Alox8

Functionⁱ

Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Catalyzes the peroxidation of arachidonate and linoleate into (8S)-HPETE and (9S)-HPODE respectively. From arachidonate mainly produces (8S)-HPETE and in addition, minor products derived from (8S)-HPETE itself that may include leukotriene A4 and 8,15-diHPETE. With arachidonate as substrate, has no detectable 15S-lipoxygenase activity and only displays a 8S-lipoxygenase activity. However, it may have a 15S-lipoxygenase activity with (8S)-HPETE to produce (8S,15S)-diHPETE. May also catalyze (15S)-HPETE peroxidation to produce 8,15-diHPETE. May play a role in keratinocyte differentiation through activation of the peroxisome proliferator activated receptor signaling pathway.4 Publications

Caution

Despite its homology with human ALOX15B (AC O15296), it seems not to have any 15S-lipoxygenase activity on arachidonate. Based on its catalytic activity it is referred to as the mouse arachidonate 8S-lipoxygenase.Curated

Catalytic activityⁱ

Arachidonate + O₂ = (5Z,9E,11Z,14Z)-8-hydroperoxyicosa-5,9,11,14-tetraenoate.3 Publications

Cofactorⁱ

Fe cationPROSITE-ProRule annotationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation

Kineticsⁱ

The highest catalytic efficiency is observed with arachidonate followed by (8S)-HPETE and(15S)-HPETE with similar efficiencies.

Pathwayⁱ: hydroperoxy eicosatetraenoic acid biosynthesis

This protein is involved in the pathway hydroperoxy eicosatetraenoic acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway hydroperoxy eicosatetraenoic acid biosynthesis and in Lipid metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	15	Calcium 1; via carbonyl oxygenBy similarity	1
Metal bindingⁱ	17	Calcium 1; via carbonyl oxygenBy similarity	1
Metal bindingⁱ	39	Calcium 2By similarity	1
Metal bindingⁱ	40	Calcium 2; via carbonyl oxygenBy similarity	1
Metal bindingⁱ	42	Calcium 2; via carbonyl oxygenBy similarity	1
Metal bindingⁱ	44	Calcium 2By similarity	1
Metal bindingⁱ	86	Calcium 1By similarity	1
Metal bindingⁱ	87	Calcium 1; via carbonyl oxygenBy similarity	1
Metal bindingⁱ	374	Iron; catalyticPROSITE-ProRule annotation	1
Metal bindingⁱ	379	Iron; catalyticPROSITE-ProRule annotation	1
Metal bindingⁱ	554	Iron; catalyticPROSITE-ProRule annotation	1
Metal bindingⁱ	677	Iron; via carboxylate; catalyticPROSITE-ProRule annotation	1

GO - Molecular functionⁱ

arachidonate 15-lipoxygenase activity Source: MGI
arachidonate 8(S)-lipoxygenase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 10625675
calcium ion binding Source: MGI
iron ion binding Source: MGI
linoleate 13S-lipoxygenase activity Source: MGI
lipid binding Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

arachidonic acid metabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 9305900
hepoxilin biosynthetic process Source: MGI
linoleic acid metabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 9305900
lipoxygenase pathway
Source: UniProtKB
Inferred from direct assayⁱ
- 9305900
negative regulation of cell cycle Source: MGI
negative regulation of cell proliferation Source: MGI
negative regulation of growth Source: MGI
positive regulation of chemokine secretion Source: MGI
positive regulation of keratinocyte differentiation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 10965849
positive regulation of macrophage derived foam cell differentiation Source: MGI
positive regulation of peroxisome proliferator activated receptor signaling pathway
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 10965849

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Dioxygenase, Oxidoreductase
Biological process	Lipid metabolism
Ligand	Calcium, Iron, Lipid-binding, Metal-binding

Enzyme and pathway databases

Reactomeⁱ	R-MMU-2142770 Synthesis of 15-eicosatetraenoic acid derivatives
UniPathwayⁱ	UPA00881

Chemistry databases

SwissLipidsⁱ	SLP:000000650 SLP:000000742

SwissLipidsⁱ

SLP:000000650
SLP:000000742

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Arachidonate 8S-lipoxygenase (EC:1.13.11.-) Short name: 8-LOX Short name: 8S-LOX Alternative name(s): 15-lipoxygenase 2 Short name: 15-LOX-2 Arachidonate 15-lipoxygenase B Short name: 15-LOX-B
Gene namesⁱ	Name:Alox8 Synonyms:Alox15b
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 11

