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P39655

- LOX12_MOUSE

UniProt

P39655 - LOX12_MOUSE

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Protein
Arachidonate 12-lipoxygenase, 12S-type
Gene
Alox12, Alox12p
Organism
Mus musculus (Mouse)
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. Mainly converts arachidonic acid to (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE but can also metabolize linoleic acid. Has a dual activity since it also converts leukotriene A4/LTA4 into both the bioactive lipoxin A4/LXA4 and lipoxin B4/LXB4. Through the production of specific bioactive lipids like (12S)-HPETE it regulates different biological processes including platelet activation. It also probably positively regulates angiogenesis through regulation of the expression of the vascular endothelial growth factor. Plays a role in apoptotic process, promoting the survival of vascular smooth muscle cells for instance. May also play a role in the control of cell migration and proliferation.1 Publication

Catalytic activityi

Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.1 Publication
(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (5S,6R,15S)-trihydroxy-(7E,9E,11Z,13E)-eicosatetraenoate.1 Publication
(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (5S,14R,15S)-trihydroxy-(6E,8Z,10E,12E)-eicosatetraenoate.

Cofactori

Binds 1 iron ion per subunit.

Enzyme regulationi

Activated by EGF By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi360 – 3601Iron; catalytic By similarity
Metal bindingi365 – 3651Iron; catalytic By similarity
Metal bindingi540 – 5401Iron; catalytic By similarity
Metal bindingi544 – 5441Iron; catalytic By similarity
Metal bindingi663 – 6631Iron; via carboxylate; catalytic By similarity

GO - Molecular functioni

  1. arachidonate 12-lipoxygenase activity Source: UniProtKB
  2. hepoxilin-epoxide hydrolase activity Source: UniProtKB
  3. iron ion binding Source: InterPro
  4. linoleate 13S-lipoxygenase activity Source: Ensembl

GO - Biological processi

  1. aging Source: Ensembl
  2. arachidonic acid metabolic process Source: UniProtKB
  3. cellular component movement Source: UniProtKB
  4. cellular response to lipid Source: Ensembl
  5. establishment of skin barrier Source: UniProtKB
  6. fatty acid oxidation Source: UniProtKB
  7. hepoxilin biosynthetic process Source: UniProtKB
  8. leukotriene A4 metabolic process Source: UniProtKB
  9. linoleic acid metabolic process Source: UniProtKB
  10. lipoxin A4 biosynthetic process Source: UniProtKB
  11. lipoxin B4 biosynthetic process Source: UniProtKB
  12. lipoxygenase pathway Source: UniProtKB
  13. negative regulation of apoptotic process Source: UniProtKB
  14. negative regulation of muscle cell apoptotic process Source: UniProtKB
  15. negative regulation of platelet aggregation Source: UniProtKB
  16. positive regulation of angiogenesis Source: UniProtKB
  17. positive regulation of apoptotic process Source: UniProtKB
  18. positive regulation of cell adhesion Source: UniProtKB
  19. positive regulation of cell growth Source: UniProtKB
  20. positive regulation of cell migration Source: UniProtKB
  21. positive regulation of cell proliferation Source: UniProtKB
  22. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  23. positive regulation of endothelial cell differentiation Source: Ensembl
  24. positive regulation of endothelial cell migration Source: Ensembl
  25. positive regulation of gene expression Source: Ensembl
  26. positive regulation of mitochondrial depolarization Source: Ensembl
  27. positive regulation of smooth muscle cell proliferation Source: Ensembl
  28. positive regulation of vasodilation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Hydrolase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196544. Synthesis of Lipoxins (LX).
REACT_196560. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
REACT_196569. Synthesis of 12-eicosatetraenoic acid derivatives.
UniPathwayiUPA00881.

Names & Taxonomyi

Protein namesi
Recommended name:
Arachidonate 12-lipoxygenase, 12S-type (EC:1.13.11.31)
Short name:
12S-LOX
Short name:
12S-lipoxygenase
Alternative name(s):
Lipoxin synthase 12-LO (EC:3.3.2.-)
Platelet-type lipoxygenase 12
Short name:
P-12LO
Gene namesi
Name:Alox12
Synonyms:Alox12p
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:87998. Alox12.

