Reviewed, UniProtKB/Swiss-Prot O35936 (LX15B_MOUSE)

Names and origin

Protein names

Recommended name:
    Arachidonate 15-lipoxygenase type II
      Short name=15-LOX-2
    EC=1.13.11.33
Alternative name(s):
    8S-lipoxygenase
      Short name=8S-LOX

Gene names

Name:	Alox15b
Synonyms:	Alox8

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	677 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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.
Tissue specificity	Expressed in epidermis and brain. No expression found in heart, spleen, liver, skeletal muscle, kidney or testis. Ref.2
Induction	By phorbol ester.
Sequence similarities	Belongs to the lipoxygenase family. Contains 1 lipoxygenase domain. Contains 1 PLAT domain.

Ontologies

Keywords
Biological process	Leukotriene biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell cycle Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of growth Inferred from sequence or structural similarity. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	arachidonate 15-lipoxygenase activity Inferred from sequence or structural similarity. Source: UniProtKB iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW lipoxygenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 677	677	Arachidonate 15-lipoxygenase type II		PRO_0000220701
Regions
	Domain	2 – 125	124	PLAT
	Domain	126 – 677	552	Lipoxygenase
Sites
	Metal binding	374	1	Iron; catalytic By similarity
	Metal binding	379	1	Iron; catalytic By similarity
	Metal binding	554	1	Iron; catalytic By similarity
	Metal binding	677	1	Iron; via carboxylate; catalytic By similarity
Natural variations
	Natural variant	32	1	E → G in clone K12.
	Natural variant	38	1	L → M in clone G2.
	Natural variant	58	1	P → R in clone K12.
	Natural variant	76	1	V → A in clones G2, G5, G11 and K1.
	Natural variant	413	1	I → V in clone K7.
	Natural variant	536	1	R → Q in clones G2, G5 and G11.

Sequences

	Sequence		Length	Mass (Da)
	O35936-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 78DB1AC9C2F68399	FASTA	677	76,230
	10 20 30 40 50 60 MAKCRVRVST GEACGAGTWD KVSVSIVGTH GESPLVPLDH LGKEFSAGAE EDFEVTLPQD 70 80 90 100 110 120 VGTVLMLRVH KAPPEVSLPL MSFRSDAWFC RWFELEWLPG AALHFPCYQW LEGAGELVLR 130 140 150 160 170 180 EGAAKVSWQD HHPTLQDQRQ KELESRQKMY SWKTYIEGWP RCLDHETVKD LDLNIKYSAM 190 200 210 220 230 240 KNAKLFFKAH SAYTELKVKG LLDRTGLWRS LREMRRLFNF RKTPAAEYVF AHWQEDAFFA 250 260 270 280 290 300 SQFLNGINPV LIRRCHSLPN NFPVTDEMVA PVLGPGTSLQ AELEKGSLFL VDHGILSGVH 310 320 330 340 350 360 TNILNGKPQF SAAPMTLLHQ SSGSGPLLPI AIQLKQTPGP DNPIFLPSDD TWDWLLAKTW 370 380 390 400 410 420 VRNSEFYIHE AVTHLLHAHL IPEVFALATL RQLPRCHPLF KLLIPHIRYT LHINTLAREL 430 440 450 460 470 480 LVAPGKLIDK STGLGTGGFS DLIKRNMEQL NYSVLCLPED IRARGVEDIP GYYYRDDGMQ 490 500 510 520 530 540 IWGAIKSFVS EIVSIYYPSD TSVQDDQELQ AWVREIFSEG FLGRESSGMP SLLDTREALV 550 560 570 580 590 600 QYITMVIFTC SAKHAAVSSG QFDSCVWMPN LPPTMQLPPP TSKGQARPES FIATLPAVNS 610 620 630 640 650 660 SSYHIIALWL LSAEPGDQRP LGHYPDEHFT EDAPRRSVAA FQRKLIQISK GIRERNRGLA 670 LPYTYLDPPL IENSVSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and functional expression of a phorbol ester-inducible 8S-lipoxygenase from mouse skin." Jisaka M., Kim R.B., Boeglin W.E., Nanney L.B., Brash A.R. J. Biol. Chem. 272:24410-24416(1997) [PubMed: 9305900] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Epidermis.
[2]	"cDNA cloning of a 8-lipoxygenase and a novel epidermis-type lipoxygenase from phorbol ester-treated mouse skin." Krieg P., Kinzig A., Heidt M., Marks F., Fuerstenberger G. Biochim. Biophys. Acta 1391:7-12(1998) [PubMed: 9518531] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: NMRI. Tissue: Epidermis.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Skin.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U93277 mRNA. Translation: AAC53356.1. Y14696 mRNA. Translation: CAA75003.1. AK028724 mRNA. Translation: BAC26085.1. BC015253 mRNA. Translation: AAH15253.1.
IPI	IPI00136170.
RefSeq	NP_033791.1.
UniGene	Mm.289672
3D structure databases
HSSP	HSSP built from PDB template 1LOX based on UniProtKB P12530.
ModBase	Search...
Genome annotation databases
Ensembl	ENSMUSG00000020891. Mus musculus. [Contig view]
GeneID	11688.
KEGG	mmu:11688.
Organism-specific databases
MGI	MGI:1098228. Alox8.
Phylogenomic databases
HOGENOM	O35936.
HOVERGEN	O35936.
OMA	O35936. MPNLPPS.
Enzyme and pathway databases
BRENDA	1.13.11.33. 244.
Gene expression databases
ArrayExpress	O35936.
Bgee	O35936.
CleanEx	MM_ALOX8.
GermOnline	ENSMUSG00000020891. Mus musculus.
Family and domain databases
InterPro	IPR000907. LipOase. IPR013819. LipOase_C. IPR001024. LipOase_LH2. IPR001885. LipOase_mml. [Graphical view]
Gene3D	G3DSA:2.60.60.20. Lipase_LipOase. 1 hit.
PANTHER	PTHR11771. LipOase. 1 hit.
Pfam	PF00305. Lipoxygenase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view]
PRINTS	PR00087. LIPOXYGENASE. PR00467. MAMLPOXGNASE.
SMART	SM00308. LH2. 1 hit. [Graphical view]
PROSITE	PS00711. LIPOXYGENASE_1. 1 hit. PS00081. LIPOXYGENASE_2. 1 hit. PS51393. LIPOXYGENASE_3. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	279335.
SOURCE	Search...

Entry information

Entry name

LX15B_MOUSE

Accession

Primary (citable) accession number: O35936

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)