Organism-specific databases

MGIⁱ	MGI:1098228 Alox8

Keywords - Cellular componentⁱ

Cytoplasm, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	374	H → L: Loss of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	558	S → A, H or N: Retains catalytic activity indicating it is not required for iron ligand-binding. 1 Publication	1
Mutagenesisⁱ	603	Y → D: Changes the stereoselectivity of the oxygenation reaction to produce (15S)-HPETE instead of (8S)-HPETE. Completely changes the stereoselectivity; when associated with V-604. 1 Publication	1
Mutagenesisⁱ	604	H → V: Changes the stereoselectivity of the oxygenation reaction to produce (15S)-HPETE instead of (8S)-HPETE. Completely changes the stereoselectivity; when associated with D-603. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000220701	1 – 677	Arachidonate 8S-lipoxygenaseAdd BLAST		677

Proteomic databases

PaxDbⁱ	O35936
PRIDEⁱ	O35936

PTM databases

PhosphoSitePlusⁱ	O35936

PhosphoSitePlusⁱ

O35936

Expressionⁱ

Tissue specificityⁱ

Expressed in epidermis and brain. No expression found in heart, spleen, liver, skeletal muscle, kidney or testis.2 Publications

Inductionⁱ

By phorbol ester.1 Publication

Gene expression databases

Bgeeⁱ	ENSMUSG00000020891 Expressed in 41 organ(s), highest expression level in skin of back
CleanExⁱ	MM_ALOX8
ExpressionAtlasⁱ	O35936 baseline and differential
Genevisibleⁱ	O35936 MM

Interactionⁱ

Protein-protein interaction databases

STRINGⁱ	10090.ENSMUSP00000021262

STRINGⁱ

10090.ENSMUSP00000021262

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	O35936
SMRⁱ	O35936
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	2 – 125	PLATPROSITE-ProRule annotationAdd BLAST		124
Domainⁱ	126 – 677	LipoxygenasePROSITE-ProRule annotationAdd BLAST		552

Domainⁱ

The PLAT domain can bind calcium ions; this promotes association with membranes.By similarity

Sequence similaritiesⁱ

Belongs to the lipoxygenase family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG410IF0U Eukaryota ENOG410YN4N LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000074415
HOGENOMⁱ	HOG000234358
HOVERGENⁱ	HBG005150
InParanoidⁱ	O35936
KEGG Orthology (KO) More...KOⁱ	K08022
OMAⁱ	EFSIHEA
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G04A4
PhylomeDBⁱ	O35936
TreeFamⁱ	TF105320

Family and domain databases

InterProⁱ	View protein in InterPro IPR000907 LipOase IPR013819 LipOase_C IPR036226 LipOase_C_sf IPR020834 LipOase_CS IPR020833 LipOase_Fe_BS IPR001885 LipOase_mml IPR001024 PLAT/LH2_dom IPR036392 PLAT/LH2_dom_sf
PANTHERⁱ	PTHR11771 PTHR11771, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00305 Lipoxygenase, 1 hit PF01477 PLAT, 1 hit
PRINTSⁱ	PR00087 LIPOXYGENASE PR00467 MAMLPOXGNASE
SMARTⁱ	View protein in SMART SM00308 LH2, 1 hit
SUPFAMⁱ	SSF48484 SSF48484, 1 hit SSF49723 SSF49723, 1 hit
PROSITEⁱ	View protein in PROSITE PS00711 LIPOXYGENASE_1, 1 hit PS00081 LIPOXYGENASE_2, 1 hit PS51393 LIPOXYGENASE_3, 1 hit PS50095 PLAT, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show all Align All

O35936-1 [UniParc]FASTA Add to basket

« Hide

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

Length:677

Mass (Da):76,230

Last modified:January 1, 1998 - v1

Checksum:ⁱ78DB1AC9C2F68399

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	B1ASX6	B1ASX6_MOUSE		Arachidonate 8S-lipoxygenase Arachidonate 8S-lipoxygenase	Alox8	648	Annotation score:

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱ	32	E → G in clone K12.	1
Natural variantⁱ	38	L → M in clone G2.	1
Natural variantⁱ	58	P → R in clone K12.	1
Natural variantⁱ	76	V → A in clones G2, G5, G11 and K1.	1
Natural variantⁱ	413	I → V in clone K7.	1
Natural variantⁱ	536	R → Q in clones G2, G5 and G11.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U93277 mRNA Translation: AAC53356.1 Y14696 mRNA Translation: CAA75003.1 AK028724 mRNA Translation: BAC26085.1 AL645527 Genomic DNA No translation available. BC015253 mRNA Translation: AAH15253.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS24886.1
NCBI Reference Sequences More...RefSeqⁱ	NP_033791.1, NM_009661.4
UniGeneⁱ	Mm.289672

Genome annotation databases

Ensemblⁱ	ENSMUST00000021262; ENSMUSP00000021262; ENSMUSG00000020891
GeneIDⁱ	11688
KEGGⁱ	mmu:11688
UCSC genome browser More...UCSCⁱ	uc007jpl.1 mouse

