Reviewed, UniProtKB/Swiss-Prot P12530 (LOX15_RABIT)

Names and origin

Protein names

Recommended name:
    Arachidonate 15-lipoxygenase
      Short name=15-LOX
    EC=1.13.11.33
Alternative name(s):
    Omega-6 lipoxygenase
    Erythroid cell-specific 15-lipoxygenase

Gene names

Name:

ALOX15

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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)

Catalytic activity	Arachidonate + O(2) = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.
Cofactor	Binds 1 iron ion per subunit By similarity.
Pathway	Lipid metabolism; leukotriene D4 biosynthesis.
Subcellular location	Cytoplasm.
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	3D-structure 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-KW
Molecular function	arachidonate 15-lipoxygenase activity Inferred from electronic annotation. Source: EC 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

Chain

2 – 663

662

Arachidonate 15-lipoxygenase

PRO_0000220699

Regions

Domain

2 – 115

114

PLAT

Domain

116 – 663

548

Lipoxygenase

Sites

Metal binding

361

1

Iron; catalytic

Metal binding

366

1

Iron; catalytic

Metal binding

541

1

Iron; catalytic

Metal binding

545

1

Iron; catalytic

Metal binding

663

1

Iron; via carboxylate; catalytic

Experimental info

Sequence conflict

190

1

N → D in AAB86978. Ref.2

Sequence conflict

194

1

I → V in AAB86978. Ref.2

Secondary structure

1

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663

Helix Strand Turn

Details...

Beta strand

3 – 10

8

Beta strand

12 – 15

4

Beta strand

19 – 30

12

Beta strand

32 – 39

8

Beta strand

46 – 52

7

Beta strand

59 – 68

10

Beta strand

70 – 72

3

Beta strand

76 – 89

14

Beta strand

93 – 101

9

Beta strand

103 – 105

3

Beta strand

107 – 110

4

Helix

126 – 139

14

Beta strand

152 – 154

3

Helix

158 – 160

3

Helix

163 – 165

3

Helix

169 – 191

23

Helix

192 – 195

4

Helix

201 – 203

3

Helix

204 – 207

4

Helix

214 – 221

8

Beta strand

222 – 224

3

Helix

226 – 235

10

Helix

260 – 271

12

Beta strand

274 – 278

5

Helix

280 – 282

3

Beta strand

301 – 307

7

Turn

308 – 310

3

Beta strand

311 – 318

8

Helix

338 – 358

21

Helix

359 – 365

7

Helix

366 – 379

14

Helix

385 – 390

6

Helix

391 – 394

4

Helix

397 – 404

8

Turn

405 – 408

4

Helix

414 – 418

5

Turn

422 – 424

3

Helix

425 – 431

7

Helix

432 – 434

3

Helix

439 – 442

4

Helix

444 – 451

8

Helix

460 – 483

24

Helix

487 – 491

5

Helix

494 – 504

11

Turn

505 – 509

5

Turn

511 – 515

5

Helix

523 – 536

14

Helix

539 – 545

7

Helix

548 – 551

4

Beta strand

552 – 554

3

Helix

555 – 557

3

Beta strand

568 – 570

3

Helix

574 – 580

7

Helix

584 – 597

14

Helix

618 – 644

27

Turn

654 – 656

3

Beta strand

657 – 660

4

Sequences

	Sequence		Length	Mass (Da)
	P12530-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C3391E1E6E7930BF	FASTA	663	75,310
	10 20 30 40 50 60 MGVYRVCVST GASIYAGSKN KVELWLVGQH GEVELGSCLR PTRNKEEEFK VNVSKYLGSL 70 80 90 100 110 120 LFVRLRKKHF LKEDAWFCNW ISVQALGAAE DKYWFPCYRW VVGDGVQSLP VGTGCTTVGD 130 140 150 160 170 180 PQGLFQKHRE QELEERRKLY QWGSWKEGLI LNVAGSKLTD LPVDERFLED KKIDFEASLA 190 200 210 220 230 240 WGLAELALKN SLNILAPWKT LDDFNRIFWC GRSKLARRVR DSWQEDSLFG YQFLNGANPM 250 260 270 280 290 300 LLRRSVQLPA RLVFPPGMEE LQAQLEKELK AGTLFEADFA LLDNIKANVI LYCQQYLAAP 310 320 330 340 350 360 LVMLKLQPDG KLMPMVIQLH LPKIGSSPPP LFLPTDPPMV WLLAKCWVRS SDFQVHELNS 370 380 390 400 410 420 HLLRGHLMAE VFTVATMRCL PSIHPVFKLI VPHLRYTLEI NVRARNGLVS DFGIFDQIMS 430 440 450 460 470 480 TGGGGHVQLL QQAGAFLTYR SFCPPDDLAD RGLLGVESSF YAQDALRLWE IISRYVQGIM 490 500 510 520 530 540 GLYYKTDEAV RDDLELQSWC REITEIGLQG AQKQGFPTSL QSVAQACHFV TMCIFTCTGQ 550 560 570 580 590 600 HSSIHLGQLD WFTWVPNAPC TMRLPPPTTK DATLETVMAT LPNLHQSSLQ MSIVWQLGRD 610 620 630 640 650 660 QPIMVPLGQH QEEYFSGPEP RAVLEKFREE LAIMDKEIEV RNEKLDIPYE YLRPSIVENS VAI

References

[1]	"The promoter structure and complete sequence of the gene encoding the rabbit erythroid cell-specific 15-lipoxygenase." O'Prey J., Chester J., Thiele B.J., Janetzki S., Prehn S., Fleming J., Harrison P.R. Gene 84:493-499(1989) [PubMed: 2612916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete sequence of the rabbit erythroid cell-specific 15-lipoxygenase mRNA: comparison of the predicted amino acid sequence of the erythrocyte lipoxygenase with other lipoxygenases." Fleming J., Thiele B.J., Chester J., O'Prey J., Janetzki S., Aitken A., Anton I.A., Rapoport S.M., Harrison P.R. Gene 79:181-188(1989) [PubMed: 2777088] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-31.
[3]	"Cloning of a rabbit erythroid-cell-specific lipoxygenase mRNA." Thiele B.J., Fleming J., Kasturi K., O'Prey J., Black E., Chester J., Rapoport S.M., Harrison P.R. Gene 57:111-119(1987) [PubMed: 3123326] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-31.
[4]	"Structure of the mRNA and of the gene coding for the rabbit erythroid 15-lipoxygenase." Thiele B.J., Fleming J., Chester J., O'Prey J., Prehn S., Janetzki S., Rapoport S.M., Harrison P.R. Biomed. Biochim. Acta 49:S17-S24(1990) [PubMed: 2386503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, GENE STRUCTURE.
[5]	"The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity." Gillmor S.A., Villasenor A., Fletterick R., Sigal E., Browner M.F. Nat. Struct. Biol. 4:1003-1009(1997) [PubMed: 9406550] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M33291 Genomic DNA. Translation: AAA75014.1.
M27214 mRNA. Translation: AAB86978.1.
M22617 mRNA. Translation: AAA31385.1.

PIR

JQ0018.

RefSeq

NP_001075751.1.

UniGene

Ocu.2185

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LOX	X-ray	2.40	A	1-663	[»]
2P0M	X-ray	2.40	A/B	2-663	[»]

ModBase

Search...

Genome annotation databases

GeneID

100009114.

Phylogenomic databases

HOVERGEN

P12530.

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]