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Protein

Arachidonate 15-lipoxygenase

Gene

ALOX15

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. In addition to its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass.2 Publications

Caution

According to the authors the mRNA described in PubMed:9600854 may be encoded by a gene different from ALOX15.Curated

Catalytic activityi

Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.1 Publication
Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.2 Publications

Cofactori

Fe cationNote: Binds 1 Fe cation per subunit.

Pathwayi: hydroperoxy eicosatetraenoic acid biosynthesis

This protein is involved in the pathway hydroperoxy eicosatetraenoic acid biosynthesis, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway hydroperoxy eicosatetraenoic acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi361Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi366Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi541Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi545Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi663Iron; via carboxylate; catalyticPROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDioxygenase, Oxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandCalcium, Iron, Lipid-binding, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.11.33 1749
UniPathwayiUPA00881

Chemistry databases

SwissLipidsiSLP:000001603

Names & Taxonomyi

Protein namesi
Recommended name:
Arachidonate 15-lipoxygenase (EC:1.13.11.332 Publications)
Short name:
15-LOX
Alternative name(s):
12/15-lipoxygenase
Arachidonate 12-lipoxygenase, leukocyte-type (EC:1.13.11.311 Publication)
Short name:
12-LOX
Short name:
L-12LO
Arachidonate omega-6 lipoxygenase
Erythroid cell-specific 15-lipoxygenase
Gene namesi
Name:ALOX15
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Lipid droplet, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi353F → L: Changes the stereoselectivity of the oxygenation reaction to produce (12S)-HPETE instead of (15S)-HPETE. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4358

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002206992 – 663Arachidonate 15-lipoxygenaseAdd BLAST662

Expressioni

Tissue specificityi

Detected in reticulocytes (at protein level).1 Publication

Interactioni

Subunit structurei

Interacts with PEBP1; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade.By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000017072

Chemistry databases

BindingDBiP12530

Structurei

Secondary structure

1663
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 10Combined sources8
Beta strandi12 – 15Combined sources4
Beta strandi19 – 30Combined sources12
Beta strandi32 – 39Combined sources8
Beta strandi46 – 52Combined sources7
Beta strandi59 – 68Combined sources10
Beta strandi70 – 72Combined sources3
Beta strandi76 – 88Combined sources13
Beta strandi93 – 101Combined sources9
Beta strandi103 – 105Combined sources3
Beta strandi107 – 110Combined sources4
Helixi126 – 139Combined sources14
Beta strandi152 – 154Combined sources3
Helixi158 – 160Combined sources3
Helixi163 – 165Combined sources3
Helixi169 – 175Combined sources7
Helixi189 – 192Combined sources4
Helixi193 – 195Combined sources3
Helixi201 – 206Combined sources6
Helixi214 – 222Combined sources9
Helixi226 – 235Combined sources10
Helixi259 – 270Combined sources12
Beta strandi274 – 278Combined sources5
Helixi280 – 282Combined sources3
Beta strandi301 – 306Combined sources6
Turni308 – 310Combined sources3
Beta strandi312 – 318Combined sources7
Helixi338 – 358Combined sources21
Helixi359 – 365Combined sources7
Helixi366 – 379Combined sources14
Helixi385 – 390Combined sources6
Helixi391 – 394Combined sources4
Helixi397 – 404Combined sources8
Turni405 – 408Combined sources4
Helixi414 – 418Combined sources5
Turni420 – 424Combined sources5
Helixi425 – 434Combined sources10
Helixi439 – 442Combined sources4
Helixi444 – 450Combined sources7
Helixi460 – 480Combined sources21
Turni481 – 483Combined sources3
Helixi487 – 491Combined sources5
Helixi494 – 504Combined sources11
Turni505 – 509Combined sources5
Helixi511 – 514Combined sources4
Helixi523 – 536Combined sources14
Helixi539 – 545Combined sources7
Helixi548 – 551Combined sources4
Beta strandi552 – 554Combined sources3
Helixi555 – 557Combined sources3
Beta strandi568 – 570Combined sources3
Helixi574 – 580Combined sources7
Helixi584 – 596Combined sources13
Helixi618 – 643Combined sources26
Beta strandi645 – 647Combined sources3
Turni654 – 656Combined sources3
Beta strandi657 – 660Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LOXX-ray2.40A2-663[»]
2P0MX-ray2.40A/B2-663[»]
ProteinModelPortaliP12530
SMRiP12530
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12530

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 115PLATPROSITE-ProRule annotationAdd BLAST114
Domaini116 – 663LipoxygenasePROSITE-ProRule annotationAdd BLAST548

