Reviewed, UniProtKB/Swiss-Prot P19602 (LKHA4_CAVPO)

Names and origin

Protein names

Recommended 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

Organism

Cavia porcellus (Guinea pig)

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	611 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity.
Pathway	Lipid metabolism; leukotriene B4 biosynthesis.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the peptidase M1 family.

Ontologies

Keywords
Biological process	Leukotriene biosynthesis
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Acetylation
Technical term	Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	leukotriene-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2 Ref.3
	Chain	2 – 611	610	Leukotriene A-4 hydrolase		PRO_0000095122
Sites
	Active site	297	1	By similarity
	Active site	384	1	Proton donor Potential
	Metal binding	296	1	Zinc; catalytic By similarity
	Metal binding	300	1	Zinc; catalytic By similarity
	Metal binding	319	1	Zinc; catalytic By similarity
	Binding site	200	1	Substrate By similarity
Amino acid modifications
	Modified residue	73	1	N6-acetyllysine By similarity
	Modified residue	337	1	N6-acetyllysine By similarity
	Modified residue	414	1	N6-acetyllysine By similarity
	Modified residue	573	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P19602-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 8FBBA08E46B2804A	FASTA	611	68,971
	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

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: 7665088] [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: 3391178] [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: 2722767] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21. Strain: Hartley. Tissue: Lung.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D16669 mRNA. Translation: BAA04077.1.
PIR	JC4237.
3D structure databases
HSSP	HSSP built from PDB template 1HS6 based on UniProtKB P09960.
SMR	P19602. Positions 2-611.
ModBase	Search...
Protein family/group databases
MEROPS	M01.004.
Genome annotation databases
Ensembl	ENSCPOT00000013175; ENSCPOP00000011748; ENSCPOG00000013048; Cavia porcellus. [Genome view]
Phylogenomic databases
HOVERGEN	P19602.
Enzyme and pathway databases
BRENDA	3.3.2.6. 44.
Family and domain databases
InterPro	IPR012777. Leuk_A4_hydro_aminopept. IPR006025. Pept_M_Zn_BS. IPR001930. Peptidase_M1. IPR015211. Peptidase_M1_C. IPR014782. Peptidase_M1_N. [Graphical view]
PANTHER	PTHR11533. Peptidase_M1. 1 hit.
Pfam	PF09127. Leuk-A4-hydro_C. 1 hit. PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
TIGRFAMs	TIGR02411. leuko_A4_hydro. 1 hit.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LKHA4_CAVPO

Accession

Primary (citable) accession number: P19602

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)