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Database: UniProt
Entry: LKHA4_RAT
LinkDB: LKHA4_RAT
Original site: LKHA4_RAT 
ID   LKHA4_RAT               Reviewed;         610 AA.
AC   P30349;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   14-MAY-2014, entry version 115.
DE   RecName: Full=Leukotriene A-4 hydrolase;
DE            Short=LTA-4 hydrolase;
DE            EC=3.3.2.6;
DE   AltName: Full=Leukotriene A(4) hydrolase;
GN   Name=Lta4h;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1544505; DOI=10.1016/0014-5793(92)80130-9;
RA   Makita N., Funk C.D., Imai E., Hoover R.L., Badr K.F.;
RT   "Molecular cloning and functional expression of rat leukotriene A4
RT   hydrolase using the polymerase chain reaction.";
RL   FEBS Lett. 299:273-277(1992).
CC   -!- FUNCTION: Epoxide hydrolase that catalyzes the final step in the
CC       biosynthesis of the proinflammatory mediator leukotriene B4. Has
CC       also aminopeptidase activity.
CC   -!- CATALYTIC ACTIVITY: (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-
CC       7,9,11,14-tetraenoate + H(2)O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-
CC       dihydroxyicosa-6,8,10,14-tetraenoate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by bestatin. Subject to suicide
CC       inhibition by leukotriene A4 (By similarity).
CC   -!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Phosphorylation at Ser-415 inhibits enzymatic activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
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DR   EMBL; S87522; AAB21778.1; -; mRNA.
DR   PIR; S20444; S20444.
DR   UniGene; Rn.104990; -.
DR   ProteinModelPortal; P30349; -.
DR   SMR; P30349; 2-610.
DR   STRING; 10116.ENSRNOP00000005930; -.
DR   BindingDB; P30349; -.
DR   ChEMBL; CHEMBL2400; -.
DR   MEROPS; M01.004; -.
DR   PaxDb; P30349; -.
DR   PRIDE; P30349; -.
DR   UCSC; RGD:1311333; rat.
DR   RGD; 1311333; Lta4h.
DR   eggNOG; COG0308; -.
DR   HOVERGEN; HBG001274; -.
DR   InParanoid; P30349; -.
DR   BRENDA; 3.3.2.6; 5301.
DR   UniPathway; UPA00878; -.
DR   PRO; PR:P30349; -.
DR   Genevestigator; P30349; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0004301; F:epoxide hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0004463; F:leukotriene-A4 hydrolase activity; IDA:RGD.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0019370; P:leukotriene biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006691; P:leukotriene metabolic process; IDA:RGD.
DR   GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
DR   GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR   GO; GO:0010043; P:response to zinc ion; IEP:RGD.
DR   GO; GO:0060509; P:Type I pneumocyte differentiation; IEP:RGD.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012777; Leukotriene_A4_hydrolase.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR015211; Peptidase_M1_C.
DR   InterPro; IPR014782; Peptidase_M1_N.
DR   PANTHER; PTHR11533; PTHR11533; 1.
DR   Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   TIGRFAMs; TIGR02411; leuko_A4_hydro; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Complete proteome; Cytoplasm; Hydrolase;
KW   Leukotriene biosynthesis; Metal-binding; Metalloprotease;
KW   Phosphoprotein; Protease; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    610       Leukotriene A-4 hydrolase.
FT                                /FTId=PRO_0000095126.
FT   REGION      135    137       Substrate binding (By similarity).
FT   REGION      266    271       Substrate binding (By similarity).
FT   REGION      563    565       Substrate binding (By similarity).
FT   ACT_SITE    296    296       Proton acceptor (By similarity).
FT   ACT_SITE    383    383       Proton donor (By similarity).
FT   METAL       295    295       Zinc; catalytic (By similarity).
FT   METAL       299    299       Zinc; catalytic (By similarity).
FT   METAL       318    318       Zinc; catalytic (By similarity).
FT   SITE        375    375       Essential for epoxide hydrolase activity,
FT                                but not for aminopeptidase activity (By
FT                                similarity).
FT   SITE        378    378       Covalently modified during suicide
FT                                inhibition by leukotrienes (By
FT                                similarity).
FT   MOD_RES      73     73       N6-acetyllysine (By similarity).
FT   MOD_RES     336    336       N6-acetyllysine (By similarity).
FT   MOD_RES     413    413       N6-acetyllysine (By similarity).
FT   MOD_RES     415    415       Phosphoserine (By similarity).
FT   MOD_RES     572    572       N6-acetyllysine (By similarity).
SQ   SEQUENCE   610 AA;  69176 MW;  1A1F8DBE20293887 CRC64;
     MPEVEDTCSL ASPASVCRTQ HLHLRCSVDF ARRALTGTAA LTVQSQEDNL RTLTLDTKDL
     TIEKVVINGQ EVKYTLGESQ GYKGSPMEIS LPIALSKNQE VVIEISFETS PKSSALQWLT
     PEQTSGKQHP YLFSQWEAIH CRAILPCQDT SVKLTYTAEV SVPKELVALM SAIRDGEAPD
     PEDPSRKIYR FNQRVPIPCY LIALVVGALE SRQIGPRTLV WSEKEQVEKS AYEFSETESM
     LKIAEDLGGP YVWGQYDLLV LPPSFPYGGM ENPCLTFVTP TLLAGDKSLS NVIAHEISHS
     WTGNLVTNKT WDHFWLNEGH TVYLERHICG RLFGEKFRHF HALGGWGELQ NTIKTFGESH
     PFTKLVVDLK DVDPDVAYSS IPYEKGFALL FYLEQLLGGP EVFLGFLKAY VEKFSYQSVT
     TDDWKSFLYA HFKDKVDLLN QVDWNAWLYA PGLPPVKPNY DVTLTNACIA LSQRWVTAKE
     EDLNSFSIED LKDLSSHQLN EFLAQVLQRA PLPLGHIKRM QEVYNFNAIN NSEIRFRWLR
     LCIQSKWEEA IPLALKMATE QGRMKFTRPL FKDLAAFDKS HDQAVRTYQE HKACMHPVTA
     MLVGKDLKVD
//
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