P39655 (LOX12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arachidonate 12-lipoxygenase, 12S-type
Short name=12S-LOX
Short name=12S-lipoxygenase
EC=1.13.11.31

Alternative name(s):
Platelet-type lipoxygenase 12

Gene names

Name:	Alox12
Synonyms:	Alox12p

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › 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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from electronic annotation. Source: Compara cellular component movement Inferred from sequence or structural similarity. Source: UniProtKB cellular response to lipid Inferred from electronic annotation. Source: Compara fatty acid oxidation Inferred from sequence or structural similarity. Source: UniProtKB leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of apoptotic process Inferred from mutant phenotype PubMed 15161019. Source: UniProtKB positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara 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 PubMed 15161019. Source: UniProtKB positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of endothelial cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of endothelial cell migration Inferred from electronic annotation. Source: Compara positive regulation of gene expression Inferred from electronic annotation. Source: Compara positive regulation of mitochondrial depolarization Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of vasodilation Inferred from electronic annotation. Source: Compara
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: InterPro 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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. NM_007440.4.
UniGene	Mm.12286.
3D structure databases
ProteinModelPortal	P39655.
SMR	P39655. Positions 2-663.
ModBase	Search...
PTM databases
PhosphoSite	P39655.
Proteomic databases
PaxDb	P39655.
PRIDE	P39655.
Protocols and materials databases
DNASU	11684.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000000329; ENSMUSP00000000329; ENSMUSG00000000320.
GeneID	11684.
KEGG	mmu:11684.
Organism-specific databases
CTD	239.
MGI	MGI:87998. Alox12.
Phylogenomic databases
eggNOG	NOG69653.
GeneTree	ENSGT00550000074415.
HOGENOM	HOG000234358.
HOVERGEN	HBG005150.
InParanoid	P39655.
KO	K00458.
OMA	HHKEKYF.
OrthoDB	EOG4W0XCM.
Enzyme and pathway databases
UniPathway	UPA00880.
Gene expression databases
ArrayExpress	P39655.
Bgee	P39655.
CleanEx	MM_ALOX12.
Genevestigator	P39655.
GermOnline	ENSMUSG00000000320. Mus musculus.
Family and domain databases
Gene3D	2.60.60.20. 1 hit.
InterPro	IPR008976. Lipase_LipOase. IPR000907. LipOase. IPR013819. LipOase_C. IPR020834. LipOase_CS. IPR020833. LipOase_Fe_BS. IPR001024. LipOase_LH2. IPR001885. LipOase_mml. [Graphical view]
PANTHER	PTHR11771. PTHR11771. 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]
SUPFAM	SSF49723. Lipase_LipOase. 1 hit. SSF48484. Lipoxygenase. 1 hit.
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
BindingDB	P39655.
ChEMBL	CHEMBL3225.
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:	April 3, 2013
This is version 113 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program