Reviewed, UniProtKB/Swiss-Prot Q02759 (LX12L_RAT)

Names and origin

Protein names

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

Gene names

Name:	Alox12l
Synonyms:	Alox12, Alox15

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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 transcript level.

General annotation (Comments)

Function	Oxygenase and 14,15-leukotriene A4 synthase activity. Converts arachidonic acid to 12-hydroperoxyeicosatetraenoic acid (12-HPETE) and 15-hydroperoxyeicosatetraenoic acid (15-HPETE) in a 3:1 ratio. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid By similarity.
Catalytic activity	Arachidonate + O(2) = (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	Detected in leukocytes, lung and aorta.
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 sequence or structural similarity. Source: UniProtKB arachidonic acid metabolic process Non-traceable author statement. Source: UniProtKB fatty acid oxidation Inferred from sequence or structural similarity. Source: UniProtKB leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell volume Traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB regulation of membrane potential Traceable author statement. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB sarcolemma Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	arachidonate 12-lipoxygenase activity Inferred from electronic annotation. Source: EC hepoxilin-epoxide hydrolase activity Inferred from direct assay. Source: UniProtKB iron ion binding Inferred from electronic annotation. Source: InterPro lipoxygenase activity Inferred from electronic annotation. Source: InterPro potassium channel inhibitor activity Traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 663	662	Arachidonate 12-lipoxygenase, leukocyte-type		PRO_0000220687
Regions
	Domain	2 – 115	114	PLAT
	Domain	116 – 663	548	Lipoxygenase
Sites
	Metal binding	361	1	Iron; catalytic By similarity
	Metal binding	366	1	Iron; catalytic By similarity
	Metal binding	541	1	Iron; catalytic By similarity
	Metal binding	663	1	Iron; via carboxylate; catalytic By similarity
Experimental info
	Sequence conflict	55	1	E → G in AAB30132. Ref.2
	Sequence conflict	371	1	L → V in AAB30132. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q02759-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 91D8FB4547A3948D	FASTA	663	75,392
	10 20 30 40 50 60 MGVYRIRVST GDSKYAGSNN EVYLWLVGQH GEASLGKLLR PCRDSEAEFK VDVSEYLGPL 70 80 90 100 110 120 LFVRVQKWHY LTDDAWFCNW ISVKGPGDQG SEYMFPCYRW VQGRSILSLP EGTGCTVVED 130 140 150 160 170 180 SQGLFRKHRE EELEERRSLY RWGNWKDGSI LNVAAASISD LPVDQRFRED KRIEFEASQV 190 200 210 220 230 240 IGVMDTVVNF PINTVTCWKS LDDFNCVFKS GHTKMAERVR NSWKEDAFFG YQFLNGANPM 250 260 270 280 290 300 VLKRSTCLPA RLVFPPGMEK LQAQLNKELQ KGTLFEADFF LLDGIKANVI LCSQQYLAAP 310 320 330 340 350 360 LVMLKLMPDG QLLPIAIQLE LPKTGSTPPP IFTPSDPPMD WLLAKCWVRS SDLQLHELQA 370 380 390 400 410 420 HLLRGHLMAE LFAVATMRCL PSVHPVFKLL VPHLLYTMEI NVRARSDLIS ERGFFDKAMS 430 440 450 460 470 480 TGGGGHLDLL KQAGAFLTYC SLCPPDDLAE RGLLDIETCF YAKDALRLWQ IMNRYVVGMF 490 500 510 520 530 540 NLHYKTDKAV QDDYELQSWC REITDIGLQG AQDRGFPTSL QSRAQACYFI TMCIFTCTAQ 550 560 570 580 590 600 HSSVHLGQLD WFYWVPNAPC TMRLPPPTTK EATMEKLMAT LPNPNQSTLQ INVVWLLGRR 610 620 630 640 650 660 QAVMVPLGQH SEEHFPNPEA KAVLKKFREE LAALDKEIEI RNKSLDIPYE YLRPSMVENS VAI

References

[1]

"Molecular cloning of a 12-lipoxygenase cDNA from rat brain." Watanabe T., Medina J.F., Haeggstroem J.Z., Raadmark O.P., Samuelsson B. Eur. J. Biochem. 212:605-612(1993) [PubMed: 8444196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Strain: Sprague-Dawley. Tissue: Brain.

[2]

"Arachidonate 12-lipoxygenase of rat pineal glands: catalytic properties and primary structure deduced from its cDNA." Hada T., Hagiya H., Suzuki H., Arakawa T., Nakamura M., Matsuda S., Yoshimoto T., Yamamoto S., Azekawa T., Morita Y., Ishimura K., Kim H.Y. Biochim. Biophys. Acta 1211:221-228(1994) [PubMed: 8117750] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION. Tissue: Pineal gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L06040 mRNA. Translation: AAA41532.1. S69383 mRNA. Translation: AAB30132.1.
PIR	I52462. S30051.
RefSeq	NP_112272.2.
UniGene	Rn.11318
3D structure databases
HSSP	HSSP built from PDB template 1LOX based on UniProtKB P12530.
SMR	Q02759. Positions 2-663.
ModBase	Search...
Genome annotation databases
Ensembl	ENSRNOG00000019183. Rattus norvegicus. [Contig view]
GeneID	81639.
KEGG	rno:81639.
Organism-specific databases
RGD	70493. Alox15.
Phylogenomic databases
HOVERGEN	Q02759.
Gene expression databases
ArrayExpress	Q02759.
GermOnline	ENSRNOG00000019183. Rattus norvegicus.
Family and domain databases
InterPro	IPR000907. LipOase. IPR013819. LipOase_C. 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	615136.

Entry information

Entry name

LX12L_RAT

Accession

Primary (citable) accession number: Q02759

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)