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Protein

Arachidonate 15-lipoxygenase

Gene

Alox15

Organism
Mus musculus (Mouse)
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 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. In addition to 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.6 Publications

Catalytic activityi

Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.1 Publication
Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.1 Publication

Cofactori

Fe cationNote: Binds 1 Fe cation per subunit.

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 bindingi361 – 3611Iron; catalyticPROSITE-ProRule annotation
Metal bindingi366 – 3661Iron; catalyticPROSITE-ProRule annotation
Metal bindingi541 – 5411Iron; catalyticPROSITE-ProRule annotation
Metal bindingi545 – 5451Iron; catalyticPROSITE-ProRule annotation
Metal bindingi663 – 6631Iron; via carboxylate; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • apoptotic cell clearance Source: UniProtKB
  • arachidonic acid metabolic process Source: UniProtKB
  • bone mineralization Source: MGI
  • cellular response to calcium ion Source: UniProtKB
  • cellular response to interleukin-13 Source: UniProtKB
  • hepoxilin biosynthetic process Source: UniProtKB
  • lipoxin A4 biosynthetic process Source: UniProtKB
  • lipoxygenase pathway Source: UniProtKB
  • negative regulation of adaptive immune response Source: UniProtKB
  • ossification Source: MGI
  • phosphatidylethanolamine biosynthetic process Source: UniProtKB
  • positive regulation of actin filament polymerization Source: UniProtKB
  • positive regulation of cell-substrate adhesion Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of heterotypic cell-cell adhesion Source: Ensembl
  • regulation of engulfment of apoptotic cell Source: UniProtKB
  • regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
  • response to endoplasmic reticulum stress Source: UniProtKB
  • 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

BRENDAi1.13.11.31. 3474.
ReactomeiR-MMU-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-MMU-2142712. Synthesis of 12-eicosatetraenoic acid derivatives.
R-MMU-2142770. Synthesis of 15-eicosatetraenoic acid derivatives.
UniPathwayiUPA00881.

Names & Taxonomyi

Protein namesi
Recommended name:
Arachidonate 15-lipoxygenase (EC:1.13.11.331 Publication)
Short name:
15-LOX
Alternative name(s):
12/15-lipoxygenase
Short name:
12/15-LO
Arachidonate 12-lipoxygenase, leukocyte-type (EC:1.13.11.311 Publication)
Short name:
12-LOX
Short name:
L-12LO
Arachidonate omega-6 lipoxygenase
Gene namesi
Name:Alox15
Synonyms:Alox12l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:87997. Alox15.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  • lipid particle Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Lipid droplet, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are fertile and do not display overt phenotype. However, reduced endoplasmic reticulum stress response to high-fat diet is observed. Aged mice also display systemic autoimmunity, a significant and spontaneous production of several forms of autoantibodies being detected and glomerulonephritis and deposits of complement and immunoglobulins within their glomeruli being observed. They also display reduced bone mass.4 Publications

Chemistry

ChEMBLiCHEMBL3259476.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 663662Arachidonate 15-lipoxygenasePRO_0000220686Add
BLAST

Proteomic databases

MaxQBiP39654.
PaxDbiP39654.
PRIDEiP39654.

PTM databases

PhosphoSiteiP39654.

Expressioni

Tissue specificityi

Found in pituitary and pineal glands as well as leukocytes, kidney, aorta, small intestine and cornea. Also expressed by resident peritoneal macrophages (at protein level).4 Publications

Inductioni

Up-regulated in response to endoplasmic reticulum stress (at protein level).1 Publication

Gene expression databases

BgeeiP39654.
CleanExiMM_ALOX15.
ExpressionAtlasiP39654. baseline and differential.
GenevisibleiP39654. MM.

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

STRINGi10090.ENSMUSP00000019068.

Chemistry

BindingDBiP39654.

Structurei

3D structure databases

ProteinModelPortaliP39654.
SMRiP39654. Positions 2-663.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 115114PLATPROSITE-ProRule annotationAdd
BLAST
Domaini116 – 663548LipoxygenasePROSITE-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

eggNOGiENOG410IKAN. Eukaryota.
ENOG410YN4N. LUCA.
GeneTreeiENSGT00550000074415.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiP39654.
KOiK00460.
OMAiLTCWKDL.
OrthoDBiEOG7B05CG.
PhylomeDBiP39654.
TreeFamiTF105320.

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.