Domaini

The PLAT domain can bind calcium ions; this promotes association with membranes.By similarity

Sequence similaritiesi

Belongs to the lipoxygenase family.Curated

Phylogenomic databases

eggNOGiENOG410IKAN Eukaryota
ENOG410YN4N LUCA
HOGENOMiHOG000234358
HOVERGENiHBG005150
InParanoidiP12530
KOiK00460

Family and domain databases

InterProiView protein in InterPro
IPR000907 LipOase
IPR013819 LipOase_C
IPR036226 LipOase_C_sf
IPR020834 LipOase_CS
IPR020833 LipOase_Fe_BS
IPR001885 LipOase_mml
IPR001024 PLAT/LH2_dom
IPR036392 PLAT/LH2_dom_sf
PANTHERiPTHR11771 PTHR11771, 1 hit
PfamiView protein in Pfam
PF00305 Lipoxygenase, 1 hit
PF01477 PLAT, 1 hit
PRINTSiPR00087 LIPOXYGENASE
PR00467 MAMLPOXGNASE
SMARTiView protein in SMART
SM00308 LH2, 1 hit
SUPFAMiSSF48484 SSF48484, 1 hit
SSF49723 SSF49723, 1 hit
PROSITEiView protein in PROSITE
PS00711 LIPOXYGENASE_1, 1 hit
PS00081 LIPOXYGENASE_2, 1 hit
PS51393 LIPOXYGENASE_3, 1 hit
PS50095 PLAT, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12530-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVYRVCVST GASIYAGSKN KVELWLVGQH GEVELGSCLR PTRNKEEEFK
60 70 80 90 100
VNVSKYLGSL LFVRLRKKHF LKEDAWFCNW ISVQALGAAE DKYWFPCYRW
110 120 130 140 150
VVGDGVQSLP VGTGCTTVGD PQGLFQKHRE QELEERRKLY QWGSWKEGLI
160 170 180 190 200
LNVAGSKLTD LPVDERFLED KKIDFEASLA WGLAELALKN SLNILAPWKT
210 220 230 240 250
LDDFNRIFWC GRSKLARRVR DSWQEDSLFG YQFLNGANPM LLRRSVQLPA
260 270 280 290 300
RLVFPPGMEE LQAQLEKELK AGTLFEADFA LLDNIKANVI LYCQQYLAAP
310 320 330 340 350
LVMLKLQPDG KLMPMVIQLH LPKIGSSPPP LFLPTDPPMV WLLAKCWVRS
360 370 380 390 400
SDFQVHELNS HLLRGHLMAE VFTVATMRCL PSIHPVFKLI VPHLRYTLEI
410 420 430 440 450
NVRARNGLVS DFGIFDQIMS TGGGGHVQLL QQAGAFLTYR SFCPPDDLAD
460 470 480 490 500
RGLLGVESSF YAQDALRLWE IISRYVQGIM GLYYKTDEAV RDDLELQSWC
510 520 530 540 550
REITEIGLQG AQKQGFPTSL QSVAQACHFV TMCIFTCTGQ HSSIHLGQLD
560 570 580 590 600
WFTWVPNAPC TMRLPPPTTK DATLETVMAT LPNLHQSSLQ MSIVWQLGRD
610 620 630 640 650
QPIMVPLGQH QEEYFSGPEP RAVLEKFREE LAIMDKEIEV RNEKLDIPYE
660
YLRPSIVENS VAI
Length:663
Mass (Da):75,310
Last modified:January 23, 2007 - v3
Checksum:iC3391E1E6E7930BF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti42T → S in CAB10746 (PubMed:9600854).Curated1
Sequence conflicti64R → K in CAB10746 (PubMed:9600854).Curated1
Sequence conflicti190N → D in AAB86978 (PubMed:2777088).Curated1
Sequence conflicti194I → V in AAB86978 (PubMed:2777088).Curated1
Sequence conflicti353F → L in CAB10746 (PubMed:9600854).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33291 Genomic DNA Translation: AAA75014.1
Z97654 mRNA Translation: CAB10746.1
M27214 mRNA Translation: AAB86978.1
M22617 mRNA Translation: AAA31385.1
PIRiJQ0018
RefSeqiNP_001075751.1, NM_001082282.1
NP_001139620.1, NM_001146148.1
UniGeneiOcu.2185
Ocu.7470

Genome annotation databases

GeneIDi100009114
100271999
KEGGiocu:100009114
ocu:100271999

Similar proteinsi

Entry informationi

Entry nameiLOX15_RABIT
AccessioniPrimary (citable) accession number: P12530
Secondary accession number(s): O19043
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 142 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health