 Publication	1
Mutagenesisⁱ	271	M → L: No loss of activity. 1 Publication	1
Mutagenesisⁱ	272	E → A or D: Complete loss of activity. 1 Publication	1
Mutagenesisⁱ	272	E → Q: Loss of LTA4 activity, and aminopeptidase activity strongly impaired. 1 Publication	1
Mutagenesisⁱ	273	N → A: No loss of activity. 1 Publication	1
Mutagenesisⁱ	296	H → Y: Complete loss of activity. 1 Publication	1
Mutagenesisⁱ	297	E → A: Loss of both activities. 3 Publications	1
Mutagenesisⁱ	297	E → K: Loss of both activities. 3 Publications	1
Mutagenesisⁱ	297	E → Q: Loss of aminopeptidase activity, but keeps LTA4 activity. 3 Publications	1
Mutagenesisⁱ	300	H → L: Complete loss of activity. 1 Publication	1
Mutagenesisⁱ	319	E → A: Complete loss of activity. 1 Publication	1
Mutagenesisⁱ	372	D → N: No loss of activity. 1 Publication	1
Mutagenesisⁱ	374	D → N: No loss of activity. 1 Publication	1
Mutagenesisⁱ	376	D → A: Strongly reduced hydrolysis of peptides starting with Arg. Small effect on hydrolysis of peptides starting with Ala. Strongly reduced epoxide hydrolase activity. 2 Publications	1
Mutagenesisⁱ	376	D → E: Strongly reduced aminopeptidase activity. Abolishes epoxide hydrolase activity. 2 Publications	1
Mutagenesisⁱ	376	D → N: Abolishes aminopeptidase and epoxide hydrolase activity. 2 Publications	1
Mutagenesisⁱ	385	E → Q: Reduced aminopeptidase activity. Minor effect on epoxide hydrolase activity. 1 Publication	1
Mutagenesisⁱ	564	R → A, K or M: Abolishes epoxide hydrolase activity. Reduced aminopeptidase activity. 1 Publication	1
Mutagenesisⁱ	566	K → A or M: Strongly reduced affinity for peptide substrates. Reduced epoxide hydrolase and aminopeptidase activity. 1 Publication	1
Mutagenesisⁱ	566	K → R: No effect on epoxide hydrolase and aminopeptidase activity. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	4048
Open Targets More...OpenTargetsⁱ	ENSG00000111144
PharmGKBⁱ	PA24345

Chemistry databases

ChEMBLⁱ	CHEMBL4618
Drug and drug target database More...DrugBankⁱ	DB07102 (2S)-2-amino-5-oxo-5-[(4-phenylmethoxyphenyl)amino]pentanoic acid DB06917 (4-fluorophenyl)(pyridin-4-yl)methanone DB07258 (R)-pyridin-4-yl[4-(2-pyrrolidin-1-ylethoxy)phenyl]methanol DB07259 1-(4-thiophen-2-ylphenyl)methanamine DB02352 3-(Benzyloxy)Pyridin-2-Amine DB07104 4-amino-N-[4-(benzyloxy)phenyl]butanamide DB06828 5-[2-(1H-pyrrol-1-yl)ethoxy]-1H-indole DB01197 Captopril DB05745 CHR-2797 DB05177 DG051 DB06851 N-(pyridin-3-ylmethyl)aniline DB08040 N-[(2R)-2-benzyl-4-(hydroxyamino)-4-oxobutanoyl]-L-alanine DB07099 N-[4-(benzyloxy)phenyl]glycinamide DB07260 N-benzyl-4-[(2R)-pyrrolidin-2-ylmethoxy]aniline DB07196 N-methyl-1-(2-thiophen-2-ylphenyl)methanamine DB03424 Ubenimex DB07237 {4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanone
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	1395

Polymorphism and mutation databases

BioMutaⁱ	LTA4H
DMDMⁱ	126353

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources2 Publications
ChainⁱPRO_0000095124	2 – 611	Leukotriene A-4 hydrolaseAdd BLAST		610

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	73	N6-acetyllysineCombined sources	1
Modified residueⁱ	337	N6-acetyllysineCombined sources	1
Modified residueⁱ	414	N6-acetyllysineCombined sources	1
Modified residueⁱ	416	Phosphoserine1 Publication	1
Modified residueⁱ	573	N6-acetyllysineCombined sources	1

Post-translational modificationⁱ

Phosphorylation at Ser-416 inhibits enzymatic activity.1 Publication

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	P09960
jPOSTⁱ	P09960
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P09960
PaxDbⁱ	P09960
PeptideAtlas More...PeptideAtlasⁱ	P09960
PRIDEⁱ	P09960
ProteomicsDBⁱ	52284 52285 [P09960-2] 52286 [P09960-3]

2D gel databases

REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00219077

REPRODUCTION-2DPAGEⁱ

IPI00219077

PTM databases

iPTMnetⁱ	P09960
PhosphoSitePlusⁱ	P09960
SwissPalmⁱ	P09960

Expressionⁱ

Tissue specificityⁱ

Isoform 1 and isoform 2 are expressed in monocytes, lymphocytes, neutrophils, reticulocytes, platelets and fibroblasts.

