[1]	NUCLEOTIDE SEQUENCE [MRNA]. Boeglin W.E., Schneider C., Brash A.R.; "A 15-lipoxygenase in the rat, homolog of human 15-lipoxygenase-2 and mouse 8-lipoxygenase."; Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: Arachidonate + O₂ = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.
COFACTOR: Binds 1 iron ion per subunit (By similarity).
PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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

AF415240; AAN03708.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_695213.1; -.

UniGene

Rn.86437

3D structure databases

HSSP

P12530; 1LOX. [HSSP ENTRY / PDB]

ModBase

Q8K4F2.

PTM databases

PhosphoSite

Q8K4F2; -.

Organism-specific databases

RGD

628809; Alox15b.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0050473;	Molecular function: arachidonate 15-lipoxygenase activity (inferred from sequence or structural similarity from UniProtKB).
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:0045786;	Biological process: negative regulation of cell cycle (inferred from sequence or structural similarity from UniProtKB).
GO:0008285;	Biological process: negative regulation of cell proliferation (inferred from sequence or structural similarity from UniProtKB).
GO:0045926;	Biological process: negative regulation of growth (inferred from sequence or structural similarity from UniProtKB).
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).

Genome annotation databases

Ensembl

ENSRNOG00000007778; Rattus norvegicus. [Contig view]

GeneID

266604; -.

KEGG

rno:266604; -.

Phylogenomic databases

HOVERGEN

Q8K4F2; -.

Other

624420; -.

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`
`CHAIN`	`1 677`	`677`	`Arachidonate 15-lipoxygenase type II.`	`PRO_0000220702`
`DOMAIN`	`2 125`	`124`	`PLAT.`
`DOMAIN`	`126 677`	`552`	`Lipoxygenase.`
`METAL`	`374 374`		`Iron; catalytic (By similarity).`
`METAL`	`379 379`		`Iron; catalytic (By similarity).`
`METAL`	`554 554`		`Iron; catalytic (By similarity).`
`METAL`	`677 677`		`Iron; via carboxylate; catalytic (By similarity).`

Sequence information

Length: 677 AA [This is the length of the unprocessed precursor]

Molecular weight: 76145 Da [This is the MW of the unprocessed precursor]

CRC64: 49A47B47C491B8B1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKFRVRVST GEACGAGTWD KVSVSIVGTH GESPLVPLDH LGKEFSAGAE EDFEVTLPQD 

        70         80         90        100        110        120 
VGTVLMLRIH KAPPEAPLPL LSFPPDAWYC RWFELEWLPG AALRFPCYQW LEGAGELVLR 

       130        140        150        160        170        180 
EGAAKVSWQD HHRTLQDQRQ KELESRKDMY SWKTYIEGWP HCLDHETVKD LDLNIKYSAM 

       190        200        210        220        230        240 
KNAKFFFKAQ SAFTELKFKG LLDRTGLWRS LREMKRMFNF HNTPAAEYVF AHWQEDAFFA 

       250        260        270        280        290        300 
SQFLNGLNPV LIRRCRRLPE NFPVTDEMVA PVLGPGTSLQ AELEKGSLFL VDHGILSGVQ 

       310        320        330        340        350        360 
TNVINGKPQF SAAPMTLLYQ SPGSGPLLPI AIQLKQTPGP DNPIFLPSDD KWDWLLAKTW 

       370        380        390        400        410        420 
VRNAEFSIHE ALTHLLHAHL IPEVFALATL RQLPHCHPLF KLLIPHTRYT LHINTLAREL 

       430        440        450        460        470        480 
LIAPGKVVDK STGLGIGGFS DLIKRNMEQL SYSVLCLPED IRARDVGDLP GYYYRDDGMQ 

       490        500        510        520        530        540 
IWSAIRSFVS EIVDIYYPSD ASVRDDQELQ AWVGEIFSEG FLSQESSGMP SLLDTQEALV 

       550        560        570        580        590        600 
QYVTMVIFTC SAKHAAVSAS QFDSCVWMPN LPPSMQLPPP TSKGQASPEG FIATLPAVNA 

       610        620        630        640        650        660 
TCDVIIALWL LSKEPGDRRP LGHYPDEHFT EEVPRRSIAA FQRKLIQISS GIRKRNQSLA 

       670 
LPYTYLDPPL IENSVSI

Q8K4F2 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