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Q02759

- LOX15_RAT

UniProt

Q02759 - LOX15_RAT

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Protein
Arachidonate 15-lipoxygenase
Gene
Alox15, Alox12l
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. Beside its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass.4 Publications

Catalytic activityi

Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.2 Publications
Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.2 Publications

Cofactori

Binds 1 iron ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi361 – 3611Iron; catalytic By similarity
Metal bindingi366 – 3661Iron; catalytic By similarity
Metal bindingi541 – 5411Iron; catalytic By similarity
Metal bindingi545 – 5451Iron; catalytic By similarity
Metal bindingi663 – 6631Iron; via carboxylate; catalytic By similarity

GO - Molecular functioni

  1. arachidonate 12-lipoxygenase activity Source: RGD
  2. arachidonate 15-lipoxygenase activity Source: RGD
  3. hepoxilin A3 synthase activity Source: RGD
  4. hepoxilin-epoxide hydrolase activity Source: UniProtKB
  5. iron ion binding Source: UniProtKB
  6. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  7. potassium channel inhibitor activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. apoptotic cell clearance Source: UniProtKB
  2. arachidonic acid metabolic process Source: UniProtKB
  3. bone mineralization Source: UniProtKB
  4. cellular response to calcium ion Source: UniProtKB
  5. cellular response to interleukin-13 Source: UniProtKB
  6. fatty acid oxidation Source: UniProtKB
  7. hepoxilin biosynthetic process Source: UniProtKB
  8. icosanoid biosynthetic process Source: UniProtKB
  9. lipoxin A4 biosynthetic process Source: UniProtKB
  10. lipoxygenase pathway Source: RGD
  11. negative regulation of adaptive immune response Source: UniProtKB
  12. negative regulation of apoptotic process Source: UniProtKB
  13. negative regulation of cell volume Source: UniProtKB
  14. ossification Source: UniProtKB
  15. phosphatidylethanolamine biosynthetic process Source: UniProtKB
  16. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  17. positive regulation of actin filament polymerization Source: UniProtKB
  18. positive regulation of cell growth Source: UniProtKB
  19. positive regulation of cell proliferation Source: UniProtKB
  20. positive regulation of cell-substrate adhesion Source: UniProtKB
  21. positive regulation of heterotypic cell-cell adhesion Source: RGD
  22. regulation of engulfment of apoptotic cell Source: UniProtKB
  23. regulation of membrane potential Source: UniProtKB
  24. regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
  25. response to endoplasmic reticulum stress Source: UniProtKB
  26. wound healing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

Calcium, Iron, Lipid-binding, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_197237. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_198843. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_198846. Synthesis of 15-eicosatetraenoic acid derivatives.
UniPathwayiUPA00881.

Names & Taxonomyi

Protein namesi
Recommended name:
Arachidonate 15-lipoxygenase (EC:1.13.11.33)
Short name:
15-LOX
Alternative name(s):
12/15-lipoxygenase
Arachidonate 12-lipoxygenase, leukocyte-type (EC:1.13.11.31)
Short name:
12-LOX
Arachidonate omega-6 lipoxygenase
Gene namesi
Name:Alox15
Synonyms:Alox12l
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi70493. Alox15.

Subcellular locationi

Cytoplasmcytosol. Cell membrane; Peripheral membrane protein By similarity. Lipid droplet By similarity
Note: Predominantly cytosolic; becomes enriched at membranes upon calcium binding. Translocates from the cytosol to the plasma membrane when stimulated by IL13/interleukin-13 and in macrophages binding apoptotic cells By similarity.1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  3. lipid particle Source: UniProtKB
  4. membrane Source: UniProtKB
  5. plasma membrane Source: UniProtKB
  6. sarcolemma Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Lipid droplet, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 663662Arachidonate 15-lipoxygenase
PRO_0000220687Add
BLAST

Proteomic databases

PaxDbiQ02759.
PRIDEiQ02759.

Expressioni

Tissue specificityi

Detected in leukocytes, lung and aorta.1 Publication

Gene expression databases

GenevestigatoriQ02759.

Interactioni

Subunit structurei

Interacts with PEBP1; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade By similarity.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026038.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 115114PLAT
Add
BLAST
Domaini116 – 663548Lipoxygenase
Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the lipoxygenase family.
Contains 1 PLAT domain.