Gene expression databases

Bgeeⁱ	ENSG00000111144 Expressed in 233 organ(s), highest expression level in visceral pleura
ExpressionAtlasⁱ	P09960 baseline and differential
Genevisibleⁱ	P09960 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB015221 HPA008399 HPA017017

HPAⁱ

CAB015221
HPA008399
HPA017017

Interactionⁱ

Subunit structureⁱ

Monomer.3 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
TINF2	Q9BSI4	2	EBI-721089,EBI-717399

With

Entry

#Exp.

IntAct

Notes

TINF2

Q9BSI4

2

EBI-721089,EBI-717399

Protein-protein interaction databases

BioGridⁱ	110226, 24 interactors
IntActⁱ	P09960, 7 interactors
STRINGⁱ	9606.ENSP00000228740

Chemistry databases

BindingDBⁱ

P09960

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	14 – 16	Combined sources	3
Beta strandⁱ	17 – 29	Combined sources	13
Turnⁱ	30 – 33	Combined sources	4
Beta strandⁱ	34 – 45	Combined sources	12
Beta strandⁱ	50 – 59	Combined sources	10
Beta strandⁱ	61 – 67	Combined sources	7
Beta strandⁱ	74 – 76	Combined sources	3
Helixⁱ	81 – 83	Combined sources	3
Beta strandⁱ	85 – 95	Combined sources	11
Beta strandⁱ	100 – 108	Combined sources	9
Beta strandⁱ	116 – 119	Combined sources	4
Helixⁱ	121 – 123	Combined sources	3
Beta strandⁱ	124 – 129	Combined sources	6
Beta strandⁱ	131 – 134	Combined sources	4
Turnⁱ	137 – 140	Combined sources	4
Helixⁱ	141 – 143	Combined sources	3
Beta strandⁱ	155 – 164	Combined sources	10
Beta strandⁱ	167 – 180	Combined sources	14
Beta strandⁱ	182 – 184	Combined sources	3
Beta strandⁱ	187 – 198	Combined sources	12
Helixⁱ	200 – 202	Combined sources	3
Beta strandⁱ	205 – 209	Combined sources	5
Beta strandⁱ	211 – 216	Combined sources	6
Beta strandⁱ	219 – 223	Combined sources	5
Helixⁱ	225 – 227	Combined sources	3
Helixⁱ	228 – 234	Combined sources	7
Turnⁱ	235 – 237	Combined sources	3
Helixⁱ	238 – 249	Combined sources	12
Beta strandⁱ	253 – 255	Combined sources	3
Beta strandⁱ	258 – 261	Combined sources	4
Beta strandⁱ	267 – 271	Combined sources	5
Beta strandⁱ	276 – 279	Combined sources	4
Helixⁱ	281 – 283	Combined sources	3
Beta strandⁱ	286 – 288	Combined sources	3
Turnⁱ	289 – 291	Combined sources	3
Helixⁱ	292 – 299	Combined sources	8
Turnⁱ	300 – 302	Combined sources	3
Turnⁱ	304 – 306	Combined sources	3
Beta strandⁱ	307 – 311	Combined sources	5
Helixⁱ	312 – 314	Combined sources	3
Helixⁱ	315 – 334	Combined sources	20
Helixⁱ	336 – 357	Combined sources	22
Helixⁱ	362 – 364	Combined sources	3
Beta strandⁱ	365 – 367	Combined sources	3
Helixⁱ	375 – 378	Combined sources	4
Helixⁱ	382 – 398	Combined sources	17
Helixⁱ	401 – 415	Combined sources	15
Beta strandⁱ	418 – 420	Combined sources	3
Helixⁱ	422 – 432	Combined sources	11
Helixⁱ	434 – 436	Combined sources	3
Helixⁱ	437 – 441	Combined sources	5
Helixⁱ	445 – 450	Combined sources	6
Turnⁱ	464 – 466	Combined sources	3
Helixⁱ	467 – 478	Combined sources	12
Helixⁱ	481 – 486	Combined sources	6
Helixⁱ	489 – 492	Combined sources	4
Helixⁱ	497 – 508	Combined sources	12
Helixⁱ	515 – 525	Combined sources	11
Helixⁱ	527 – 529	Combined sources	3
Helixⁱ	533 – 545	Combined sources	13
Helixⁱ	551 – 561	Combined sources	11
Helixⁱ	565 – 577	Combined sources	13
Helixⁱ	579 – 592	Combined sources	14
Helixⁱ	593 – 595	Combined sources	3
Helixⁱ	598 – 608	Combined sources	11

