LTA4H

Functionⁱ

Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities. Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the proinflammatory mediator leukotriene B4 (LTB4) (PubMed:11917124, PubMed:12207002, PubMed:15078870, PubMed:18804029, PubMed:1897988, PubMed:1975494, PubMed:2244921).

Has also aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides (PubMed:20813919, PubMed:18804029).

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) (PubMed:20813919, PubMed:24591641).

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 (PubMed:21206090).

10 Publications

Catalytic activityⁱ

Release of the N-terminal residue from a tripeptide.
5 Publications
Manual assertion based on experiment inⁱ
- Ref.19
  "Regulation of leukotriene A4 hydrolase activity in endothelial cells by phosphorylation."
  Rybina I.V., Liu H., Gor Y., Feinmark S.J.
  J. Biol. Chem. 272:31865-31871(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: PHOSPHORYLATION AT SER-416, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
- Ref.21
  "A critical role for LTA4H in limiting chronic pulmonary neutrophilic inflammation."
  Snelgrove R.J., Jackson P.L., Hardison M.T., Noerager B.D., Kinloch A., Gaggar A., Shastry S., Rowe S.M., Shim Y.M., Hussell T., Blalock J.E.
  Science 330:90-94(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
- Ref.29
  "Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms."
  Rudberg P.C., Tholander F., Thunnissen M.M.G.M., Haeggstroem J.Z.
  J. Biol. Chem. 277:1398-1404(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-611 IN COMPLEX WITH ZINC, ACTIVE SITE, MUTAGENESIS OF GLN-137; GLY-270; MET-271; GLU-272 AND ASN-273, CATALYTIC ACTIVITY, FUNCTION.
- Ref.30
  "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.34
  "Binding of Pro-Gly-Pro at the active site of leukotriene A4 hydrolase/aminopeptidase and development of an epoxide hydrolase selective inhibitor."
  Stsiapanava A., Olsson U., Wan M., Kleinschmidt T., Rutishauser D., Zubarev R.A., Samuelsson B., Rinaldo-Matthis A., Haeggstrom J.Z.
  Proc. Natl. Acad. Sci. U.S.A. 111:4227-4232(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) IN COMPLEX WITH PRO-GLY-PRO ANALOG 4-(4-BENZYLPHENYL)THIAZOL-2-AMINE AND ZINC IONS, CATALYTIC ACTIVITY, FUNCTION.
EC:3.4.11.4

Cofactorⁱ

Zn²⁺5 PublicationsNote: Binds 1 zinc ion per subunit.3 Publications

Activity regulationⁱ

Inhibited by bestatin (PubMed:11175901). The epoxide hydrolase activity is restrained by suicide inactivation that involves binding of LTA4 to Tyr-379 (PubMed:7667299). 4-(4-benzylphenyl)thiazol-2-amine (ARM1) selectively inhibits the epoxide hydrolase activity (PubMed:24591641).3 Publications

Kineticsⁱ

K_M=
1.29 mM for Pro-Gly-Pro
1 Publication
Manual assertion based on experiment inⁱ
Ref.21
"A critical role for LTA4H in limiting chronic pulmonary neutrophilic inflammation."
Snelgrove R.J., Jackson P.L., Hardison M.T., Noerager B.D., Kinloch A., Gaggar A., Shastry S., Rowe S.M., Shim Y.M., Hussell T., Blalock J.E.
Science 330:90-94(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

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 key	Position(s)	DescriptionActions	Length
Siteⁱ	272	Pro-Gly-Pro binding1 Publication	1
Metal bindingⁱ	296	Zinc; catalyticCombined sources8 Publications	1
Active siteⁱ	297	Proton acceptorCombined sources2 Publications1 Publication	1
Metal bindingⁱ	300	Zinc; catalyticCombined sources8 Publications	1
Metal bindingⁱ	319	Zinc; catalyticCombined sources2 Publications	1
Siteⁱ	376	Essential for epoxide hydrolase activity, but not for aminopeptidase activity1 Publication	1
Siteⁱ	379	Covalently modified during suicide inhibition by leukotrienes1 Publication	1
Active siteⁱ	384	Proton donorCombined sources2 Publications1 Publication	1
Siteⁱ	563	Pro-Gly-Pro binding1 Publication	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

