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P30349 (LKHA4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length610 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 610609Leukotriene A-4 hydrolase
PRO_0000095126

Regions

Region135 – 1373Substrate binding By similarity
Region266 – 2716Substrate binding By similarity
Region563 – 5653Substrate binding By similarity

Sites

Active site2961Proton acceptor By similarity
Active site3831Proton donor By similarity
Metal binding2951Zinc; catalytic By similarity
Metal binding2991Zinc; catalytic By similarity
Metal binding3181Zinc; catalytic By similarity
Site3751Essential for epoxide hydrolase activity, but not for aminopeptidase activity By similarity
Site3781Covalently modified during suicide inhibition by leukotrienes By similarity

Amino acid modifications

Modified residue731N6-acetyllysine By similarity
Modified residue3361N6-acetyllysine By similarity
Modified residue4131N6-acetyllysine By similarity
Modified residue5721N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P30349 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1A1F8DBE20293887

FASTA61069,176
        10         20         30         40         50         60 
MPEVEDTCSL ASPASVCRTQ HLHLRCSVDF ARRALTGTAA LTVQSQEDNL RTLTLDTKDL 

        70         80         90        100        110        120 
TIEKVVINGQ EVKYTLGESQ GYKGSPMEIS LPIALSKNQE VVIEISFETS PKSSALQWLT 

       130        140        150        160        170        180 
PEQTSGKQHP YLFSQWEAIH CRAILPCQDT SVKLTYTAEV SVPKELVALM SAIRDGEAPD 

       190        200        210        220        230        240 
PEDPSRKIYR FNQRVPIPCY LIALVVGALE SRQIGPRTLV WSEKEQVEKS AYEFSETESM 

       250        260        270        280        290        300 
LKIAEDLGGP YVWGQYDLLV LPPSFPYGGM ENPCLTFVTP TLLAGDKSLS NVIAHEISHS 

       310        320        330        340        350        360 
WTGNLVTNKT WDHFWLNEGH TVYLERHICG RLFGEKFRHF HALGGWGELQ NTIKTFGESH 

       370        380        390        400        410        420 
PFTKLVVDLK DVDPDVAYSS IPYEKGFALL FYLEQLLGGP EVFLGFLKAY VEKFSYQSVT 

       430        440        450        460        470        480 
TDDWKSFLYA HFKDKVDLLN QVDWNAWLYA PGLPPVKPNY DVTLTNACIA LSQRWVTAKE 

       490        500        510        520        530        540 
EDLNSFSIED LKDLSSHQLN EFLAQVLQRA PLPLGHIKRM QEVYNFNAIN NSEIRFRWLR 

       550        560        570        580        590        600 
LCIQSKWEEA IPLALKMATE QGRMKFTRPL FKDLAAFDKS HDQAVRTYQE HKACMHPVTA 

       610 
MLVGKDLKVD

« Hide

References

[1]"Molecular cloning and functional expression of rat leukotriene A4 hydrolase using the polymerase chain reaction."
Makita N., Funk C.D., Imai E., Hoover R.L., Badr K.F.
FEBS Lett. 299:273-277(1992) [PubMed: 1544505] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S87522 mRNA. Translation: AAB21778.1.
IPIIPI00207947.
PIRS20444.
UniGeneRn.104990.

3D structure databases

ProteinModelPortalP30349.
SMRP30349. Positions 2-610.
ModBaseSearch...

Protein-protein interaction databases

STRINGP30349.

Protein family/group databases

MEROPSM01.004.

Proteomic databases

PRIDEP30349.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCNM_001030031. rat.

Organism-specific databases

RGD1311333. Lta4h.

Phylogenomic databases

eggNOGroNOG05312.
HOVERGENHBG001274.
InParanoidP30349.
OrthoDBEOG40GCQC.

Enzyme and pathway databases

BRENDA3.3.2.6. 5301.

Gene expression databases

ArrayExpressP30349.
GenevestigatorP30349.
GermOnlineENSRNOG00000004494. Rattus norvegicus.

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. Peptidase_M1. 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...

Entry information

Entry nameLKHA4_RAT
AccessionPrimary (citable) accession number: P30349
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 96 of the entry and version 2 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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