Show more details

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1GW6	X-ray	2.20	A	2-611	[»]
	1H19	X-ray	2.10	A	2-611	[»]
	1HS6	X-ray	1.95	A	1-611	[»]
	1SQM	X-ray	2.30	A	2-611	[»]
	2R59	X-ray	1.89	A	2-611	[»]
	2VJ8	X-ray	1.80	A	1-611	[»]
	3B7R	X-ray	1.81	L	2-611	[»]
	3B7S	X-ray	1.47	A	2-611	[»]
	3B7T	X-ray	2.30	A	2-611	[»]
	3B7U	X-ray	1.90	X	2-611	[»]
	3CHO	X-ray	1.80	A	2-611	[»]
	3CHP	X-ray	2.10	A	2-611	[»]
	3CHQ	X-ray	2.09	A	2-611	[»]
	3CHR	X-ray	2.20	A	2-611	[»]
	3CHS	X-ray	2.55	A	2-611	[»]
	3FH5	X-ray	1.63	A	1-611	[»]
	3FH7	X-ray	2.05	A	1-611	[»]
	3FH8	X-ray	1.67	A	1-611	[»]
	3FHE	X-ray	2.16	A	1-611	[»]
	3FTS	X-ray	2.33	A	1-611	[»]
	3FTU	X-ray	1.90	A	1-611	[»]
	3FTV	X-ray	1.70	A	1-611	[»]
	3FTW	X-ray	1.85	A	1-611	[»]
	3FTX	X-ray	1.96	A	1-611	[»]
	3FTY	X-ray	2.15	A	1-611	[»]
	3FTZ	X-ray	2.00	A	1-611	[»]
	3FU0	X-ray	1.80	A	1-611	[»]
	3FU3	X-ray	2.00	A	1-611	[»]
	3FU5	X-ray	2.30	A	1-611	[»]
	3FU6	X-ray	2.05	A	1-611	[»]
	3FUD	X-ray	2.20	A	1-611	[»]
	3FUE	X-ray	2.38	A	1-611	[»]
	3FUF	X-ray	2.60	A	1-611	[»]
	3FUH	X-ray	1.80	A	1-611	[»]
	3FUI	X-ray	2.20	A	1-611	[»]
	3FUJ	X-ray	1.90	A	1-611	[»]
	3FUK	X-ray	1.95	A	1-611	[»]
	3FUL	X-ray	2.39	A	1-611	[»]
	3FUM	X-ray	2.15	A	1-611	[»]
	3FUN	X-ray	1.58	A	1-611	[»]
	3U9W	X-ray	1.25	A	4-611	[»]
	4DPR	X-ray	2.02	A	1-611	[»]
	4L2L	X-ray	1.65	A	1-611	[»]
	4MKT	X-ray	1.62	A	1-611	[»]
	4MS6	X-ray	1.72	A	1-611	[»]
	4R7L	X-ray	1.66	A	1-611	[»]
	4RSY	X-ray	1.93	A	1-611	[»]
	4RVB	X-ray	1.93	A	1-611	[»]
	5AEN	X-ray	1.86	A	4-611	[»]
	5BPP	X-ray	2.03	A	1-611	[»]
	5FWQ	X-ray	2.05	A	1-611	[»]
	5N3W	X-ray	2.30	A	1-611	[»]
	5NI2	X-ray	1.50	A	2-611	[»]
	5NI4	X-ray	1.90	A/B/C	2-611	[»]
	5NI6	X-ray	1.54	A	2-611	[»]
	5NIA	X-ray	1.76	A	2-611	[»]
	5NID	X-ray	1.57	A	2-611	[»]
	5NIE	X-ray	2.60	A/B/C	2-611	[»]
	6ENB	X-ray	1.84	A	2-611	[»]
	6ENC	X-ray	1.95	A	2-611	[»]
	6END	X-ray	2.24	A	2-611	[»]
ProteinModelPortalⁱ	P09960
SMRⁱ	P09960
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P09960

EvolutionaryTraceⁱ

P09960

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	135 – 137	Substrate binding1 Publication	3
Regionⁱ	267 – 272	Substrate binding1 Publication	6
Regionⁱ	564 – 566	Substrate binding1 Publication	3

Sequence similaritiesⁱ

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

eggNOGⁱ	KOG1047 Eukaryota COG0308 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000156375
HOGENOMⁱ	HOG000293296
HOVERGENⁱ	HBG001274
InParanoidⁱ	P09960
KEGG Orthology (KO) More...KOⁱ	K01254
OMAⁱ	NSNFRMK
Database of Orthologous Groups More...OrthoDBⁱ	481627at2759
PhylomeDBⁱ	P09960
TreeFamⁱ	TF300758

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd09599 M1_LTA4H, 1 hit
Gene3Dⁱ	1.10.390.10, 1 hit 1.25.40.320, 1 hit
InterProⁱ	View protein in InterPro 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	PTHR11533 PTHR11533, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF09127 Leuk-A4-hydro_C, 1 hit PF01433 Peptidase_M1, 1 hit
PRINTSⁱ	PR00756 ALADIPTASE
SMARTⁱ	View protein in SMART SM01263 Leuk-A4-hydro_C, 1 hit
SUPFAMⁱ	SSF48371 SSF48371, 1 hit
TIGRFAMsⁱ	TIGR02411 leuko_A4_hydro, 1 hit
PROSITEⁱ	View protein in PROSITE PS00142 ZINC_PROTEASE, 1 hit

