NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Leukocyte;
PubMed=2315307 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshimoto T., Suzuki H., Yamamoto S., Takai T., Yokoyama C., Tanabe T.;
"Cloning and sequence analysis of the cDNA for arachidonate 12-lipoxygenase of porcine leukocytes.";
Proc. Natl. Acad. Sci. U.S.A. 87:2142-2146(1990).

[2]

MUTAGENESIS.
DOI=10.1016/0005-2760(94)90234-8; PubMed=8305485 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki H., Kishimoto K., Yoshimoto T., Yamamoto S., Kanai F., Ebina Y., Miyatake A., Tanabe T.;
"Site-directed mutagenesis studies on the iron-binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase.";
Biochim. Biophys. Acta 1210:308-316(1994).

Comments

FUNCTION: Oxygenase and 14,15-leukotriene A4 synthase activity.
CATALYTIC ACTIVITY: Arachidonate + O₂ = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.
COFACTOR: Binds 1 iron ion per subunit.
PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Leukocytes, pituitary gland, lung and in very small amount in jejunum and spleen.
SIMILARITY: Belongs to the lipoxygenase family.
SIMILARITY: Contains 1 lipoxygenase domain.
SIMILARITY: Contains 1 PLAT domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M31417; AAA31068.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10621; BAA01471.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A35087; A35087.

NP_999096.1; -.

3D structure databases

HSSP

P12530; 1LOX. [HSSP ENTRY / PDB]

SMR

P16469; 2-663.

ModBase

P16469.

Family and domain databases

InterPro

IPR000907; LipOase.
IPR013819; LipOase_C.
IPR001024; LipOase_LH2.
IPR001885; LipOase_mml.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.60.20; Lipase_LipOase; 1.

PANTHER

PTHR11771; LipOase; 1.

Pfam

PF00305; Lipoxygenase; 1.
PF01477; PLAT; 1.
Pfam graphical view of domain structure.

PRINTS

PR00087; LIPOXYGENASE.
PR00467; MAMLPOXGNASE.

SMART

SM00308; LH2; 1.
SMART graphical view of domain structure.

PROSITE

PS00711; LIPOXYGENASE_1; 1.
PS00081; LIPOXYGENASE_2; 1.
PS51393; LIPOXYGENASE_3; 1.
PS50095; PLAT; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P16469.

Genome annotation databases

GeneID

396971; -.

KEGG

ssc:396971; -.

Phylogenomic databases

HOVERGEN

P16469; -.

Other

ProtoNet

P16469.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Dioxygenase; Direct protein sequencing; Iron; Leukotriene biosynthesis; Metal-binding; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 663`	`662`	`Arachidonate 12-lipoxygenase, 12S-type.`	`PRO_0000220684`
`DOMAIN`	`2 115`	`114`	`PLAT.`
`DOMAIN`	`116 663`	`548`	`Lipoxygenase.`
`METAL`	`361 361`		`Iron; catalytic (By similarity).`
`METAL`	`366 366`		`Iron; catalytic (By similarity).`
`METAL`	`541 541`		`Iron; catalytic (By similarity).`
`METAL`	`663 663`		`Iron; via carboxylate; catalytic (By similarity).`

Sequence information

Length: 663 AA [This is the length of the unprocessed precursor]

Molecular weight: 75043 Da [This is the MW of the unprocessed precursor]

CRC64: A06B655D6E6BAA36 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGLYRVRVST GSSFYAGSQN QVQLWLVGQH GEAALGWCLR PARGKETEFS VDVSEYLGPL 

        70         80         90        100        110        120 
LFVKLRKRHL LQDDAWFCNW ISVQGPGANG DEFRFPCYRW VEGDRILSLP EGTARTVVDD 

       130        140        150        160        170        180 
PQGLFKKHRE EELAERRKLY RWGNWKDGLI LNIASTGIHD LPVDERFLED KRIDFEASLA 

       190        200        210        220        230        240 
KGLADLAVKD SLNVLMSWNS LDSFNRIFWC GQSKLAEQVR DSWKEDALFG YQFLNGTNPM 

       250        260        270        280        290        300 
LLRHSVELPA RLKFPPGMEE LQAQLEKELQ GGTLFEADFS LLDGIKANVI LCSQQYLAVP 

       310        320        330        340        350        360 
LVMLKLQPDG KLLPMVIQLQ LPREGSPLPP LFLPTDPPMV WLLAKCWVRS SDFQLHELHS 

       370        380        390        400        410        420 
HLLRGHLMAE VIAVATMRCL PSIHPIFKLL IPHFRYTMEI NVRARNGLVS DLGIFDQVVS 

       430        440        450        460        470        480 
TGGGGHVELL RRAAALLTYS SFCPPDDLAD RGLLGVESSF YAQDALRLWE VISRYVEGIV 

       490        500        510        520        530        540 
SLHYKTDESV KEDFELQAWC REFTEIGLLG AQDRGFPVSL QSKEQLCHFV TMCIFTCTGQ 

       550        560        570        580        590        600 
HSSNHLGQLD WYTWVPNAPC TMRLPPPTTK DATLETVMAT LPNFHQASLQ MSITWQLGRC 

       610        620        630        640        650        660 
QPTMVALGQH EEEYFSGPGP KAVLTKFREE LAALDKDIEV RNAKLALPYE YLRPSRVENS 


VAI

P16469 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools