Reviewed, UniProtKB/Swiss-Prot P16469 (LOX12_PIG)

Names and origin

Protein names

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

Gene names

Name:

ALOX12

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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	Leukocytes, pituitary gland, lung and in very small amount in jejunum and spleen.
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	Direct protein sequencing
Gene Ontology (GO)
Biological process	leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	arachidonate 12-lipoxygenase activity Inferred from electronic annotation. Source: EC 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
	Chain	2 – 663	662	Arachidonate 12-lipoxygenase, 12S-type		PRO_0000220684
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

Sequences

	Sequence		Length	Mass (Da)
	P16469-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A06B655D6E6BAA36	FASTA	663	75,043
	10 20 30 40 50 60 MGLYRVRVST GSSFYAGSQN QVQLWLVGQH GEAALGWCLR PARGKETEFS VDVSEYLGPL 70 80 90 100 110 120 LFVKLRKRHL LQDDAWFCNW ISVQGPGANG DEFRFPCYRW VEGDRILSLP EGTARTVVDD 130 140 150 160 170 180 PQGLFKKHRE EELAERRKLY RWGNWKDGLI LNIASTGIHD LPVDERFLED KRIDFEASLA 190 200 210 220 230 240 KGLADLAVKD SLNVLMSWNS LDSFNRIFWC GQSKLAEQVR DSWKEDALFG YQFLNGTNPM 250 260 270 280 290 300 LLRHSVELPA RLKFPPGMEE LQAQLEKELQ GGTLFEADFS LLDGIKANVI LCSQQYLAVP 310 320 330 340 350 360 LVMLKLQPDG KLLPMVIQLQ LPREGSPLPP LFLPTDPPMV WLLAKCWVRS SDFQLHELHS 370 380 390 400 410 420 HLLRGHLMAE VIAVATMRCL PSIHPIFKLL IPHFRYTMEI NVRARNGLVS DLGIFDQVVS 430 440 450 460 470 480 TGGGGHVELL RRAAALLTYS SFCPPDDLAD RGLLGVESSF YAQDALRLWE VISRYVEGIV 490 500 510 520 530 540 SLHYKTDESV KEDFELQAWC REFTEIGLLG AQDRGFPVSL QSKEQLCHFV TMCIFTCTGQ 550 560 570 580 590 600 HSSNHLGQLD WYTWVPNAPC TMRLPPPTTK DATLETVMAT LPNFHQASLQ MSITWQLGRC 610 620 630 640 650 660 QPTMVALGQH EEEYFSGPGP KAVLTKFREE LAALDKDIEV RNAKLALPYE YLRPSRVENS VAI

References

[1]	"Cloning and sequence analysis of the cDNA for arachidonate 12-lipoxygenase of porcine leukocytes." Yoshimoto T., Suzuki H., Yamamoto S., Takai T., Yokoyama C., Tanabe T. Proc. Natl. Acad. Sci. U.S.A. 87:2142-2146(1990) [PubMed: 2315307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Leukocyte.
[2]	"Site-directed mutagenesis studies on the iron-binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase." Suzuki H., Kishimoto K., Yoshimoto T., Yamamoto S., Kanai F., Ebina Y., Miyatake A., Tanabe T. Biochim. Biophys. Acta 1210:308-316(1994) [PubMed: 8305485] [Abstract] Cited for: MUTAGENESIS.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M31417 mRNA. Translation: AAA31068.1. D10621 Genomic DNA. Translation: BAA01471.1.
PIR	A35087.
RefSeq	NP_999096.1.
UniGene	Ssc.10974
3D structure databases
HSSP	HSSP built from PDB template 1LOX based on UniProtKB P12530.
SMR	P16469. Positions 2-663.
ModBase	Search...
Genome annotation databases
GeneID	396971.
KEGG	ssc:396971.
Phylogenomic databases
HOVERGEN	P16469.
Enzyme and pathway databases
BRENDA	1.13.11.31. 249.
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...

Entry information

Entry name

LOX12_PIG

Accession

Primary (citable) accession number: P16469

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)