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

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

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform 1 (identifier: P09960-1) [UniParc]FASTA Add to basket

Also known as: L-LTA4

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
MPEIVDTCSL ASPASVCRTK HLHLRCSVDF TRRTLTGTAA LTVQSQEDNL 
        60         70         80         90        100
RSLVLDTKDL TIEKVVINGQ EVKYALGERQ SYKGSPMEIS LPIALSKNQE 
       110        120        130        140        150
IVIEISFETS PKSSALQWLT PEQTSGKEHP YLFSQCQAIH CRAILPCQDT 
       160        170        180        190        200
PSVKLTYTAE VSVPKELVAL MSAIRDGETP DPEDPSRKIY KFIQKVPIPC 
       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 FNALGGWGEL 
       360        370        380        390        400
QNSVKTFGET HPFTKLVVDL TDIDPDVAYS SVPYEKGFAL LFYLEQLLGG 
       410        420        430        440        450
PEIFLGFLKA YVEKFSYKSI TTDDWKDFLY SYFKDKVDVL NQVDWNAWLY 
       460        470        480        490        500
SPGLPPIKPN YDMTLTNACI ALSQRWITAK EDDLNSFNAT DLKDLSSHQL 
       510        520        530        540        550
NEFLAQTLQR APLPLGHIKR MQEVYNFNAI NNSEIRFRWL RLCIQSKWED 
       560        570        580        590        600
AIPLALKMAT EQGRMKFTRP LFKDLAAFDK SHDQAVRTYQ EHKASMHPVT 
       610 
AMLVGKDLKV D

Length:611

Mass (Da):69,285

Last modified:January 23, 2007 - v2

Checksum:ⁱ329BF6D04D4A06E1

GO

Isoform 2 (identifier: P09960-2) [UniParc]FASTA Add to basket

Also known as: S-LTA4

The sequence of this isoform differs from the canonical sequence as follows:
511-532: APLPLGHIKRMQEVYNFNAINN → MAAALHSIQVGGRNSFGAKDGN
533-611: Missing.

« Hide

        10         20         30         40         50
MPEIVDTCSL ASPASVCRTK HLHLRCSVDF TRRTLTGTAA LTVQSQEDNL 
        60         70         80         90        100
RSLVLDTKDL TIEKVVINGQ EVKYALGERQ SYKGSPMEIS LPIALSKNQE 
       110        120        130        140        150
IVIEISFETS PKSSALQWLT PEQTSGKEHP YLFSQCQAIH CRAILPCQDT 
       160        170        180        190        200
PSVKLTYTAE VSVPKELVAL MSAIRDGETP DPEDPSRKIY KFIQKVPIPC 
       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 FNALGGWGEL 
       360        370        380        390        400
QNSVKTFGET HPFTKLVVDL TDIDPDVAYS SVPYEKGFAL LFYLEQLLGG 
       410        420        430        440        450
PEIFLGFLKA YVEKFSYKSI TTDDWKDFLY SYFKDKVDVL NQVDWNAWLY 
       460        470        480        490        500
SPGLPPIKPN YDMTLTNACI ALSQRWITAK EDDLNSFNAT DLKDLSSHQL 
       510        520        530 
NEFLAQTLQR MAAALHSIQV GGRNSFGAKD GN

Show »

Length:532

Mass (Da):59,733

Checksum:ⁱ474891F08B0215A8

GO

Isoform 3 (identifier: P09960-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MPEIVDTCSL...QSQEDNLRSL → MLPQRNLSKRQVPTMHIPVKTRRLLAALK
     511-532: APLPLGHIKRMQEVYNFNAINN → MAAALHSIQVGGRNSFGAKDGN
     533-611: Missing.

« Hide

        10         20         30         40         50
MLPQRNLSKR QVPTMHIPVK TRRLLAALKV LDTKDLTIEK VVINGQEVKY 
        60         70         80         90        100
ALGERQSYKG SPMEISLPIA LSKNQEIVIE ISFETSPKSS ALQWLTPEQT 
       110        120        130        140        150
SGKEHPYLFS QCQAIHCRAI LPCQDTPSVK LTYTAEVSVP KELVALMSAI 
       160        170        180        190        200
RDGETPDPED PSRKIYKFIQ KVPIPCYLIA LVVGALESRQ IGPRTLVWSE 
       210        220        230        240        250
KEQVEKSAYE FSETESMLKI AEDLGGPYVW GQYDLLVLPP SFPYGGMENP 
       260        270        280        290        300
CLTFVTPTLL AGDKSLSNVI AHEISHSWTG NLVTNKTWDH FWLNEGHTVY 
       310        320        330        340        350
LERHICGRLF GEKFRHFNAL GGWGELQNSV KTFGETHPFT KLVVDLTDID 
       360        370        380        390        400
PDVAYSSVPY EKGFALLFYL EQLLGGPEIF LGFLKAYVEK FSYKSITTDD 
       410        420        430        440        450
WKDFLYSYFK DKVDVLNQVD WNAWLYSPGL PPIKPNYDMT LTNACIALSQ 
       460        470        480        490        500
RWITAKEDDL NSFNATDLKD LSSHQLNEFL AQTLQRMAAA LHSIQVGGRN 