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

P39654-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVYRIRVST GDSVYAGSNN EVYLWLIGQH GEASLGKLFR PCRNSEAEFK
60 70 80 90 100
VDVSEYLGPL LFVRVQKWHY LKEDAWFCNW ISVKGPGDQG SEYTFPCYRW
110 120 130 140 150
VQGTSILNLP EGTGCTVVED SQGLFRNHRE EELEERRSLY RWGNWKDGTI
160 170 180 190 200
LNVAATSISD LPVDQRFRED KRLEFEASQV LGTMDTVINF PKNTVTCWKS
210 220 230 240 250
LDDFNYVFKS GHTKMAERVR NSWKEDAFFG YQFLNGANPM VLKRSTCLPA
260 270 280 290 300
RLVFPPGMEK LQAQLDEELK KGTLFEADFF LLDGIKANVI LCSQQYLAAP
310 320 330 340 350
LVMLKLQPDG QLLPIAIQLE LPKTGSTPPP IFTPLDPPMD WLLAKCWVRS
360 370 380 390 400
SDLQLHELQA HLLRGHLVAE VFAVATMRCL PSVHPVFKLL VPHLLYTMEI
410 420 430 440 450
NVRARSDLIS ERGFFDKVMS TGGGGHLDLL KQAGAFLTYS SLCPPDDLAE
460 470 480 490 500
RGLLDIDTCF YAKDALQLWQ VMNRYVVGMF DLYYKTDQAV QDDYELQSWC
510 520 530 540 550
QEITEIGLQG AQDRGFPTSL QSRAQACHFI TMCIFTCTAQ HSSIHLGQLD
560 570 580 590 600
WFYWVPNAPC TMRLPPPKTK DATMEKLMAT LPNPNQSTLQ INVVWLLGRR
610 620 630 640 650
QAVMVPLGQH SEEHFPNPEA KAVLKKFREE LAALDKEIEI RNKSLDIPYE
660
YLRPSLVENS VAI
Length:663
Mass (Da):75,445
Last modified:September 11, 2007 - v4
Checksum:i0D5412B4502B5799
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371K → N in AAA64930 (PubMed:7811740).Curated
Sequence conflicti119 – 1191E → Q in AAA64930 (PubMed:7811740).Curated
Sequence conflicti397 – 3971T → N in AAA64930 (PubMed:7811740).Curated
Sequence conflicti568 – 5681K → T in CAJ18471 (Ref. 4) Curated
Sequence conflicti568 – 5681K → T in AAH56625 (PubMed:15489334).Curated
Sequence conflicti568 – 5681K → T in AAH81546 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04331 mRNA. Translation: AAA20658.1.
L34570 mRNA. Translation: AAA64930.1.
AK142371 mRNA. Translation: BAE25045.1.
CT010263 mRNA. Translation: CAJ18471.1.
AL596096 Genomic DNA. Translation: CAI51979.1.
BC056625 mRNA. Translation: AAH56625.1.
BC081546 mRNA. Translation: AAH81546.1.
CCDSiCCDS24944.1.
PIRiB54075.
RefSeqiNP_033790.3. NM_009660.3.
UniGeneiMm.4584.

Genome annotation databases

EnsembliENSMUST00000019068; ENSMUSP00000019068; ENSMUSG00000018924.
GeneIDi11687.
KEGGimmu:11687.
UCSCiuc007juo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04331 mRNA. Translation: AAA20658.1.
L34570 mRNA. Translation: AAA64930.1.
AK142371 mRNA. Translation: BAE25045.1.
CT010263 mRNA. Translation: CAJ18471.1.
AL596096 Genomic DNA. Translation: CAI51979.1.
BC056625 mRNA. Translation: AAH56625.1.
BC081546 mRNA. Translation: AAH81546.1.
CCDSiCCDS24944.1.
PIRiB54075.
RefSeqiNP_033790.3. NM_009660.3.
UniGeneiMm.4584.

3D structure databases

ProteinModelPortaliP39654.
SMRiP39654. Positions 2-663.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000019068.

Chemistry

BindingDBiP39654.
ChEMBLiCHEMBL3259476.

PTM databases

PhosphoSiteiP39654.

Proteomic databases

MaxQBiP39654.
PaxDbiP39654.
PRIDEiP39654.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019068; ENSMUSP00000019068; ENSMUSG00000018924.
GeneIDi11687.
KEGGimmu:11687.
UCSCiuc007juo.1. mouse.