Subcellular locationi

Cytoplasmcytosol. Membrane By similarity
Note: Membrane association is stimulated by EGF By similarity.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB-SubCell
  3. membrane Source: UniProtKB
  4. sarcolemma Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are fertile and appear to exhibit no gross abnormalities. However, they display increased aggregation of platelets in response to ADP. They also display a mild basal transepidermal water loss.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi663 – 6631I → D, R, K or G: Loss of activity. 1 Publication
Mutagenesisi663 – 6631I → S or N: Little activity (8-15%). 1 Publication
Mutagenesisi663 – 6631I → V: Nearly full activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 663663Arachidonate 12-lipoxygenase, 12S-type
PRO_0000220683Add
BLAST

Proteomic databases

MaxQBiP39655.
PaxDbiP39655.
PRIDEiP39655.

PTM databases

PhosphoSiteiP39655.

Expressioni

Tissue specificityi

Found primarily in platelets and in microsomal and cytosolic fractions of the epidermis (at protein level).3 Publications

Gene expression databases

ArrayExpressiP39655.
BgeeiP39655.
CleanExiMM_ALOX12.
GenevestigatoriP39655.

Interactioni

Structurei

3D structure databases

ProteinModelPortaliP39655.
SMRiP39655. Positions 2-663.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 114113PLAT
Add
BLAST
Domaini115 – 663549Lipoxygenase
Add
BLAST

Sequence similaritiesi

Belongs to the lipoxygenase family.
Contains 1 PLAT domain.

Phylogenomic databases

eggNOGiNOG69653.
GeneTreeiENSGT00550000074415.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiP39655.
KOiK00458.
OMAiQNQLCHF.
OrthoDBiEOG7B05CG.
PhylomeDBiP39655.
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. 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.

P39655-1 [UniParc]FASTAAdd to Basket

« Hide

MGRYRVRVVT GAWLFSGSLN LVRLWLVGEH REAKLELQLR PARGKEEEFD    50
FDVPEDLGPL QFVKLHKQHT VVDDAWFCNL ITVQGPGTSA EAVFPCYRWV 100
QGEGILSLPE GTARLAGDNA LDVFQKYREK ELKERQQTYC WATWKEGLPQ 150
TIAADCKDDL PPNMRFHEEK RLDFEWTLKA GVLEMGLKRV YTLLRSWNHL 200
EDFDQIFWGQ KSALAEKVHQ CWQEDELFGY QFLNGANPML LRRSTSLPSR 250
LVLPSGMEEL QAQLEKELKN GSLFEADFIL LDGIPANVIR GEPQYLAAPL 300
VMLRMDPGGK LLPMAIQIQP PNPSSPAPTL FLPSDPPLAW LLAKIWVRNS 350
DFQLQELQFH LLNTHLVAEV IAVATMRCLP GLHPIFKLLV PHIRYTMEIN 400
TRSRTQLISD GGIFDQVVST GGGGHVQLLT RAVAQLTYHS LCPPDDLANR 450
GLLRIPSALY ARDALQLWEV TARYVKGMVH LFYQSDDIVR GDPELQAWCR 500
EITEVGLCHA QDRGFPVSFQ SRAQLCHFLT MCVFTCTAQH AAINQGQLDW 550
YGWVPNAPCT MRMPPPTSKD DVTMETVMGS LPDVQKACLQ MTITWHLGRL 600
QPDMVPLGHH TEKYFSDPRT KAVLSQFQAD LDNLEKEITA RNEQLDLPYE 650
YLKPSRIENS ITI 663
Length:663
Mass (Da):75,390
Last modified:September 11, 2007 - v4
Checksum:i205BE32BE2CF3E87
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31R → A in AAA20659. 1 Publication
Sequence conflicti112 – 1121T → Q in AAA20659. 1 Publication
Sequence conflicti112 – 1121T → Q in AAB36013. 1 Publication
Sequence conflicti403 – 4031S → T in AAA20659. 1 Publication
Sequence conflicti403 – 4031S → T in AAB36013. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U04334 mRNA. Translation: AAA20659.1.
S80446 mRNA. Translation: AAB36013.1.
AK036898 mRNA. Translation: BAC29629.1.
AK087724 mRNA. Translation: BAC39981.1.
AL669869 Genomic DNA. Translation: CAI35235.1.
S77511 mRNA. Translation: AAB34667.1.
CCDSiCCDS24942.1.
PIRiA54075.
RefSeqiNP_031466.2. NM_007440.4.
UniGeneiMm.12286.

