Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P24527 (LKHA4_MOUSE)

Last modified October 13, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Leukotriene A-4 hydrolase
    EC=3.3.2.6
Alternative name(s):
    Leukotriene A(4) hydrolase
      Short name=LTA-4 hydrolase
Gene names
Name: Lta4h
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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

Hydrolyzes an epoxide moiety of leukotriene A4 (LTA-4) to form leukotriene B4 (LTB-4). The enzyme also has some peptidase 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.

Pathway

Lipid metabolism; leukotriene B4 biosynthesis.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the peptidase M1 family.

Ontologies

Keywords
   Biological processLeukotriene biosynthesis
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMAcetylation
   Technical termMultifunctional enzyme
Gene Ontology (GO)
   Biological processleukotriene biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionleukotriene-A4 hydrolase activity

Inferred from electronic annotation. Source: EC

metallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 611610Leukotriene A-4 hydrolase
PRO_0000095125

Sites

Active site2971 By similarity
Active site3841Proton donor Potential
Metal binding2961Zinc; catalytic
Metal binding3001Zinc; catalytic
Metal binding3191Zinc; catalytic
Binding site2001Substrate By similarity

Amino acid modifications

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

Experimental info

Mutagenesis2961H → Y: Complete loss of activity. Ref.3
Mutagenesis3001H → Y: Complete loss of activity. Ref.3
Mutagenesis3191E → Q: Complete loss of activity. Ref.3
Sequence conflict5931K → R Ref.1

Sequences

Sequence LengthMass (Da)Tools
P24527-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6CE9C20F630EB4C9

FASTA61169,021
        10         20         30         40         50         60 
MPEVADTCSL ASPASVCRTQ HLHLRCSVDF ARRTLTGTAA LTVQSQEENL RSLTLDTKDL 

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

       130        140        150        160        170        180 
PEQTSGKQHP YLFSQCQAIH CRAILPCQDT PSVKLTYTAE VSVPKELVAL MSAIRDGEAP 

       190        200        210        220        230        240 
DPEDPSRKIY RFNQRVPIPC YLIALVVGAL ESRQIGPRTL VWSEKEQVEK SANEFSETES 

       250        260        270        280        290        300 
MLKIAEDLGG PYVWGQYDLL VLPPSFPYGG MENPCLTFVT PTLLAGDKSL SNVIAHEISH 

       310        320        330        340        350        360 
SWTGNLVTNK TWDHFWLNEG HTVYLERHIC GRLFGEKFRH FHALGGWGEL QNTIKTFGES 

       370        380        390        400        410        420 
HPFTKLVVDL KDVDPDVAYS SIPYEKGFAL LFYLEQLLGG PEVFLGFLKA YVKKFSYQSV 

       430        440        450        460        470        480 
TTDDWKSFLY SHFKDKVDLL NQVDWNAWLY APGLPPVKPN YDVTLTNACI ALSQRWVTAK 

       490        500        510        520        530        540 
EEDLSSFSIA DLKDLSSHQL NEFLAQVLQK APLPLGHIKR MQEVYNFNAI NNSEIRFRWL 

       550        560        570        580        590        600 
RLCIQSKWEE AIPLALKMAT EQGRMKFTRP LFKDLAAFDK SHDQAVHTYQ EHKASMHPVT 

       610 
AMLVGRDLKV D 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of mouse leukotriene A4 hydrolase cDNA."
Medina J.F., Raadmark O., Funk C.D., Haeggstroem J.Z.
Biochem. Biophys. Res. Commun. 176:1516-1524(1991) [PubMed: 1710117] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spleen.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Leukotriene A4 hydrolase: determination of the three zinc-binding ligands by site-directed mutagenesis and zinc analysis."
Medina J.F., Wetterholm A., Raadmark O., Shapiro R., Haeggstroem J.Z., Vallee B.L., Samuelsson B.
Proc. Natl. Acad. Sci. U.S.A. 88:7620-7624(1991) [PubMed: 1881903] [Abstract]
Cited for: MUTAGENESIS OF ZINC LIGANDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

M63848 mRNA. Translation: AAB59675.1. Sequence problems.
BC021417 mRNA. Translation: AAH21417.1.
IPIIPI00229527.
PIRJN0066.
UniGeneMm.271071

3D structure databases

HSSPHSSP built from PDB template 1HS6 based on UniProtKB P09960.
SMRP24527. Positions 2-611.
ModBaseSearch...

Protein-protein interaction databases

STRINGP24527.

Protein family/group databases

MEROPSM01.004.

PTM databases

PhosphoSiteP24527.

Proteomic databases

PRIDEP24527.

Genome annotation databases

EnsemblENSMUST00000016033; ENSMUSP00000016033; ENSMUSG00000015889; Mus musculus. [Genome view]

Organism-specific databases

MGIMGI:96836. Lta4h.

Phylogenomic databases

HOGENOMP24527.
HOVERGENP24527.

Enzyme and pathway databases

BRENDA3.3.2.6. 244.

Gene expression databases

ArrayExpressP24527.
BgeeP24527.
CleanExMM_LTA4H.
GenevestigatorP24527.
GermOnlineENSMUSG00000015889. Mus musculus.

Family and domain databases

InterProIPR012777. Leuk_A4_hydro_aminopept.
IPR006025. Pept_M_Zn_BS.
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.
TIGRFAMsTIGR02411. leuko_A4_hydro. 1 hit.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameLKHA4_MOUSE
AccessionPrimary (citable) accession number: P24527
Secondary accession number(s): Q8VDR8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: October 13, 2009
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents