NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Tracheal epithelium;
PubMed=1539676 [NCBI, ExPASy, EBI, Israel, Japan]
de Marzo N., Sloan D.L., Dicharry S., Highland E., Sigal E.;
"Cloning and expression of an airway epithelial 12-lipoxygenase.";
Am. J. Physiol. 262:L198-L207(1992).

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: Detected in tracheal epithelium.
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

M81320; AAA30346.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M62516; AAC41614.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S96247; AAB21522.2; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S32825; S32825.

NP_776926.1; -.

3D structure databases

HSSP

P12530; 1LOX. [HSSP ENTRY / PDB]

SMR

P27479; 2-663.

ModBase

P27479.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004052;	Molecular function: arachidonate 12-lipoxygenase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0016165;	Molecular function: lipoxygenase activity (inferred from electronic annotation from InterPro).
GO:0019370;	Biological process: leukotriene biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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).

ProtoNet

P27479.

Genome annotation databases

Ensembl

ENSBTAG00000011990; Bos taurus. [Contig view]

GeneID

282139; -.

KEGG

bta:282139; -.

Phylogenomic databases

HOVERGEN

P27479; -.

Other

UniRef

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

Keywords

Cytoplasm; Dioxygenase; Iron; Leukotriene biosynthesis; Metal-binding; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 663`	`662`	`Arachidonate 12-lipoxygenase, 12S-type.`	`PRO_0000220681`
`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: 75041 Da [This is the MW of the unprocessed precursor]

CRC64: 58063351F14E15D4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGLYRVRVST GSSFCAGSNN QVHLWLVGEH GEAALGWAVR PARGKEVEFQ VDVSEYLGRL 

        70         80         90        100        110        120 
LFVKLRKRHL LSDDAWFCNW ISVQGPGASG NEFRFPCYRW VEGDGILSLP EGTGRTVVDD 

       130        140        150        160        170        180 
PQGLFKKHRE EELAERRKLY RWGNWKDGLI LNIAGATIND LPVDERFLED KRIDFEASLT 

       190        200        210        220        230        240 
KGLADLAIKD SLNILTCWKS LDDFNRIFWC GQSKLAERVR DSWKEDALFG YQFLNGTNPM 

       250        260        270        280        290        300 
LLRRSVRLPA RLEFPPGMGE LQAELEKELQ QGTLFEADFS LLMGIKANVI LCTQQYVAAP 

       310        320        330        340        350        360 
LVMLKLQPDG KLLPMAIQLQ LPHKGSPPPP LFLPTDPPMT WLLAKCWVRS SDFQLHELHS 

       370        380        390        400        410        420 
HLLRGHLVAE VIAVATMRCL PSIHPMFKLL IPHLRYTMEI NIRARTGLVS DSGVFDQVVS 

       430        440        450        460        470        480 
TGGGGHVELL QRAGAFLTYS SFCPPDDLAD RGLLGVKSSF YAQDALRLWE ILSRYVEGIV 

       490        500        510        520        530        540 
SLHYKTDESV RDDIELQAWC RDITEIGLLG AQDRGFPVTL QSKDQLCHFV TMCIFTCTGQ 

       550        560        570        580        590        600 
HSSTHLGQLD WYSWVPNAPC TMRLPPPTTK DVTLEKVMAT LPNFHQASLQ MSITWQLGRR 

       610        620        630        640        650        660 
QPIMVALGQH EEEYFSGPEP KAVLKKFREE LAALEKDIEI RNAQLDWPYE YLRPSLVENS 


VAI

P27479 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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