SFGAKDGN

Show »

Length:508

Mass (Da):57,300

Checksum:ⁱA1CDA72AF83A875C

GO

Isoform 4 (identifier: P09960-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-53: MPEIVDTCSL...QSQEDNLRSL → MLPQRNLSKRQVPTMHIPVKTRRLLAALK

« Hide

        10         20         30         40         50
MLPQRNLSKR QVPTMHIPVK TRRLLAALKV LDTKDLTIEK VVINGQEVKY 
        60         70         80         90        100
ALGERQSYKG SPMEISLPIA LSKNQEIVIE ISFETSPKSS ALQWLTPEQT 
       110        120        130        140        150
SGKEHPYLFS QCQAIHCRAI LPCQDTPSVK LTYTAEVSVP KELVALMSAI 
       160        170        180        190        200
RDGETPDPED PSRKIYKFIQ KVPIPCYLIA LVVGALESRQ IGPRTLVWSE 
       210        220        230        240        250
KEQVEKSAYE FSETESMLKI AEDLGGPYVW GQYDLLVLPP SFPYGGMENP 
       260        270        280        290        300
CLTFVTPTLL AGDKSLSNVI AHEISHSWTG NLVTNKTWDH FWLNEGHTVY 
       310        320        330        340        350
LERHICGRLF GEKFRHFNAL GGWGELQNSV KTFGETHPFT KLVVDLTDID 
       360        370        380        390        400
PDVAYSSVPY EKGFALLFYL EQLLGGPEIF LGFLKAYVEK FSYKSITTDD 
       410        420        430        440        450
WKDFLYSYFK DKVDVLNQVD WNAWLYSPGL PPIKPNYDMT LTNACIALSQ 
       460        470        480        490        500
RWITAKEDDL NSFNATDLKD LSSHQLNEFL AQTLQRAPLP LGHIKRMQEV 
       510        520        530        540        550
YNFNAINNSE IRFRWLRLCI QSKWEDAIPL ALKMATEQGR MKFTRPLFKD 
       560        570        580 
LAAFDKSHDQ AVRTYQEHKA SMHPVTAMLV GKDLKVD

Note: No experimental confirmation available.

Show »

Length:587

Mass (Da):66,852

Checksum:ⁱA70BF2792A0427C7

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	B4DEH5	B4DEH5_HUMAN		Leukotriene A-4 hydrolase Leukotriene A-4 hydrolase (cDNA FLJ51712, moderately similar to Leukotriene A-4 hydrolase)	LTA4H	132	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	115	A → T in BX647158 (PubMed:17974005).Curated	1
Sequence conflictⁱ	123	Q → R in BX647158 (PubMed:17974005).Curated	1
Sequence conflictⁱ	297	E → G in BAG60321 (PubMed:14702039).Curated	1
Sequence conflictⁱ	309	N → S in BX647158 (PubMed:17974005).Curated	1
Sequence conflictⁱ	378	A → V in BX647158 (PubMed:17974005).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_051570	131	Y → H. Corresponds to variant dbSNP:rs45630737Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_041107	1 – 53	MPEIV…NLRSL → MLPQRNLSKRQVPTMHIPVK TRRLLAALK in isoform 3 and isoform 4. 2 PublicationsAdd BLAST	53
Alternative sequenceⁱVSP_041108	511 – 532	APLPL…NAINN → MAAALHSIQVGGRNSFGAKD GN in isoform 2 and isoform 3. 1 PublicationAdd BLAST	22
Alternative sequenceⁱVSP_041109	533 – 611	Missing in isoform 2 and isoform 3. 1 PublicationAdd BLAST	79

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J03459 mRNA Translation: AAA36176.1 J02959 mRNA Translation: AAA36177.1 U27293 U27292 Genomic DNA Translation: AAA89077.1 AK298017 mRNA Translation: BAG60321.1 CR457068 mRNA Translation: CAG33349.1 BX647158 mRNA No translation available. AC007298 Genomic DNA No translation available. CH471054 Genomic DNA Translation: EAW97559.1 BC032528 mRNA Translation: AAH32528.1 U43410 Genomic DNA No translation available. U43411 Genomic DNA No translation available.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS58266.1 [P09960-3] CCDS58267.1 [P09960-4] CCDS9059.1 [P09960-1]
PIRⁱ	S65947
NCBI Reference Sequences More...RefSeqⁱ	NP_000886.1, NM_000895.2 [P09960-1] NP_001243572.1, NM_001256643.1 [P09960-4] NP_001243573.1, NM_001256644.1 [P09960-3] XP_005268928.1, XM_005268871.1 [P09960-2]
UniGeneⁱ	Hs.524648