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

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS03372-MONOMER
BRENDAⁱ	3.3.2.6, 2681 3.4.11.6, 2681
PathwayCommonsⁱ	P09960
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:3.3.2.68 Publications) Short name: LTA-4 hydrolase Alternative name(s): Leukotriene A(4) hydrolase Tripeptide aminopeptidase LTA4HCurated (EC:3.4.11.45 Publications)
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

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

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 epoxide hydrolase activity and aminopeptidase activity. 1 Publication	1
Mutagenesisⁱ	272	E → Q: Loss of LTA4 hydrolase activity, and aminopeptidase activity strongly impaired. 1 Publication	1
Mutagenesisⁱ	273	N → A: No loss of epoxide hydrolase activity and aminopeptidase activity. 1 Publication	1
Mutagenesisⁱ	296	H → Y: Complete loss of LTA4 hydrolase and peptidase enzyme activities. 1 Publication	1
Mutagenesisⁱ	297	E → A: Loss of epoxide hydrolase and aminopeptidase activities. 3 Publications	1
Mutagenesisⁱ	297	E → K: Loss of epoxide hydrolase and aminopeptidase activities. 3 Publications	1
Mutagenesisⁱ	297	E → Q: Loss of aminopeptidase activity, but keeps LTA4 hydrolase activity. 3 Publications	1
Mutagenesisⁱ	300	H → L: Complete loss of LTA4 hydrolase and peptidase enzyme activities. 1 Publication	1
Mutagenesisⁱ	319	E → A: Complete loss of LTA4 hydrolase and peptidase enzyme activities. 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. Abolishes 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 activity. Decreased 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

Miscellaneous databases

Pharosⁱ	P09960, Tchem

Pharosⁱ

P09960, Tchem

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 DB07094, 1-(2,2'-bithiophen-5-yl)methanamine DB07259, 1-(4-thiophen-2-ylphenyl)methanamine DB02352, 3-(Benzyloxy)Pyridin-2-Amine DB07292, 4-(2-amino-1,3-thiazol-4-yl)phenol DB07104, 4-amino-N-[4-(benzyloxy)phenyl]butanamide DB06828, 5-[2-(1H-pyrrol-1-yl)ethoxy]-1H-indole DB08466, 5-[2-(4-hydroxyphenyl)ethyl]benzene-1,3-diol DB01197, Captopril DB05177, DG051 DB03366, Imidazole DB08040, Kelatorphan DB06851, N-(pyridin-3-ylmethyl)aniline DB02062, N-[3-[(1-Aminoethyl)(Hydroxy)Phosphoryl]-2-(1,1'-Biphenyl-4-Ylmethyl)Propanoyl]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 DB11781, Tosedostat DB03424, Ubenimex DB07237, {4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanone
DrugCentral More...DrugCentralⁱ	P09960
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	1395

Genetic variation 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 leukotriene-A4 hydrolase activity.1 Publication

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal More...CPTACⁱ	CPTAC-92 CPTAC-93
EPDⁱ	P09960
jPOSTⁱ	P09960
MassIVEⁱ	P09960
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P09960
PaxDbⁱ	P09960
PeptideAtlas More...PeptideAtlasⁱ	P09960
PRIDEⁱ	P09960
ProteomicsDBⁱ	28779 52284 [P09960-1] 52285 [P09960-2] 52286 [P09960-3]

2D gel databases

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

REPRODUCTION-2DPAGEⁱ

IPI00219077

PTM databases

GlyGenⁱ	P09960, 2 sites, 1 O-linked glycan (2 sites)
iPTMnetⁱ	P09960
MetOSiteⁱ	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 visceral pleura and 247 other tissues
ExpressionAtlasⁱ	P09960, baseline and differential
Genevisibleⁱ	P09960, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000111144, Low tissue specificity

HPAⁱ

ENSG00000111144, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

Monomer.

