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Protein

Arachidonate 15-lipoxygenase B

Gene

Alox15b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Converts arachidonic acid to 15S-hydroperoxyeicosatetraenoic acid/(15S)-HPETE. Also acts on linoleic acid to produce 13-hydroxyoctadecadienoic acid/13-HPODE. Has no detectable 8S-lipoxygenase activity but reacts with (8S)-HPETE to produce (8S,15S)-diHPETE. May regulate progression through the cell cycle and cell proliferation. May also regulate cytokine secretion by macrophages and therefore play a role in the immune response. May also regulate macrophage differentiation into proatherogenic foam cells.1 Publication

Catalytic activityi

Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.1 Publication
Linoleate + O2 = (9Z,11E)-13-hydroxyoctadeca-9,11-dienoate.1 Publication

Cofactori

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

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi15 – 151Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi17 – 171Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi39 – 391Calcium 2By similarity
Metal bindingi40 – 401Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi42 – 421Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi44 – 441Calcium 2By similarity
Metal bindingi86 – 861Calcium 1By similarity
Metal bindingi87 – 871Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi374 – 3741Iron; catalyticPROSITE-ProRule annotation
Metal bindingi379 – 3791Iron; catalyticPROSITE-ProRule annotation
Metal bindingi554 – 5541Iron; catalyticPROSITE-ProRule annotation
Metal bindingi677 – 6771Iron; via carboxylate; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • arachidonic acid metabolic process Source: UniProtKB
  • hepoxilin biosynthetic process Source: UniProtKB
  • lipoxygenase pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Lipid metabolism

Keywords - Ligandi

Calcium, Iron, Lipid-binding, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.11.33. 5301.
UniPathwayiUPA00881.

Names & Taxonomyi

Protein namesi
Recommended name:
Arachidonate 15-lipoxygenase B (EC:1.13.11.33)
Short name:
15-LOX-B
Alternative name(s):
15-lipoxygenase 2
Short name:
15-LOX-2
Arachidonate 15-lipoxygenase type II
Linoleate 13-lipoxygenase 15-LOb (EC:1.13.11.-)
Gene namesi
Name:Alox15b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628809. Alox15b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3289.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 677677Arachidonate 15-lipoxygenase BPRO_0000220702Add
BLAST

Proteomic databases

PaxDbiQ8K4F2.
PRIDEiQ8K4F2.

PTM databases

PhosphoSiteiQ8K4F2.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010416.

Chemistry

BindingDBiQ8K4F2.

Structurei

3D structure databases

ProteinModelPortaliQ8K4F2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 125124PLATPROSITE-ProRule annotationAdd
BLAST
Domaini126 – 677552LipoxygenasePROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the lipoxygenase family.Curated
Contains 1 lipoxygenase domain.PROSITE-ProRule annotation
Contains 1 PLAT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IF0U. Eukaryota.
ENOG410YN4N. LUCA.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiQ8K4F2.
KOiK08022.
PhylomeDBiQ8K4F2.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
InterProiIPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K4F2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKFRVRVST GEACGAGTWD KVSVSIVGTH GESPLVPLDH LGKEFSAGAE
60 70 80 90 100
EDFEVTLPQD VGTVLMLRIH KAPPEAPLPL LSFPPDAWYC RWFELEWLPG
110 120 130 140 150
AALRFPCYQW LEGAGELVLR EGAAKVSWQD HHRTLQDQRQ KELESRKDMY
160 170 180 190 200
SWKTYIEGWP HCLDHETVKD LDLNIKYSAM KNAKFFFKAQ SAFTELKFKG
210 220 230 240 250
LLDRTGLWRS LREMKRMFNF HNTPAAEYVF AHWQEDAFFA SQFLNGLNPV
260 270 280 290 300
LIRRCRRLPE NFPVTDEMVA PVLGPGTSLQ AELEKGSLFL VDHGILSGVQ
310 320 330 340 350
TNVINGKPQF SAAPMTLLYQ SPGSGPLLPI AIQLKQTPGP DNPIFLPSDD
360 370 380 390 400
KWDWLLAKTW VRNAEFSIHE ALTHLLHAHL IPEVFALATL RQLPHCHPLF
410 420 430 440 450
KLLIPHTRYT LHINTLAREL LIAPGKVVDK STGLGIGGFS DLIKRNMEQL
460 470 480 490 500
SYSVLCLPED IRARDVGDLP GYYYRDDGMQ IWSAIRSFVS EIVDIYYPSD
510 520 530 540 550
ASVRDDQELQ AWVGEIFSEG FLSQESSGMP SLLDTQEALV QYVTMVIFTC
560 570 580 590 600
SAKHAAVSAS QFDSCVWMPN LPPSMQLPPP TSKGQASPEG FIATLPAVNA
610 620 630 640 650
TCDVIIALWL LSKEPGDRRP LGHYPDEHFT EEVPRRSIAA FQRKLIQISS
660 670
GIRKRNQSLA LPYTYLDPPL IENSVSI
Length:677
Mass (Da):76,145
Last modified:October 1, 2002 - v1
Checksum:i49A47B47C491B8B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF415240 mRNA. Translation: AAN03708.1.
RefSeqiNP_695213.1. NM_153301.2.
UniGeneiRn.86437.

Genome annotation databases

GeneIDi266604.
KEGGirno:266604.
UCSCiRGD:628809. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF415240 mRNA. Translation: AAN03708.1.
RefSeqiNP_695213.1. NM_153301.2.
UniGeneiRn.86437.

3D structure databases

ProteinModelPortaliQ8K4F2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010416.

Chemistry

BindingDBiQ8K4F2.
ChEMBLiCHEMBL3289.

PTM databases

PhosphoSiteiQ8K4F2.

Proteomic databases

PaxDbiQ8K4F2.
PRIDEiQ8K4F2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi266604.
KEGGirno:266604.
UCSCiRGD:628809. rat.

Organism-specific databases

CTDi247.
RGDi628809. Alox15b.

Phylogenomic databases

eggNOGiENOG410IF0U. Eukaryota.
ENOG410YN4N. LUCA.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiQ8K4F2.
KOiK08022.
PhylomeDBiQ8K4F2.

Enzyme and pathway databases

UniPathwayiUPA00881.
BRENDAi1.13.11.33. 5301.

Miscellaneous databases

NextBioi624420.
PROiQ8K4F2.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
InterProiIPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A 15-lipoxygenase in the rat, homolog of human 15-lipoxygenase-2 and mouse 8-lipoxygenase."
    Boeglin W.E., Schneider C., Brash A.R.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Systematic analysis of rat 12/15-lipoxygenase enzymes reveals critical role for spinal eLOX3 hepoxilin synthase activity in inflammatory hyperalgesia."
    Gregus A.M., Dumlao D.S., Wei S.C., Norris P.C., Catella L.C., Meyerstein F.G., Buczynski M.W., Steinauer J.J., Fitzsimmons B.L., Yaksh T.L., Dennis E.A.
    FASEB J. 27:1939-1949(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiLX15B_RAT
AccessioniPrimary (citable) accession number: Q8K4F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: October 1, 2002
Last modified: November 11, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.