Organism-specific databases

CTDi246.
MGIiMGI:87997. Alox15.

Phylogenomic databases

eggNOGiENOG410IKAN. Eukaryota.
ENOG410YN4N. LUCA.
GeneTreeiENSGT00550000074415.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiP39654.
KOiK00460.
OMAiLTCWKDL.
OrthoDBiEOG7B05CG.
PhylomeDBiP39654.
TreeFamiTF105320.

Enzyme and pathway databases

UniPathwayiUPA00881.
BRENDAi1.13.11.31. 3474.
ReactomeiR-MMU-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-MMU-2142712. Synthesis of 12-eicosatetraenoic acid derivatives.
R-MMU-2142770. Synthesis of 15-eicosatetraenoic acid derivatives.

Miscellaneous databases

NextBioi279331.
PROiP39654.
SOURCEiSearch...

Gene expression databases

BgeeiP39654.
CleanExiMM_ALOX15.
ExpressionAtlasiP39654. baseline and differential.
GenevisibleiP39654. MM.

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

« Hide 'large scale' publications
  1. "cDNA cloning, expression, mutagenesis of C-terminal isoleucine, genomic structure, and chromosomal localizations of murine 12-lipoxygenases."
    Chen X.-S., Kurre U., Jenkins N.A., Copeland N.G., Funk C.D.
    J. Biol. Chem. 269:13979-13987(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Strain: C57BL/6J and ICR.
    Tissue: Spleen.
  2. "Cloning and characterization of a murine macrophage lipoxygenase."
    Freire-Moar J., Alavi-Nassab A., Ng M., Mulkins M., Sigal E.
    Biochim. Biophys. Acta 1254:112-116(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Macrophage.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung.
  4. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N and FVB/N-3.
    Tissue: Mammary tumor.
  7. "Disruption of 12/15-lipoxygenase expression in peritoneal macrophages. Enhanced utilization of the 5-lipoxygenase pathway and diminished oxidation of low density lipoprotein."
    Sun D., Funk C.D.
    J. Biol. Chem. 271:24055-24062(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  8. "Interleukin-4-dependent production of PPAR-gamma ligands in macrophages by 12/15-lipoxygenase."
    Huang J.T., Welch J.S., Ricote M., Binder C.J., Willson T.M., Kelly C., Witztum J.L., Funk C.D., Conrad D., Glass C.K.
    Nature 400:378-382(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MACROPHAGE.
  9. "12/15-lipoxygenase translocation enhances site-specific actin polymerization in macrophages phagocytosing apoptotic cells."
    Miller Y.I., Chang M.K., Funk C.D., Feramisco J.R., Witztum J.L.
    J. Biol. Chem. 276:19431-19439(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIN REGULATION, SUBCELLULAR LOCATION.
  10. Cited for: FUNCTION IN BONE DEVELOPMENT, DISRUPTION PHENOTYPE.
  11. "A role for the mouse 12/15-lipoxygenase pathway in promoting epithelial wound healing and host defense."
    Gronert K., Maheshwari N., Khan N., Hassan I.R., Dunn M., Laniado Schwartzman M.
    J. Biol. Chem. 280:15267-15278(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HEALING, TISSUE SPECIFICITY.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung and Spleen.
  13. "12/15-Lipoxygenase signaling in the endoplasmic reticulum stress response."
    Cole B.K., Kuhn N.S., Green-Mitchell S.M., Leone K.A., Raab R.M., Nadler J.L., Chakrabarti S.K.
    Am. J. Physiol. 302:E654-E665(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ER STRESS RESPONSE, DISRUPTION PHENOTYPE, INDUCTION.
  14. "12/15-lipoxygenase orchestrates the clearance of apoptotic cells and maintains immunologic tolerance."
    Uderhardt S., Herrmann M., Oskolkova O.V., Aschermann S., Bicker W., Ipseiz N., Sarter K., Frey B., Rothe T., Voll R., Nimmerjahn F., Bochkov V.N., Schett G., Kroenke G.
    Immunity 36:834-846(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOTIC CELL CLEARANCE, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiLOX15_MOUSE
AccessioniPrimary (citable) accession number: P39654
Secondary accession number(s): Q4FJY9, Q5F2E3, Q6PHB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: September 11, 2007
Last modified: January 20, 2016
This is version 140 of the entry and version 4 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.