3 Publications

Binary interactionsⁱ

P09960

With	#Exp.	IntAct
TINF2 [Q9BSI4]	2	EBI-721089,EBI-717399

Protein-protein interaction databases

BioGRIDⁱ	110226, 38 interactors
IntActⁱ	P09960, 11 interactors
Molecular INTeraction database More...MINTⁱ	P09960
STRINGⁱ	9606.ENSP00000228740

Chemistry databases

BindingDBⁱ

P09960

Miscellaneous databases

RNActⁱ	P09960, protein

RNActⁱ

P09960, protein

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

SMRⁱ	P09960
ModBaseⁱ	Search...
PDBe-KBⁱ	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	362 – 365	Inhibitor ARM1 binding1 Publication	4
Regionⁱ	564 – 566	Substrate binding1 Publication	3

Sequence similaritiesⁱ

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

eggNOGⁱ	KOG1047, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000156375
HOGENOMⁱ	CLU_014505_0_0_1
InParanoidⁱ	P09960
OMAⁱ	CTALQWM
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 2.60.40.1730, 1 hit
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
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
PRINTSⁱ	PR00756, ALADIPTASE
SMARTⁱ	View protein in SMART SM01263, Leuk-A4-hydro_C, 1 hit
SUPFAMⁱ	SSF48371, SSF48371, 1 hit SSF63737, SSF63737, 1 hit
TIGRFAMsⁱ	TIGR02411, leuko_A4_hydro, 1 hit
PROSITEⁱ	View protein in PROSITE PS00142, ZINC_PROTEASE, 1 hit

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 canonicalⁱ 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

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]

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

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
Leukotriene A(4) hydrolase		PANTR		611
LTA4H protein		HUMAN		149
+3
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		OCTDE		598
Leukotriene A(4) hydrolase		MACNE		586
+26
P09960-2	Leukotriene A(4) hydrolase		MUSCR		532	UniRef90_A0A6P7RBL4
Leukotriene A(4) hydrolase		PANTR		532
Leukotriene A(4) hydrolase		OCTDE		532
Leukotriene A(4) hydrolase		MESAU		532
Leukotriene A(4) hydrolase		PERMB		532
+29
P09960-4	Leukotriene A-4 hydrolase		MOUSE		611	UniRef90_P09960-4
Leukotriene A-4 hydrolase		BOVIN		611
Leukotriene A-4 hydrolase		CHILA		611
Leukotriene A-4 hydrolase		RAT		611
Leukotriene A-4 hydrolase		CAVPO		611
+200

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		OCTDE		598
Leukotriene A(4) hydrolase		MACNE		586
+381
P09960-2	Leukotriene A(4) hydrolase		NEMVE		614	UniRef50_A7SS27
Leuk-A4-hydro_C domain-containing protein (Fragment)		BAMTH		525
Leukotriene A4 hydrolase		SAIBB		481
Leukotriene A4 hydrolase		AOTNA		495
Leukotriene A(4) hydrolase		ERIEU		532
+47
P09960-4	Leukotriene A-4 hydrolase		MOUSE		611	UniRef50_P09960-4
Leukotriene A-4 hydrolase		CHILA		611
Leukotriene A-4 hydrolase		RAT		611
Leukotriene A-4 hydrolase		BOVIN		611
Leukotriene A-4 hydrolase		CAVPO		611
+244

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]

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	[»]
	6O5H	X-ray	2.84	A/B/C	4-611	[»]
	7AUZ	X-ray	1.90	A	2-611	[»]
7AV0	X-ray	1.90	A	2-611	[»]
7AV1	X-ray	1.79	A	2-611	[»]
7AV2	X-ray	1.95	A	2-611	[»]
SMRⁱ	P09960
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	110226, 38 interactors
IntActⁱ	P09960, 11 interactors
MINTⁱ	P09960
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 DB07094, 1-(2,2'-bithiophen-5-yl)methanamine DB07259, 1-(4-thiophen-2-ylphenyl)methanamine DB02352, 3-(Benzyloxy)Pyridin-2-Amine DB07292, 4-(2-amino-1,3-thiazol-4-yl)phenol DB07104, 4-amino-N-[4-(benzyloxy)phenyl]butanamide DB06828, 5-[2-(1H-pyrrol-1-yl)ethoxy]-1H-indole DB08466, 5-[2-(4-hydroxyphenyl)ethyl]benzene-1,3-diol DB01197, Captopril DB05177, DG051 DB03366, Imidazole DB08040, Kelatorphan DB06851, N-(pyridin-3-ylmethyl)aniline DB02062, N-[3-[(1-Aminoethyl)(Hydroxy)Phosphoryl]-2-(1,1'-Biphenyl-4-Ylmethyl)Propanoyl]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 DB11781, Tosedostat DB03424, Ubenimex DB07237, {4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanone
DrugCentralⁱ	P09960
GuidetoPHARMACOLOGYⁱ	1395
SwissLipidsⁱ	SLP:000001118

