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UniProtKB/Swiss-Prot entry P39655


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LOX12_MOUSE
Primary accession number P39655
Secondary accession number Q8BHG4
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on September 11, 2007 (Sequence version 4)
Annotations were last modified on    July 22, 2008 (Entry version 71)
Name and origin of the protein
Protein name Arachidonate 12-lipoxygenase, 12S-type
Synonyms 12-LOX
EC 1.13.11.31
Platelet-type lipoxygenase 12
Gene name
Name: Alox12
Synonyms: Alox12p
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF ILE-663.
STRAIN=C57BL/6, and ICR;
TISSUE=Spleen;
PubMed=8188678 [NCBI, ExPASy, EBI, Israel, Japan]
Chen X.-S., Kurre U., Jenkins N.A., Copeland N.G., Funk C.D.;
"cDNA cloning, expression, mutagenesis of C-terminal isoleucine, genomic structure, and chromosomal localizations of murine 12-lipoxygenases.";
J. Biol. Chem. 269:13979-13987(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7576099 [NCBI, ExPASy, EBI, Israel, Japan]
Krieg P., Kinzig A., Ress-Loschke M., Vogel S., Vanlandingham B., Stephan M., Lehmann W.D., Marks F., Furstenberger G.;
"12-lipoxygenase isoenzymes in mouse skin tumor development.";
Mol. Carcinog. 14:118-129(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Ovary, and Vagina;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 126-218.
TISSUE=Lung;
DOI=10.1016/0090-6980(94)00005-H; PubMed=7792391 [NCBI, ExPASy, EBI, Israel, Japan]
Hagmann W., Gao X., Zacharek A., Wojciechowski L.A., Honn K.V.;
"12-lipoxygenase in Lewis lung carcinoma cells: molecular identity, intracellular distribution of activity and protein, and Ca(2+)-dependent translocation from cytosol to membranes.";
Prostaglandins 49:49-62(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U04334; AAA20659.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S80446; AAB36013.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK036898; BAC29629.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK087724; BAC39981.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669869; CAI35235.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S77511; AAB34667.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A54075; A54075.
RefSeq NP_031466.2; -.
UniGene Mm.12286
3D structure databases
HSSP P12530; 1LOX. [HSSP ENTRY / PDB]
ModBase P39655.
Organism-specific databases
MGI MGI:87998; Alox12.
Gene expression databases
ArrayExpress P39655; -.
CleanEx MM_ALOX12; -.
GermOnline ENSMUSG00000000320; Mus musculus.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from sequence or structural similarity from UniProtKB).
GO:0042383; Cellular component: sarcolemma (inferred from sequence or structural similarity from UniProtKB).
GO:0004052; Molecular function: arachidonate 12-lipoxygenase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0047977; Molecular function: hepoxilin-epoxide hydrolase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (inferred from mutant phenotype from UniProtKB).
GO:0006928; Biological process: cell motion (inferred from sequence or structural similarity from UniProtKB).
GO:0019395; Biological process: fatty acid oxidation (inferred from sequence or structural similarity from UniProtKB).
GO:0045785; Biological process: positive regulation of cell adhesion (inferred from sequence or structural similarity from UniProtKB).
GO:0030307; Biological process: positive regulation of cell growth (inferred from sequence or structural similarity from UniProtKB).
GO:0008284; Biological process: positive regulation of cell proliferation (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000907; LipOase.
IPR013819; LipOase_C.
IPR001024; LipOase_LH2.
IPR001885; LipOase_mml.
Graphical view of domain structure.
Gene3D G3DSA:2.60.60.20; Lipase_LipOase; 1.
PANTHER PTHR11771; LipOase; 1.
Pfam PF00305; Lipoxygenase; 1.
PF01477; PLAT; 1.
Pfam graphical view of domain structure.
PRINTS PR00087; LIPOXYGENASE.
PR00467; MAMLPOXGNASE.
SMART SM00308; LH2; 1.
SMART graphical view of domain structure.
PROSITE PS00711; LIPOXYGENASE_1; 1.
PS00081; LIPOXYGENASE_2; 1.
PS50095; PLAT; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P39655.
Genome annotation databases
Ensembl ENSMUSG00000000320; Mus musculus. [Contig view]
GeneID 11684; -.
KEGG mmu:11684; -.
Phylogenomic databases
HOGENOM P39655; -.
HOVERGEN P39655; -.
Other
SOURCE Alox12; Mus musculus.
ProtoNet P39655.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Dioxygenase; Iron; Leukotriene biosynthesis; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   663  662     Arachidonate 12-lipoxygenase, 12S-type. PRO_0000220683
DOMAIN   2   114  113     PLAT. 
METAL   360   360        Iron (catalytic) (By similarity). 
METAL   365   365        Iron (catalytic) (By similarity). 
METAL   540   540        Iron (catalytic) (By similarity). 
METAL   544   544        Iron (catalytic) (By similarity). 
METAL   663   663        Iron (via carboxylate) (catalytic) (By similarity). 
MUTAGEN   663   663        I->D,R,K,G: Loss of activity. 
MUTAGEN   663   663        I->S,N: Little activity (8-15%). 
MUTAGEN   663   663        I->V: Nearly full activity. 
CONFLICT   3     3        R -> A (in Ref. 1; AAA20659). 
CONFLICT   112   112        T -> Q (in Ref. 1; AAA20659 and 2; AAB36013). 
CONFLICT   403   403        S -> T (in Ref. 1; AAA20659 and 2; AAB36013). 
Sequence information
Length: 663 AA [This is the length of the unprocessed precursor] Molecular weight: 75390 Da [This is the MW of the unprocessed precursor] CRC64: 205BE32BE2CF3E87 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGRYRVRVVT GAWLFSGSLN LVRLWLVGEH REAKLELQLR PARGKEEEFD FDVPEDLGPL 