Genome annotation databases

EnsembliENSMUST00000000329; ENSMUSP00000000329; ENSMUSG00000000320.
GeneIDi11684.
KEGGimmu:11684.
UCSCiuc007juj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U04334 mRNA. Translation: AAA20659.1 .
S80446 mRNA. Translation: AAB36013.1 .
AK036898 mRNA. Translation: BAC29629.1 .
AK087724 mRNA. Translation: BAC39981.1 .
AL669869 Genomic DNA. Translation: CAI35235.1 .
S77511 mRNA. Translation: AAB34667.1 .
CCDSi CCDS24942.1.
PIRi A54075.
RefSeqi NP_031466.2. NM_007440.4.
UniGenei Mm.12286.

3D structure databases

ProteinModelPortali P39655.
SMRi P39655. Positions 2-663.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P39655.
ChEMBLi CHEMBL3225.

PTM databases

PhosphoSitei P39655.

Proteomic databases

MaxQBi P39655.
PaxDbi P39655.
PRIDEi P39655.

Protocols and materials databases

DNASUi 11684.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000000329 ; ENSMUSP00000000329 ; ENSMUSG00000000320 .
GeneIDi 11684.
KEGGi mmu:11684.
UCSCi uc007juj.1. mouse.

Organism-specific databases

CTDi 239.
MGIi MGI:87998. Alox12.

Phylogenomic databases

eggNOGi NOG69653.
GeneTreei ENSGT00550000074415.
HOGENOMi HOG000234358.
HOVERGENi HBG005150.
InParanoidi P39655.
KOi K00458.
OMAi QNQLCHF.
OrthoDBi EOG7B05CG.
PhylomeDBi P39655.
TreeFami TF105320.

Enzyme and pathway databases

UniPathwayi UPA00881 .
Reactomei REACT_196544. Synthesis of Lipoxins (LX).
REACT_196560. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
REACT_196569. Synthesis of 12-eicosatetraenoic acid derivatives.

Miscellaneous databases

NextBioi 279319.
PROi P39655.
SOURCEi Search...

Gene expression databases

ArrayExpressi P39655.
Bgeei P39655.
CleanExi MM_ALOX12.
Genevestigatori P39655.

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. 1 hit.
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. "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, MUTAGENESIS OF ILE-663, TISSUE SPECIFICITY.
    Strain: C57BL/6 and ICR.
    Tissue: Spleen.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Ovary and Vagina.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "12-lipoxygenase in Lewis lung carcinoma cells: molecular identity, intracellular distribution of activity and protein, and Ca(2+)-dependent translocation from cytosol to membranes."
    Hagmann W., Gao X., Zacharek A., Wojciechowski L.A., Honn K.V.
    Prostaglandins 49:49-62(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 126-218.
    Tissue: Lung.
  6. "Immunocytochemical localization of platelet-type arachidonate 12-lipoxygenase in mouse blood cells."
    Nakamura M., Ueda N., Kishimoto K., Yoshimoto T., Yamamoto S., Ishimura K.
    J. Histochem. Cytochem. 43:237-244(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Increased platelet sensitivity to ADP in mice lacking platelet-type 12-lipoxygenase."
    Johnson E.N., Brass L.F., Funk C.D.
    Proc. Natl. Acad. Sci. U.S.A. 95:3100-3105(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PLATELET ACTIVATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  8. "Basal transepidermal water loss is increased in platelet-type 12-lipoxygenase deficient mice."
    Johnson E.N., Nanney L.B., Virmani J., Lawson J.A., Funk C.D.
    J. Invest. Dermatol. 112:861-865(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiLOX12_MOUSE
AccessioniPrimary (citable) accession number: P39655
Secondary accession number(s): Q8BHG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: September 11, 2007
Last modified: September 3, 2014
This is version 125 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

External Data

Dasty 3

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