Genome annotation databases

Ensemblⁱ	ENST00000228740; ENSP00000228740; ENSG00000111144 [P09960-1] ENST00000413268; ENSP00000395051; ENSG00000111144 [P09960-3] ENST00000552789; ENSP00000449958; ENSG00000111144 [P09960-4]
GeneIDⁱ	4048
KEGGⁱ	hsa:4048
UCSC genome browser More...UCSCⁱ	uc001ten.3 human [P09960-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P09960	Leukotriene A(4) hydrolase		HUMAN		611	UniRef100_P09960
Leukotriene A(4) hydrolase		PANTR		611
Leukotriene A4 hydrolase		PANPA		149
LTA4H protein		HUMAN		149
UPI000859AD57		HUMAN		633
+2
P09960-2	Leukotriene A(4) hydrolase		PANTR		532	UniRef100_A0A2J8N0M9
P09960-3	Leukotriene A(4) hydrolase		PANTR		508	UniRef100_A0A2I3TUJ2

Protein	Similar proteins		Species	Score	Length	Source
P09960	Leukotriene A(4) hydrolase		HUMAN		611	UniRef90_P09960
Leukotriene A(4) hydrolase		PANTR		611
Leukotriene A4 hydrolase		PANPA		149
Leukotriene A(4) hydrolase		CANLF		701
Leukotriene A(4) hydrolase		CALJA		625
+157
P09960-2	Leukotriene A(4) hydrolase		PROCO		479	UniRef90_A0A2K6F7K7
Leukotriene A(4) hydrolase (Fragment)		MUSPF		557
Leukotriene A(4) hydrolase		PANTR		532
UPI000C9FB5D7		OCTDE		598
UPI00042ADB5B		PERMB		545
+24
P09960-3	Leukotriene A(4) hydrolase		PANTR		508	UniRef90_A0A2I3TUJ2
Leukotriene A(4) hydrolase		RHIBE		586
Leukotriene A(4) hydrolase		AOTNA		574
Leukotriene A(4) hydrolase		Cebus capucinus imitator		564
Leukotriene A(4) hydrolase		HUMAN		561
+13

Protein	Similar proteins		Species	Score	Length	Source
P09960	Leukotriene A(4) hydrolase		HUMAN		611	UniRef50_P09960
Leukotriene A(4) hydrolase		PANTR		611
Leukotriene A4 hydrolase		PANPA		149
Leukotriene A(4) hydrolase		CANLF		701
Leukotriene A(4) hydrolase		CALJA		625
+459
P09960-2	Leukotriene A(4) hydrolase		PANTR		508	UniRef50_A0A2I3TUJ2
Isoform 3 of Leukotriene A-4 hydrolase		HUMAN		508
Leukotriene A(4) hydrolase		RHIBE		586
Leukotriene A(4) hydrolase		AOTNA		574
Leukotriene A(4) hydrolase		Cebus capucinus imitator		564
+92
P09960-3	Leukotriene A(4) hydrolase		PANTR		508	UniRef50_A0A2I3TUJ2
Leukotriene A(4) hydrolase		RHIBE		586
Leukotriene A(4) hydrolase		AOTNA		574
Leukotriene A(4) hydrolase		Cebus capucinus imitator		564
Leukotriene A(4) hydrolase		HUMAN		561
+92

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J03459 mRNA Translation: AAA36176.1 J02959 mRNA Translation: AAA36177.1 U27293 U27292 Genomic DNA Translation: AAA89077.1 AK298017 mRNA Translation: BAG60321.1 CR457068 mRNA Translation: CAG33349.1 BX647158 mRNA No translation available. AC007298 Genomic DNA No translation available. CH471054 Genomic DNA Translation: EAW97559.1 BC032528 mRNA Translation: AAH32528.1 U43410 Genomic DNA No translation available. U43411 Genomic DNA No translation available.
CCDSⁱ	CCDS58266.1 [P09960-3] CCDS58267.1 [P09960-4] CCDS9059.1 [P09960-1]
PIRⁱ	S65947
RefSeqⁱ	NP_000886.1, NM_000895.2 [P09960-1] NP_001243572.1, NM_001256643.1 [P09960-4] NP_001243573.1, NM_001256644.1 [P09960-3] XP_005268928.1, XM_005268871.1 [P09960-2]
UniGeneⁱ	Hs.524648

