LTA4H report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0043434Biological processresponse to peptide hormone
GO_0019370Biological processleukotriene biosynthetic process
GO_0060509Biological processtype I pneumocyte differentiation
GO_0006508Biological processproteolysis
GO_0010043Biological processresponse to zinc ion
GO_0019538Biological processprotein metabolic process
GO_0006629Biological processlipid metabolic process
GO_0043171Biological processpeptide catabolic process
GO_0005576Cellular componentextracellular region
GO_0070062Cellular componentextracellular exosome
GO_0005654Cellular componentnucleoplasm
GO_1904724Cellular componenttertiary granule lumen
GO_1904813Cellular componentficolin-1-rich granule lumen
GO_0005829Cellular componentcytosol
GO_0005634Cellular componentnucleus
GO_0008233Molecular functionpeptidase activity
GO_0070006Molecular functionmetalloaminopeptidase activity
GO_0045148Molecular functiontripeptide aminopeptidase activity
GO_0004301Molecular functionepoxide hydrolase activity
GO_0008270Molecular functionzinc ion binding
GO_0004177Molecular functionaminopeptidase activity
GO_0003723Molecular functionRNA binding
GO_0004463Molecular functionleukotriene-A4 hydrolase activity
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameLTA4H
Protein nameLeukotriene A4 hydrolase (cDNA FLJ51712, moderately similar to Leukotriene A-4 hydrolase)
LTA4H protein
Leukotriene A-4 hydrolase (LTA-4 hydrolase) (EC 3.3.2.6) (Leukotriene A(4) hydrolase) (Tripeptide aminopeptidase LTA4H) (EC 3.4.11.4)
SynonymsLTA4
DescriptionFUNCTION: 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 pro-inflammatory mediator leukotriene B4 (LTB4) . Has also aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides . In addition to its pro-inflammatory 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 . .

AccessionsENST00000552789.5 [P09960-4]
ENST00000548852.5
ENST00000413268.6 [P09960-3]
Q49AK0
B4DEH5
ENST00000228740.7 [P09960-1]
P09960