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D3ZKX9 (LOXE3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hydroperoxide isomerase ALOXE3

EC=5.4.4.-
Alternative name(s):
Epidermis-type lipoxygenase 3
Short name=Epidermal LOX-3
Short name=e-LOX-3
Short name=eLOX-3
EC=1.13.11.-
Gene names
Name:Aloxe3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length711 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced dioxygenase activity compared to other lipoxygenases. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols. The dioxygenase activity requires a step of activation of the enzyme by molecular oxygen. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites. Plays also a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activates PPARG. Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia. Ref.3

Catalytic activity

(5Z,8Z,10E,14Z)-(12R)-12-hydroperoxyicosa-5,8,10,14-tetraenoate = (5Z,9E,14Z)-(8R,11R,12R)-8-hydroxy-11,12-hydroperoxyicosa-5,9,14-trienoate.

Cofactor

Binds 1 iron ion per subunit By similarity.

Pathway

Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis.

Lipid metabolism; sphingolipid metabolism.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Isomerase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Inferred from direct assay Ref.3. Source: UniProtKB

ceramide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of skin barrier

Inferred from sequence or structural similarity. Source: UniProtKB

fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

hepoxilin biosynthetic process

Inferred from direct assay Ref.3. Source: UniProtKB

linoleic acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

lipoxygenase pathway

Inferred from sequence or structural similarity. Source: UniProtKB

peroxisome proliferator activated receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

sensory perception of pain

Inferred from mutant phenotype Ref.3. Source: UniProtKB

sphingolipid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhepoxilin A3 synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 711711Hydroperoxide isomerase ALOXE3
PRO_0000423419

Regions

Domain2 – 119118PLAT
Domain119 – 711593Lipoxygenase

Sites

Metal binding4081Iron; catalytic By similarity
Metal binding4131Iron; catalytic By similarity
Metal binding5881Iron; catalytic By similarity
Metal binding5921Iron; catalytic By similarity
Metal binding7111Iron; via carboxylate; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
D3ZKX9 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: 41C3D9BBC6C4532B

FASTA71180,440
        10         20         30         40         50         60 
MAVYRLCVTT GSYLKAGTLD NIYATLVGTC GESPKQKLDR VGRDFATGSV QKYKVRCASE 

        70         80         90        100        110        120 
LGEILLLRLH KERFAFFCKD PWYCSRICVT TPDGSVVHFP CYQWIDGYCT VELRPGTART 

       130        140        150        160        170        180 
ICQDALPLLL DHRKRELQAR QECYRWKIYA PGFPRMVDVS SFEEMESDKK FALTKTAPCA 

       190        200        210        220        230        240 
DQDDNSGNRY LPGFPMKVDI PSLLHMEPNI RYSATKTASL IFNALPASLG MKIRGLLDRK 

       250        260        270        280        290        300 
GSWKRLDDIR NIFWCHKTFT SEYVTEHWCE DSFFGYQYLN GVNPIMLHCL SSLPSKLPVT 

       310        320        330        340        350        360 
NDMVAPLLGP GTCLQTELER GHIFLADYWI LAEAPVHCLN GRQQYVTAPL CLLWLNPQGV 

       370        380        390        400        410        420 
LLPLAIQLSQ IPGPESPIFL PTDCELDWLL AKTWVRNSEF LVHENNTHFL CTHLLCEAFS 

       430        440        450        460        470        480 
MATLRQLPLC HPVYKLLLPH TRYTLQVNTI ARATLLNPDG LVDKVTSIGR RGLIYLMSTG 

       490        500        510        520        530        540 
LAHFTYTDFC LPDSLRARGV LTIPNYHYRD DGLKIWAAIE RFVSEIVSYY YPNDACVQQD 

       550        560        570        580        590        600 
SELQAWVGEI FAQAFLGRES SGFPSRLCTP GELVKYLTAI IFNCSAQHAA VNSGQHDFGA 

       610        620        630        640        650        660 
WMPNAPSSMR QPPPQTKGNT TMESYLETLP EVNTTCSNLL LFWLVSQEPK DQRPLGTYPD 

       670        680        690        700        710 
EHFTEEAPRQ SIAAFQKCLA QISKDIRARN ESLALPYAYL DPPLIENSVS I 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[3]"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 IN ALGESIA.
+Additional computationally mapped references.

Web resources

Protein Spotlight

about water - Issue 153 of September 2013

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR06064371 Genomic DNA. No translation available.
CH473948 Genomic DNA. Translation: EDM04845.1.
RefSeqNP_001099263.1. NM_001105793.1.
XP_006246679.1. XM_006246617.1.
UniGeneRn.8716.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010141; ENSRNOP00000010141; ENSRNOG00000007454.
GeneID287424.
KEGGrno:287424.
UCSCRGD:1306252. rat.

Organism-specific databases

CTD59344.
RGD1306252. Aloxe3.

Phylogenomic databases

GeneTreeENSGT00550000074415.
OMACSRICVT.
OrthoDBEOG7V49XR.
PhylomeDBD3ZKX9.
TreeFamTF105320.

Enzyme and pathway databases

UniPathwayUPA00222.
UPA00881.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11771. PTHR11771. 1 hit.
PfamPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio626099.
PROD3ZKX9.

Entry information

Entry nameLOXE3_RAT
AccessionPrimary (citable) accession number: D3ZKX9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 18, 2013
Last sequence update: April 20, 2010
Last modified: May 14, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PATHWAY comments

Index of metabolic and biosynthesis pathways