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1GW6	X-ray	2.20	A	2-611	[»]
	1H19	X-ray	2.10	A	2-611	[»]
	1HS6	X-ray	1.95	A	1-611	[»]
	1SQM	X-ray	2.30	A	2-611	[»]
	2R59	X-ray	1.89	A	2-611	[»]
	2VJ8	X-ray	1.80	A	1-611	[»]
	3B7R	X-ray	1.81	L	2-611	[»]
	3B7S	X-ray	1.47	A	2-611	[»]
	3B7T	X-ray	2.30	A	2-611	[»]
	3B7U	X-ray	1.90	X	2-611	[»]
	3CHO	X-ray	1.80	A	2-611	[»]
	3CHP	X-ray	2.10	A	2-611	[»]
	3CHQ	X-ray	2.09	A	2-611	[»]
	3CHR	X-ray	2.20	A	2-611	[»]
	3CHS	X-ray	2.55	A	2-611	[»]
	3FH5	X-ray	1.63	A	1-611	[»]
	3FH7	X-ray	2.05	A	1-611	[»]
	3FH8	X-ray	1.67	A	1-611	[»]
	3FHE	X-ray	2.16	A	1-611	[»]
	3FTS	X-ray	2.33	A	1-611	[»]
	3FTU	X-ray	1.90	A	1-611	[»]
	3FTV	X-ray	1.70	A	1-611	[»]
	3FTW	X-ray	1.85	A	1-611	[»]
	3FTX	X-ray	1.96	A	1-611	[»]
	3FTY	X-ray	2.15	A	1-611	[»]
	3FTZ	X-ray	2.00	A	1-611	[»]
	3FU0	X-ray	1.80	A	1-611	[»]
	3FU3	X-ray	2.00	A	1-611	[»]
	3FU5	X-ray	2.30	A	1-611	[»]
	3FU6	X-ray	2.05	A	1-611	[»]
	3FUD	X-ray	2.20	A	1-611	[»]
	3FUE	X-ray	2.38	A	1-611	[»]
	3FUF	X-ray	2.60	A	1-611	[»]
	3FUH	X-ray	1.80	A	1-611	[»]
	3FUI	X-ray	2.20	A	1-611	[»]
	3FUJ	X-ray	1.90	A	1-611	[»]
	3FUK	X-ray	1.95	A	1-611	[»]
	3FUL	X-ray	2.39	A	1-611	[»]
	3FUM	X-ray	2.15	A	1-611	[»]
	3FUN	X-ray	1.58	A	1-611	[»]
	3U9W	X-ray	1.25	A	4-611	[»]
	4DPR	X-ray	2.02	A	1-611	[»]
	4L2L	X-ray	1.65	A	1-611	[»]
	4MKT	X-ray	1.62	A	1-611	[»]
	4MS6	X-ray	1.72	A	1-611	[»]
	4R7L	X-ray	1.66	A	1-611	[»]
	4RSY	X-ray	1.93	A	1-611	[»]
	4RVB	X-ray	1.93	A	1-611	[»]
	5AEN	X-ray	1.86	A	4-611	[»]
	5BPP	X-ray	2.03	A	1-611	[»]
	5FWQ	X-ray	2.05	A	1-611	[»]
	5N3W	X-ray	2.30	A	1-611	[»]
	5NI2	X-ray	1.50	A	2-611	[»]
	5NI4	X-ray	1.90	A/B/C	2-611	[»]
	5NI6	X-ray	1.54	A	2-611	[»]
	5NIA	X-ray	1.76	A	2-611	[»]
	5NID	X-ray	1.57	A	2-611	[»]
	5NIE	X-ray	2.60	A/B/C	2-611	[»]
	6ENB	X-ray	1.84	A	2-611	[»]
	6ENC	X-ray	1.95	A	2-611	[»]
	6END	X-ray	2.24	A	2-611	[»]
ProteinModelPortalⁱ	P09960
SMRⁱ	P09960
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	110226, 24 interactors
IntActⁱ	P09960, 7 interactors
STRINGⁱ	9606.ENSP00000228740

Chemistry databases

BindingDBⁱ	P09960
ChEMBLⁱ	CHEMBL4618
DrugBankⁱ	DB07102 (2S)-2-amino-5-oxo-5-[(4-phenylmethoxyphenyl)amino]pentanoic acid DB06917 (4-fluorophenyl)(pyridin-4-yl)methanone DB07258 (R)-pyridin-4-yl[4-(2-pyrrolidin-1-ylethoxy)phenyl]methanol DB07259 1-(4-thiophen-2-ylphenyl)methanamine DB02352 3-(Benzyloxy)Pyridin-2-Amine DB07104 4-amino-N-[4-(benzyloxy)phenyl]butanamide DB06828 5-[2-(1H-pyrrol-1-yl)ethoxy]-1H-indole DB01197 Captopril DB05745 CHR-2797 DB05177 DG051 DB06851 N-(pyridin-3-ylmethyl)aniline DB08040 N-[(2R)-2-benzyl-4-(hydroxyamino)-4-oxobutanoyl]-L-alanine DB07099 N-[4-(benzyloxy)phenyl]glycinamide DB07260 N-benzyl-4-[(2R)-pyrrolidin-2-ylmethoxy]aniline DB07196 N-methyl-1-(2-thiophen-2-ylphenyl)methanamine DB03424 Ubenimex DB07237 {4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanone
GuidetoPHARMACOLOGYⁱ	1395
SwissLipidsⁱ	SLP:000001118