Protein family/group databases

MEROPSⁱ	M01.004
MoonProtⁱ	P09960

PTM databases

GlyGenⁱ	P09960, 2 sites, 1 O-linked glycan (2 sites)
iPTMnetⁱ	P09960
MetOSiteⁱ	P09960
PhosphoSitePlusⁱ	P09960
SwissPalmⁱ	P09960

Genetic variation databases

BioMutaⁱ	LTA4H
DMDMⁱ	126353

2D gel databases

REPRODUCTION-2DPAGEⁱ	IPI00219077

REPRODUCTION-2DPAGEⁱ

IPI00219077

Proteomic databases

CPTACⁱ	CPTAC-92 CPTAC-93
EPDⁱ	P09960
jPOSTⁱ	P09960
MassIVEⁱ	P09960
MaxQBⁱ	P09960
PaxDbⁱ	P09960
PeptideAtlasⁱ	P09960
PRIDEⁱ	P09960
ProteomicsDBⁱ	28779 52284 [P09960-1] 52285 [P09960-2] 52286 [P09960-3]

Protocols and materials databases

Antibodypediaⁱ	4453, 510 antibodies
The DNASU plasmid repository More...DNASUⁱ	4048

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
GeneCardsⁱ	LTA4H
HGNCⁱ	HGNC:6710, LTA4H
HPAⁱ	ENSG00000111144, Low tissue specificity
MIMⁱ	151570, gene
neXtProtⁱ	NX_P09960
OpenTargetsⁱ	ENSG00000111144
PharmGKBⁱ	PA24345
VEuPathDBⁱ	HostDB:ENSG00000111144
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1047, Eukaryota
GeneTreeⁱ	ENSGT00940000156375
HOGENOMⁱ	CLU_014505_0_0_1
InParanoidⁱ	P09960
OMAⁱ	CTALQWM
PhylomeDBⁱ	P09960
TreeFamⁱ	TF300758

Enzyme and pathway databases

UniPathwayⁱ	UPA00878
BioCycⁱ	MetaCyc:HS03372-MONOMER
BRENDAⁱ	3.3.2.6, 2681 3.4.11.6, 2681
PathwayCommonsⁱ	P09960
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

BioGRID-ORCSⁱ	4048, 4 hits in 1020 CRISPR screens
ChiTaRSⁱ	LTA4H, human
EvolutionaryTraceⁱ	P09960
GenomeRNAiⁱ	4048
Pharosⁱ	P09960, Tchem
Protein Ontology More...PROⁱ	PR:P09960
RNActⁱ	P09960, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000111144, Expressed in visceral pleura and 247 other tissues
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 2.60.40.1730, 1 hit
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
PANTHERⁱ	PTHR45726, PTHR45726, 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 SSF63737, SSF63737, 1 hit
TIGRFAMsⁱ	TIGR02411, leuko_A4_hydro, 1 hit
PROSITEⁱ	View protein in PROSITE PS00142, ZINC_PROTEASE, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	LKHA4_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:	September 29, 2021
	This is version 240 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, Direct protein sequencing, Reference proteome

Documents

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

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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

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

<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

Sites

<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

Enzyme and pathway databases

Protein family/group databases

Chemistry databases

<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

Cytoplasm and Cytosol

Cytosol

Extracellular region or secreted

Nucleus

Other locations

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

Mutagenesis

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation 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

Gene expression databases

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

P09960

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<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

3D structure databases

Miscellaneous databases

<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

Phylogenomic databases

Family and domain databases

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

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Genetic variation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

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