        70         80         90        100        110        120 
QFVKLHKQHT VVDDAWFCNL ITVQGPGTSA EAVFPCYRWV QGEGILSLPE GTARLAGDNA 

       130        140        150        160        170        180 
LDVFQKYREK ELKERQQTYC WATWKEGLPQ TIAADCKDDL PPNMRFHEEK RLDFEWTLKA 

       190        200        210        220        230        240 
GVLEMGLKRV YTLLRSWNHL EDFDQIFWGQ KSALAEKVHQ CWQEDELFGY QFLNGANPML 

       250        260        270        280        290        300 
LRRSTSLPSR LVLPSGMEEL QAQLEKELKN GSLFEADFIL LDGIPANVIR GEPQYLAAPL 

       310        320        330        340        350        360 
VMLRMDPGGK LLPMAIQIQP PNPSSPAPTL FLPSDPPLAW LLAKIWVRNS DFQLQELQFH 

       370        380        390        400        410        420 
LLNTHLVAEV IAVATMRCLP GLHPIFKLLV PHIRYTMEIN TRSRTQLISD GGIFDQVVST 

       430        440        450        460        470        480 
GGGGHVQLLT RAVAQLTYHS LCPPDDLANR GLLRIPSALY ARDALQLWEV TARYVKGMVH 

       490        500        510        520        530        540 
LFYQSDDIVR GDPELQAWCR EITEVGLCHA QDRGFPVSFQ SRAQLCHFLT MCVFTCTAQH 

       550        560        570        580        590        600 
AAINQGQLDW YGWVPNAPCT MRMPPPTSKD DVTMETVMGS LPDVQKACLQ MTITWHLGRL 

       610        620        630        640        650        660 
QPDMVPLGHH TEKYFSDPRT KAVLSQFQAD LDNLEKEITA RNEQLDLPYE YLKPSRIENS 


ITI 

P39655 in FASTA format

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View entry in raw text format (no links)
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