Protein family/group databases

MEROPSⁱ	M01.004
MoonProtⁱ	P09960

PTM databases

iPTMnetⁱ	P09960
PhosphoSitePlusⁱ	P09960
SwissPalmⁱ	P09960

Polymorphism and mutation databases

BioMutaⁱ	LTA4H
DMDMⁱ	126353

2D gel databases

REPRODUCTION-2DPAGEⁱ	IPI00219077

REPRODUCTION-2DPAGEⁱ

IPI00219077

Proteomic databases

EPDⁱ	P09960
jPOSTⁱ	P09960
MaxQBⁱ	P09960
PaxDbⁱ	P09960
PeptideAtlasⁱ	P09960
PRIDEⁱ	P09960
ProteomicsDBⁱ	52284 52285 [P09960-2] 52286 [P09960-3]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	4048
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000228740; ENSP00000228740; ENSG00000111144 [P09960-1] ENST00000413268; ENSP00000395051; ENSG00000111144 [P09960-3] ENST00000552789; ENSP00000449958; ENSG00000111144 [P09960-4]
GeneIDⁱ	4048
KEGGⁱ	hsa:4048
UCSCⁱ	uc001ten.3 human [P09960-1]

Organism-specific databases

CTDⁱ	4048
DisGeNETⁱ	4048
EuPathDBⁱ	HostDB:ENSG00000111144.9
GeneCardsⁱ	LTA4H
HGNCⁱ	HGNC:6710 LTA4H
HPAⁱ	CAB015221 HPA008399 HPA017017
MIMⁱ	151570 gene
neXtProtⁱ	NX_P09960
OpenTargetsⁱ	ENSG00000111144
PharmGKBⁱ	PA24345
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1047 Eukaryota COG0308 LUCA
GeneTreeⁱ	ENSGT00940000156375
HOGENOMⁱ	HOG000293296
HOVERGENⁱ	HBG001274
InParanoidⁱ	P09960
KOⁱ	K01254
OMAⁱ	NSNFRMK
OrthoDBⁱ	481627at2759
PhylomeDBⁱ	P09960
TreeFamⁱ	TF300758

Enzyme and pathway databases

UniPathwayⁱ	UPA00878
BioCycⁱ	MetaCyc:HS03372-MONOMER
BRENDAⁱ	3.3.2.6 2681
Reactomeⁱ	R-HSA-2142691 Synthesis of Leukotrienes (LT) and Eoxins (EX) R-HSA-6798695 Neutrophil degranulation R-HSA-9018676 Biosynthesis of D-series resolvins R-HSA-9018681 Biosynthesis of protectins R-HSA-9018896 Biosynthesis of E-series 18(S)-resolvins R-HSA-9020265 Biosynthesis of aspirin-triggered D-series resolvins R-HSA-9023661 Biosynthesis of E-series 18(R)-resolvins
SABIO-RKⁱ	P09960

Miscellaneous databases

ChiTaRSⁱ	LTA4H human
EvolutionaryTraceⁱ	P09960
GenomeRNAiⁱ	4048
Protein Ontology More...PROⁱ	PR:P09960
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000111144 Expressed in 233 organ(s), highest expression level in visceral pleura
ExpressionAtlasⁱ	P09960 baseline and differential
Genevisibleⁱ	P09960 HS

Family and domain databases

CDDⁱ	cd09599 M1_LTA4H, 1 hit
Gene3Dⁱ	1.10.390.10, 1 hit 1.25.40.320, 1 hit
InterProⁱ	View protein in InterPro 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	PTHR11533 PTHR11533, 1 hit
Pfamⁱ	View protein in Pfam PF09127 Leuk-A4-hydro_C, 1 hit PF01433 Peptidase_M1, 1 hit
PRINTSⁱ	PR00756 ALADIPTASE
SMARTⁱ	View protein in SMART SM01263 Leuk-A4-hydro_C, 1 hit
SUPFAMⁱ	SSF48371 SSF48371, 1 hit
TIGRFAMsⁱ	TIGR02411 leuko_A4_hydro, 1 hit
PROSITEⁱ	View protein in PROSITE PS00142 ZINC_PROTEASE, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	LKHA4_HUMAN
Accessionⁱ	P09960Primary (citable) accession number: P09960 Secondary accession number(s): B4DNQ9 , F8VV40, Q6IAT6, Q9UCT7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	January 23, 2007
	Last modified:	February 13, 2019
	This is version 226 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

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

Documents

Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
Peptidase families
Classification of peptidase families and list of entries
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways

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UniProtKB - P09960 (LKHA4_HUMAN)

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Leukotriene A-4 hydrolase

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<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

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<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'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

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GO - Biological processi

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<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

Organism-specific databases

<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

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Keywords - Cellular componenti

<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

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Organism-specific databases

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Polymorphism and mutation databases

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<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

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Organism-specific databases

<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

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<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

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<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

<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

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Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

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Chemistry databases

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PTM databases

Polymorphism and mutation databases

2D gel databases

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Protocols and materials databases

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Organism-specific databases

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Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

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Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: leukotriene B4 biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