Reviewed, UniProtKB/Swiss-Prot P39655 (LOX12_MOUSE)

Names and origin

Protein names

Recommended name:
    Arachidonate 12-lipoxygenase, 12S-type
      Short name=12S-lipoxygenase
      Short name=12S-LOX
    EC=1.13.11.31
Alternative name(s):
    Platelet-type lipoxygenase 12

Gene names

Name:	Alox12
Synonyms:	Alox12p

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	663 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Oxygenase and 14,15-leukotriene A4 synthase activity.
Catalytic activity	Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.
Cofactor	Binds 1 iron ion per subunit.
Pathway	Lipid metabolism; leukotriene D4 biosynthesis.
Subcellular location	Cytoplasm.
Tissue specificity	Found primarily in platelets and in microsomal and cytosolic fractions of the epidermis.
Sequence similarities	Belongs to the lipoxygenase family. Contains 1 lipoxygenase domain. Contains 1 PLAT domain.

Ontologies

Keywords
Biological process	Leukotriene biosynthesis
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	anti-apoptosis Inferred from mutant phenotype. Source: UniProtKB cellular component movement Inferred from sequence or structural similarity. Source: UniProtKB fatty acid oxidation Inferred from sequence or structural similarity. Source: UniProtKB leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell proliferation Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB sarcolemma Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	arachidonate 12-lipoxygenase activity Inferred from sequence or structural similarity. Source: UniProtKB hepoxilin-epoxide hydrolase activity Inferred from sequence or structural similarity. Source: UniProtKB iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW lipoxygenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 663	662	Arachidonate 12-lipoxygenase, 12S-type		PRO_0000220683
Regions
	Domain	2 – 114	113	PLAT
	Domain	115 – 663	549	Lipoxygenase
Sites
	Metal binding	360	1	Iron; catalytic By similarity
	Metal binding	365	1	Iron; catalytic By similarity
	Metal binding	540	1	Iron; catalytic By similarity
	Metal binding	544	1	Iron; catalytic By similarity
	Metal binding	663	1	Iron; via carboxylate; catalytic By similarity
Experimental info
	Mutagenesis	663	1	I → D, R, K or G: Loss of activity. Ref.1
	Mutagenesis	663	1	I → S or N: Little activity (8-15%). Ref.1
	Mutagenesis	663	1	I → V: Nearly full activity. Ref.1
	Sequence conflict	3	1	R → A in AAA20659. Ref.1
	Sequence conflict	112	1	T → Q in AAA20659. Ref.1
	Sequence conflict	112	1	T → Q in AAB36013. Ref.2
	Sequence conflict	403	1	S → T in AAA20659. Ref.1
	Sequence conflict	403	1	S → T in AAB36013. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P39655-1 [UniParc]. Last modified September 11, 2007. Version 4. Checksum: 205BE32BE2CF3E87	FASTA	663	75,390
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8188678] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF ILE-663. Strain: C57BL/6 and ICR. Tissue: Spleen.
[2]	"12-lipoxygenase isoenzymes in mouse skin tumor development." Krieg P., Kinzig A., Ress-Loschke M., Vogel S., Vanlandingham B., Stephan M., Lehmann W.D., Marks F., Furstenberger G. Mol. Carcinog. 14:118-129(1995) [PubMed: 7576099] [Abstract] 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Ovary and Vagina.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] 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: 7792391] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 126-218. Tissue: Lung.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00308268.
PIR	A54075.
RefSeq	NP_031466.2.
UniGene	Mm.12286
3D structure databases
SMR	P39655. Positions 2-663.
ModBase	Search...
Protein-protein interaction databases
STRING	P39655.
Proteomic databases
PRIDE	P39655.
Genome annotation databases
Ensembl	ENSMUST00000000329; ENSMUSP00000000329; ENSMUSG00000000320; Mus musculus. [Genome view]
GeneID	11684.
KEGG	mmu:11684.
Organism-specific databases
CTD	11684.
MGI	MGI:87998. Alox12.
Phylogenomic databases
HOGENOM	HBG443995.
HOVERGEN	P39655.
InParanoid	P39655.
OMA	HHKEKYF.
OrthoDB	EOG9ZW7WF.
PhylomeDB	P39655.
Enzyme and pathway databases
BRENDA	1.13.11.31. 244.
Gene expression databases
ArrayExpress	P39655.
Bgee	P39655.
CleanEx	MM_ALOX12.
Genevestigator	P39655.
GermOnline	ENSMUSG00000000320. Mus musculus.
Family and domain databases
InterPro	IPR008976. Lipase_LipOase. IPR000907. LipOase. IPR013819. LipOase_C. IPR020834. LipOase_CS. IPR020833. LipOase_Fe_BS. IPR001024. LipOase_LH2. IPR001885. LipOase_mml. [Graphical view]
Gene3D	G3DSA:2.60.60.20. Lipase_LipOase. 1 hit.
PANTHER	PTHR11771. LipOase. 1 hit.
Pfam	PF00305. Lipoxygenase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view]
PRINTS	PR00087. LIPOXYGENASE. PR00467. MAMLPOXGNASE.
SMART	SM00308. LH2. 1 hit. [Graphical view]
PROSITE	PS00711. LIPOXYGENASE_1. 1 hit. PS00081. LIPOXYGENASE_2. 1 hit. PS51393. LIPOXYGENASE_3. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	279319.
SOURCE	Search...

Entry information

Entry name

LOX12_MOUSE

Accession

Primary (citable) accession number: P39655
Secondary accession number(s): Q8BHG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	September 11, 2007
Last modified:	February 9, 2010
This is version 89 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)