Leukotriene A-4 hydrolase
Details
- Name
- Leukotriene A-4 hydrolase
- Synonyms
- 3.3.2.6
- Leukotriene A(4) hydrolase
- LTA-4 hydrolase
- LTA4
- Tripeptide aminopeptidase LTA4H
- Gene Name
- LTA4H
- UniProtKB Entry
- P09960Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0003332|Leukotriene A-4 hydrolase MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDL TIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLT PEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETP DPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETES MLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISH SWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGET HPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEIFLGFLKAYVEKFSYKSI TTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAK EDDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWL RLCIQSKWEDAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVT AMLVGKDLKVD
- Number of residues
- 611
- Molecular Weight
- 69284.64
- Theoretical pI
- 6.1
- GO Classification
- FunctionsRNA binding / tripeptide aminopeptidase activityProcesseslipid metabolic process / protein metabolic processComponentsextracellular region / ficolin-1-rich granule lumen / nucleus / tertiary granule lumen
- General Function
- 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) (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:18804029, PubMed:20813919). 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) (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)
- Specific Function
- aminopeptidase activity
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0020556|Leukotriene A-4 hydrolase (LTA4H) ATGCCCGAGATAGTGGATACCTGTTCGTTGGCCTCTCCGGCTTCCGTCTGCCGGACCAAG CACCTGCACCTGCGCTGCAGCGTCGACTTTACTCGCCGGACGCTGACCGGGACTGCTGCT CTCACGGTCCAGTCTCAGGAGGACAATCTGCGCAGCCTGGTTTTGGATACAAAGGACCTT ACAATAGAAAAAGTAGTGATCAATGGACAAGAAGTCAAATATGCTCTTGGAGAAAGACAA AGTTACAAGGGATCGCCAATGGAAATCTCTCTTCCTATCGCTTTGAGCAAAAATCAAGAA ATTGTTATAGAAATTTCTTTTGAGACCTCTCCAAAATCTTCTGCTCTCCAGTGGCTCACT CCTGAACAGACTTCTGGGAAGGAACACCCATATCTCTTTAGTCAGTGCCAGGCCATCCAC TGCAGAGCAATCCTTCCTTGTCAGGACACTCCTTCTGTGAAATTAACCTATACTGCAGAG GTGTCTGTCCCTAAAGAACTGGTGGCACTTATGAGTGCTATTCGTGATGGAGAAACACCT GACCCAGAAGACCCAAGCAGGAAAATATACAAATTCATCCAAAAAGTTCCAATACCCTGC TACCTGATTGCTTTAGTTGTTGGAGCTTTAGAAAGCAGGCAAATTGGCCCAAGAACTTTG GTGTGGTCTGAGAAAGAGCAGGTGGAAAAGTCTGCTTATGAGTTTTCTGAGACTGAATCT ATGCTTAAAATAGCAGAAGATCTGGGAGGACCGTATGTATGGGGACAGTATGACCTATTG GTCCTGCCACCATCCTTCCCTTATGGTGGCATGGAGAATCCTTGCCTTACTTTTGTAACT CCTACTCTACTGGCAGGCGACAAGTCACTCTCCAATGTCATTGCACATGAAATATCTCAT AGCTGGACAGGGAATCTAGTGACCAACAAAACTTGGGATCACTTTTGGTTAAATGAGGGA CATACTGTGTACTTGGAACGCCACATTTGCGGACGATTGTTTGGTGAAAAGTTCAGACAT TTTAATGCTCTGGGAGGATGGGGAGAACTACAGAATTCGGTAAAGACATTTGGGGAGACA CATCCTTTCACCAAACTTGTGGTTGATCTGACAGATATAGACCCTGATGTAGCTTATTCT TCAGTTCCCTATGAGAAGGGCTTTGCTTTACTTTTTTACCTTGAACAACTGCTTGGAGGA CCAGAGATTTTCCTAGGATTCTTAAAAGCTTATGTTGAGAAGTTTTCCTATAAGAGCATA ACTACTGATGACTGGAAGGATTTCCTGTATTCCTATTTTAAAGATAAGGTTGATGTTCTC AATCAAGTTGATTGGAATGCCTGGCTCTACTCTCCTGGACTGCCTCCCATAAAGCCCAAT TATGATATGACTCTGACAAATGCTTGTATTGCCTTAAGTCAAAGATGGATTACTGCCAAA GAAGATGATTTAAATTCATTCAATGCCACAGACCTGAAGGATCTCTCTTCTCATCAATTG AATGAGTTTTTAGCACAGACGCTCCAGAGGGCACCTCTTCCATTGGGGCACATAAAGCGA ATGCAAGAGGTGTACAACTTCAATGCCATTAACAATTCTGAAATACGATTCAGATGGCTG CGGCTCTGCATTCAATCCAAGTGGGAGGACGCAATTCCTTTGGCGCTAAAGATGGCAACT GAACAAGGAAGAATGAAGTTTACCCGGCCCTTATTCAAGGATCTTGCTGCCTTTGACAAA TCCCATGATCAAGCTGTCCGAACCTACCAAGAGCACAAAGCAAGCATGCATCCCGTGACT GCAATGCTGGTGGGGAAAGACTTAAAAGTGGATTAA
- Chromosome Location
- 12
- Locus
- 12q23.1
- External Identifiers
Resource Link UniProtKB ID P09960 UniProtKB Entry Name LKHA4_HUMAN GenBank Protein ID 976396 GenBank Gene ID U27293 GeneCard ID LTA4H GenAtlas ID LTA4H HGNC ID HGNC:6710 PDB ID(s) 1GW6, 1H19, 1HS6, 1SQM, 2R59, 2VJ8, 3B7R, 3B7S, 3B7T, 3B7U, 3CHO, 3CHP, 3CHQ, 3CHR, 3CHS, 3FH5, 3FH7, 3FH8, 3FHE, 3FTS, 3FTU, 3FTV, 3FTW, 3FTX, 3FTY, 3FTZ, 3FU0, 3FU3, 3FU5, 3FU6, 3FUD, 3FUE, 3FUF, 3FUH, 3FUI, 3FUJ, 3FUK, 3FUL, 3FUM, 3FUN, 3U9W, 4DPR, 4L2L, 4MKT, 4MS6, 4R7L, 4RSY, 4RVB, 5AEN, 5BPP, 5FWQ, 5N3W, 5NI2, 5NI4, 5NI6, 5NIA, 5NID, 5NIE, 6ENB, 6ENC, 6END, 6O5H, 7AUZ, 7AV0, 7AV1, 7AV2, 7KZE, 7LLQ, 8AVA, 8AWH, 8QOW, 8QPN, 8QQ4, 8RX3, 8RX7, 8RX9 KEGG ID hsa:4048 IUPHAR/Guide To Pharmacology ID 1395 NCBI Gene ID 4048 - General References
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Associated Data
- Bio-Entities
Bio-Entity Type Leukotriene A-4 hydrolase (Humans) protein primary- Drug Relations