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O35936	Uncharacterized protein		MOUSE		529	UniRef100_O35936

Protein	Similar proteins		Species	Score	Length	Source
O35936	Uncharacterized protein		MOUSE		529	UniRef90_O35936
UPI000A3127F1		MUSPA		677
UPI000A315671		MUSCR		677

Protein	Similar proteins		Species	Score	Length	Source
O35936	Arachidonate 15-lipoxygenase B	)	HUMAN		676	UniRef50_O15296
Arachidonate 15-lipoxygenase B		RAT		677
Uncharacterized protein		AOTNA		677
Uncharacterized protein		COLAP		676
Uncharacterized protein		RHIBE		676
+193

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U93277 mRNA Translation: AAC53356.1 Y14696 mRNA Translation: CAA75003.1 AK028724 mRNA Translation: BAC26085.1 AL645527 Genomic DNA No translation available. BC015253 mRNA Translation: AAH15253.1
CCDSⁱ	CCDS24886.1
RefSeqⁱ	NP_033791.1, NM_009661.4
UniGeneⁱ	Mm.289672

3D structure databases

ProteinModelPortalⁱ	O35936
SMRⁱ	O35936
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	10090.ENSMUSP00000021262

STRINGⁱ

10090.ENSMUSP00000021262

Chemistry databases

SwissLipidsⁱ	SLP:000000650 SLP:000000742

SwissLipidsⁱ

SLP:000000650
SLP:000000742

PTM databases

PhosphoSitePlusⁱ	O35936

PhosphoSitePlusⁱ

O35936

Proteomic databases

PaxDbⁱ	O35936
PRIDEⁱ	O35936

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000021262; ENSMUSP00000021262; ENSMUSG00000020891
GeneIDⁱ	11688
KEGGⁱ	mmu:11688
UCSCⁱ	uc007jpl.1 mouse

Organism-specific databases

CTDⁱ	11688
MGIⁱ	MGI:1098228 Alox8

Phylogenomic databases

eggNOGⁱ	ENOG410IF0U Eukaryota ENOG410YN4N LUCA
GeneTreeⁱ	ENSGT00550000074415
HOGENOMⁱ	HOG000234358
HOVERGENⁱ	HBG005150
InParanoidⁱ	O35936
KOⁱ	K08022
OMAⁱ	EFSIHEA
OrthoDBⁱ	EOG091G04A4
PhylomeDBⁱ	O35936
TreeFamⁱ	TF105320

Enzyme and pathway databases

UniPathwayⁱ	UPA00881
Reactomeⁱ	R-MMU-2142770 Synthesis of 15-eicosatetraenoic acid derivatives

Miscellaneous databases

ChiTaRSⁱ	Alox8 mouse
Protein Ontology More...PROⁱ	PR:O35936
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000020891 Expressed in 41 organ(s), highest expression level in skin of back
CleanExⁱ	MM_ALOX8
ExpressionAtlasⁱ	O35936 baseline and differential
Genevisibleⁱ	O35936 MM

Family and domain databases

InterProⁱ	View protein in InterPro IPR000907 LipOase IPR013819 LipOase_C IPR036226 LipOase_C_sf IPR020834 LipOase_CS IPR020833 LipOase_Fe_BS IPR001885 LipOase_mml IPR001024 PLAT/LH2_dom IPR036392 PLAT/LH2_dom_sf
PANTHERⁱ	PTHR11771 PTHR11771, 1 hit
Pfamⁱ	View protein in Pfam PF00305 Lipoxygenase, 1 hit PF01477 PLAT, 1 hit
PRINTSⁱ	PR00087 LIPOXYGENASE PR00467 MAMLPOXGNASE
SMARTⁱ	View protein in SMART SM00308 LH2, 1 hit
SUPFAMⁱ	SSF48484 SSF48484, 1 hit SSF49723 SSF49723, 1 hit
PROSITEⁱ	View protein in PROSITE PS00711 LIPOXYGENASE_1, 1 hit PS00081 LIPOXYGENASE_2, 1 hit PS51393 LIPOXYGENASE_3, 1 hit PS50095 PLAT, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ALOX8_MOUSE
Accessionⁱ	O35936Primary (citable) accession number: O35936 Secondary accession number(s): B1ASX5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
	Last sequence update:	January 1, 1998
	Last modified:	November 7, 2018
	This is version 156 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways

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UniProtKB - O35936 (ALOX8_MOUSE)

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Arachidonate 8S-lipoxygenase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Caution

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: hydroperoxy eicosatetraenoic acid biosynthesis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Chemistry databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytosol

Other locations

Cytoskeleton

Cytosol

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Kineticsⁱ

Pathwayⁱ: hydroperoxy eicosatetraenoic acid biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