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P19602 (LKHA4_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Leukotriene A-4 hydrolase
Short name=LTA-4 hydrolase
EC=3.3.2.6
Alternative name(s):
Leukotriene A(4) hydrolase
Gene names
Name:LTA4H
OrganismCavia porcellus (Guinea pig) [Reference proteome]
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by bestatin. Subject to suicide inhibition by leukotriene A4 By similarity.

Pathway

Lipid metabolism; leukotriene B4 biosynthesis.

Subcellular location

Cytoplasm.

Post-translational modification

Phosphorylation at Ser-416 inhibits enzymatic activity By similarity.

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.3
Chain2 – 611610Leukotriene A-4 hydrolase
PRO_0000095122

Regions

Region135 – 1373Substrate binding By similarity
Region267 – 2726Substrate binding By similarity
Region564 – 5663Substrate binding By similarity

Sites

Active site2971Proton acceptor By similarity
Active site3841Proton donor By similarity
Metal binding2961Zinc; catalytic By similarity
Metal binding3001Zinc; catalytic By similarity
Metal binding3191Zinc; catalytic By similarity
Site3761Essential for epoxide hydrolase activity, but not for aminopeptidase activity By similarity
Site3791Covalently modified during suicide inhibition by leukotrienes By similarity

Amino acid modifications

Modified residue731N6-acetyllysine By similarity
Modified residue3371N6-acetyllysine By similarity
Modified residue4141N6-acetyllysine By similarity
Modified residue4161Phosphoserine By similarity
Modified residue5731N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P19602 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8FBBA08E46B2804A

FASTA61168,971
        10         20         30         40         50         60 
MPEVVDTCSL ASPATVCRTK HLHLRCSVDF TRRALTGVAA LTIQSQEDNL RSLILDTKDL 

        70         80         90        100        110        120 
TIEKVVINGQ EVKYALGEKQ SYKGSPMEIS LPIALSKNQE VVIEISFETS PKSSALQWLT 

       130        140        150        160        170        180 
PEQTSGKEHP YLFSQCQAIH CRAFLPCQDT PSVKLTYTAE VSVPKELVAL MSAIRDGEAP 

       190        200        210        220        230        240 
DPADPSRKIY KFSQKVPIPC YLIALVVGAL ESRKIGPRTL VWSEKEQVDK SAYEFSETES 

       250        260        270        280        290        300 
MLKIAEDLGG PYVWGQYDRL VLPPSFSYGG MENPCLTFVT PTLLAGDKSL SNVIAHEISH 

       310        320        330        340        350        360 
TWTGNLVTNK TWDHFWLNEG HTVYLERHIC GRLFGEKFRH FHALGGWGEL QNTVKTLGET 

       370        380        390        400        410        420 
QAFTKLVVDL TDTDPDVAYS SVPYEKGFAL LFHLEQLLGG PEVFLGFLKA YVEKFSYKSI 

       430        440        450        460        470        480 
TTDDWKNFLF SHFKDKVDIL NQVDWDAWLY SPGLPPIKPN YDMTLTNACI ALSQRWITAK 

       490        500        510        520        530        540 
EKDLNTFSAT DLKDLSSHQV NEFLAQVLQR APLPLGHVKR MQEVYNCNAI NNSEIRFRWL 

       550        560        570        580        590        600 
RLCIQSKWEE AIPLALKMAT EQGRMKFTRP LFKDLAAFDK SHDQAIQTYH AHKASMHPVT 

       610 
AMLVGKDLKV E

« Hide

References

[1]"Amino-acid sequence and tissue distribution of guinea-pig leukotriene A4 hydrolase."
Minami M., Mutoh H., Ohishi N., Honda Z., Bito H., Shimizu T.
Gene 161:249-251(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Hartley.
Tissue: Lung.
[2]"Guinea-pig liver leukotriene A4 hydrolase. Purification, characterization and structural properties."
Haeggstroem J., Bergman T., Joernvall H., Raadmark O.
Eur. J. Biochem. 174:717-724(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Tissue: Liver.
[3]"Leukotriene A4 hydrolase from guinea pig lung: the presence of two catalytically active forms."
Bito H., Ohishi N., Miki I., Minami M., Tanabe T., Shimizu T., Seyama Y.
J. Biochem. 105:261-264(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Strain: Hartley.
Tissue: Lung.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D16669 mRNA. Translation: BAA04077.1.
PIRJC4237.
RefSeqNP_001166450.1. NM_001172979.1.

3D structure databases

ProteinModelPortalP19602.
SMRP19602. Positions 4-610.
ModBaseSearch...

Protein-protein interaction databases

STRING10141.ENSCPOP00000011748.

Protein family/group databases

MEROPSM01.004.

Proteomic databases

PRIDEP19602.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100135571.

Organism-specific databases

CTD4048.

Phylogenomic databases

eggNOGCOG0308.
HOGENOMHOG000293296.
HOVERGENHBG001274.
InParanoidP19602.
OrthoDBEOG40GCQC.

Enzyme and pathway databases

BRENDA3.3.2.6. 1225.
UniPathwayUPA00878.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR012777. Leukotriene_A4_hydrolase.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
SUPFAMSSF48371. ARM-type_fold. 1 hit.
TIGRFAMsTIGR02411. leuko_A4_hydro. 1 hit.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP19602.
ChEMBLCHEMBL5786.

Entry information

Entry nameLKHA4_CAVPO
AccessionPrimary (citable) accession number: P19602
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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