Phylogenomic databases

eggNOGiNOG133298.
GeneTreeiENSGT00550000074415.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiQ02759.
KOiK00460.
OMAiLTCWKDL.
OrthoDBiEOG7B05CG.
TreeFamiTF105320.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. 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. 2 hits.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02759-1 [UniParc]FASTAAdd to Basket

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MGVYRIRVST GDSKYAGSNN EVYLWLVGQH GEASLGKLLR PCRDSEAEFK    50
VDVSEYLGPL LFVRVQKWHY LTDDAWFCNW ISVKGPGDQG SEYMFPCYRW 100
VQGRSILSLP EGTGCTVVED SQGLFRKHRE EELEERRSLY RWGNWKDGSI 150
LNVAAASISD LPVDQRFRED KRIEFEASQV IGVMDTVVNF PINTVTCWKS 200
LDDFNCVFKS GHTKMAERVR NSWKEDAFFG YQFLNGANPM VLKRSTCLPA 250
RLVFPPGMEK LQAQLNKELQ KGTLFEADFF LLDGIKANVI LCSQQYLAAP 300
LVMLKLMPDG QLLPIAIQLE LPKTGSTPPP IFTPSDPPMD WLLAKCWVRS 350
SDLQLHELQA HLLRGHLMAE VFAVATMRCL PSVHPVFKLL VPHLLYTMEI 400
NVRARSDLIS ERGFFDKAMS TGGGGHLDLL KQAGAFLTYC SLCPPDDLAE 450
RGLLDIETCF YAKDALRLWQ IMNRYVVGMF NLHYKTDKAV QDDYELQSWC 500
REITDIGLQG AQDRGFPTSL QSRAQACYFI TMCIFTCTAQ HSSVHLGQLD 550
WFYWVPNAPC TMRLPPPTTK EATMEKLMAT LPNPNQSTLQ INVVWLLGRR 600
QAVMVPLGQH SEEHFPNPEA KAVLKKFREE LAALDKEIEI RNKSLDIPYE 650
YLRPSMVENS VAI 663
Length:663
Mass (Da):75,378
Last modified:October 16, 2013 - v3
Checksum:iC732D3EB22CA0411
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551E → G in AAB30132. 1 Publication
Sequence conflicti371 – 3711V → L in AAA41532. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L06040 mRNA. Translation: AAA41532.1.
S69383 mRNA. Translation: AAB30132.1.
AABR06064408 Genomic DNA. No translation available.
PIRiI52462.
S30051.
RefSeqiNP_112272.2. NM_031010.2.
UniGeneiRn.11318.

Genome annotation databases

EnsembliENSRNOT00000026038; ENSRNOP00000026038; ENSRNOG00000019183.
GeneIDi81639.
KEGGirno:81639.
UCSCiRGD:70493. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L06040 mRNA. Translation: AAA41532.1 .
S69383 mRNA. Translation: AAB30132.1 .
AABR06064408 Genomic DNA. No translation available.
PIRi I52462.
S30051.
RefSeqi NP_112272.2. NM_031010.2.
UniGenei Rn.11318.

3D structure databases

ModBasei Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000026038.

Chemistry

BindingDBi Q02759.
ChEMBLi CHEMBL2741.

Proteomic databases

PaxDbi Q02759.
PRIDEi Q02759.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000026038 ; ENSRNOP00000026038 ; ENSRNOG00000019183 .
GeneIDi 81639.
KEGGi rno:81639.
UCSCi RGD:70493. rat.

Organism-specific databases

CTDi 246.
RGDi 70493. Alox15.

Phylogenomic databases

eggNOGi NOG133298.
GeneTreei ENSGT00550000074415.
HOGENOMi HOG000234358.
HOVERGENi HBG005150.
InParanoidi Q02759.
KOi K00460.
OMAi LTCWKDL.
OrthoDBi EOG7B05CG.
TreeFami TF105320.

Enzyme and pathway databases

UniPathwayi UPA00881 .
Reactomei REACT_197237. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_198843. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_198846. Synthesis of 15-eicosatetraenoic acid derivatives.

Miscellaneous databases

NextBioi 35583133.

Gene expression databases

Genevestigatori Q02759.

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
InterProi IPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11771. PTHR11771. 1 hit.
Pfami PF00305. Lipoxygenase. 2 hits.
PF01477. PLAT. 1 hit.
[Graphical view ]
PRINTSi PR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTi SM00308. LH2. 1 hit.
[Graphical view ]
SUPFAMi SSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEi PS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Arachidonate 12-lipoxygenase of rat pineal glands: catalytic properties and primary structure deduced from its cDNA."
    Hada T., Hagiya H., Suzuki H., Arakawa T., Nakamura M., Matsuda S., Yoshimoto T., Yamamoto S., Azekawa T., Morita Y., Ishimura K., Kim H.Y.
    Biochim. Biophys. Acta 1211:221-228(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    Tissue: Pineal gland.
  3. "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.
    , 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.
  4. "The rat leukocyte-type 12-lipoxygenase exhibits an intrinsic hepoxilin A3 synthase activity."
    Nigam S., Patabhiraman S., Ciccoli R., Ishdorj G., Schwarz K., Petrucev B., Kuehn H., Haeggstroem J.Z.
    J. Biol. Chem. 279:29023-29030(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HEPOXILIN A3 SYNTHESIS.
  5. "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.

Entry informationi

Entry nameiLOX15_RAT
AccessioniPrimary (citable) accession number: Q02759
Secondary accession number(s): F1MA51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 16, 2013
Last modified: September 3, 2014
This is version 121 of the entry and version 3 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

External Data

Dasty 3

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