UniProtKB - P12527 (LOX5_RAT)
Polyunsaturated fatty acid 5-lipoxygenase
Alox5
Functioni
Catalytic activityi
- EC:1.13.11.34By similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- (18R)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + O2 = (5S)-hydroperoxy-(18R)-hydroxy-(6E,8Z,11Z,14Z,16E)-eicosapentaenoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (18S)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + O2 = (5S)-hydroperoxy-(18S)-hydroxy-(6E,8Z,11Z,14Z,16E)-eicosapentaenoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (5S)-hydroperoxy-(18S)-hydroxy-(6E,8Z,11Z,14Z,16E)-eicosapentaenoate = (5S,6S)-epoxy-(18S)-hydroxy-(7E,9E,11Z,14Z,16E)-eicosapentaenoate + H2OBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (5S)-hydroperoxy-(18R)-hydroxy-(6E,8Z,11Z,14Z,16E)-eicosapentaenoate = (5S,6S)-epoxy-(18R)-hydroxy-(7E,9E,11Z,14Z,16E)-eicosapentaenoate + H2OBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (5S)-hydroperoxy-18-hydroxy-(7E,9E,11Z,14Z,16E)-eicosapentaenoate = (5S,6S)-epoxy-18-hydroxy-(7E,9E,11Z,14Z,16E)-eicosapentaenoate + H2OBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate + O2 = (5S)-hydroperoxy-(15S)-hydroxy-(6E,8Z,11Z,13E)-eicosatetraenoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (8S)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 = 5-hydroperoxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (14S)-hydroperoxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (7S)-hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (17S)-hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
Cofactori
: leukotriene A4 biosynthesis Pathwayi
This protein is involved in the pathway leukotriene A4 biosynthesis, which is part of Lipid metabolism.By similarityView all proteins of this organism that are known to be involved in the pathway leukotriene A4 biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 17 | Calcium 1; via carbonyl oxygen; structuralBy similarity | 1 | |
Metal bindingi | 18 | Calcium 2; via carbonyl oxygen; structuralBy similarity | 1 | |
Metal bindingi | 19 | Calcium 2; structuralBy similarity | 1 | |
Metal bindingi | 44 | Calcium 2; structuralBy similarity | 1 | |
Metal bindingi | 45 | Calcium 2; via carbonyl oxygen; structuralBy similarity | 1 | |
Metal bindingi | 47 | Calcium 2; structuralBy similarity | 1 | |
Metal bindingi | 79 | Calcium 1; via carbonyl oxygen; structuralBy similarity | 1 | |
Metal bindingi | 80 | Calcium 1; via carbonyl oxygen; structuralBy similarity | 1 | |
Sitei | 103 | Essential for stabilizing binding to COTL1By similarity | 1 | |
Metal bindingi | 367 | Iron; via tele nitrogen; catalyticBy similarity | 1 | |
Metal bindingi | 372 | Iron; via tele nitrogen; catalyticPROSITE-ProRule annotationBy similarity | 1 | |
Metal bindingi | 550 | Iron; via tele nitrogen; catalyticPROSITE-ProRule annotationBy similarity | 1 | |
Metal bindingi | 554 | Iron; catalyticPROSITE-ProRule annotationBy similarity | 1 | |
Metal bindingi | 673 | Iron; via carbonyl oxygen; catalyticPROSITE-ProRule annotationBy similarity | 1 | |
Metal bindingi | 673 | Iron; via carboxylate; catalyticPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- arachidonate 5-lipoxygenase activity Source: UniProtKB
- hydrolase activity Source: UniProtKB-KW
- iron ion binding Source: UniProtKB
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: GO_Central
GO - Biological processi
- acute inflammatory response Source: RGD
- arachidonic acid metabolic process Source: GO_Central
- dendritic cell migration Source: UniProtKB
- glucose homeostasis Source: UniProtKB
- hepoxilin biosynthetic process Source: GO_Central
- humoral immune response Source: UniProtKB
- inflammatory response Source: RGD
- leukocyte chemotaxis involved in inflammatory response Source: UniProtKB
- leukocyte migration involved in inflammatory response Source: UniProtKB
- leukotriene A4 biosynthetic process Source: UniProtKB
- leukotriene biosynthetic process Source: UniProtKB
- leukotriene metabolic process Source: RGD
- leukotriene production involved in inflammatory response Source: RGD
- linoleic acid metabolic process Source: GO_Central
- lipid oxidation Source: GO_Central
- lipoxin biosynthetic process Source: UniProtKB
- lipoxygenase pathway Source: GO_Central
- negative regulation of angiogenesis Source: UniProtKB
- negative regulation of endothelial cell proliferation Source: UniProtKB
- negative regulation of inflammatory response Source: UniProtKB
- negative regulation of response to endoplasmic reticulum stress Source: UniProtKB
- negative regulation of sprouting angiogenesis Source: UniProtKB
- negative regulation of vascular wound healing Source: UniProtKB
- negative regulation of wound healing Source: UniProtKB
- positive regulation of bone mineralization Source: UniProtKB
- positive regulation of cytochrome-c oxidase activity Source: RGD
- positive regulation of leukocyte adhesion to arterial endothelial cell Source: UniProtKB
- positive regulation of vasoconstriction Source: RGD
- regulation of cellular response to oxidative stress Source: UniProtKB
- regulation of cytokine production involved in inflammatory response Source: UniProtKB
- regulation of fat cell differentiation Source: UniProtKB
- regulation of inflammatory response Source: UniProtKB
- regulation of inflammatory response to wounding Source: UniProtKB
- regulation of insulin secretion Source: UniProtKB
- regulation of reactive oxygen species biosynthetic process Source: UniProtKB
- response to hyperoxia Source: RGD
- response to nutrient Source: RGD
- sensory perception of pain Source: RGD
Keywordsi
Molecular function | Dioxygenase, Hydrolase, Oxidoreductase |
Biological process | Leukotriene biosynthesis |
Ligand | Calcium, Iron, Metal-binding |
Enzyme and pathway databases
BRENDAi | 1.13.11.34, 5301 |
Reactomei | R-RNO-2142688, Synthesis of 5-eicosatetraenoic acids R-RNO-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX) R-RNO-2142700, Synthesis of Lipoxins (LX) R-RNO-6798695, Neutrophil degranulation R-RNO-9018676, Biosynthesis of D-series resolvins R-RNO-9018682, Biosynthesis of maresins R-RNO-9018896, Biosynthesis of E-series 18(S)-resolvins R-RNO-9020265, Biosynthesis of aspirin-triggered D-series resolvins R-RNO-9023661, Biosynthesis of E-series 18(R)-resolvins R-RNO-9026286, Biosynthesis of DPAn-3-derived protectins and resolvins R-RNO-9026290, Biosynthesis of DPAn-3-derived maresins R-RNO-9026403, Biosynthesis of DPAn-3-derived 13-series resolvins R-RNO-9027604, Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives |
UniPathwayi | UPA00877 |
Names & Taxonomyi
Protein namesi | Recommended name: Polyunsaturated fatty acid 5-lipoxygenaseCurated (EC:1.13.11.-By similarity)Alternative name(s): Arachidonate 5-lipoxygenase (EC:1.13.11.34By similarity) Short name: 5-LOBy similarity Short name: 5-lipoxygenase1 Publication |
Gene namesi | Name:Alox5Imported |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 2096, Alox5 |
Subcellular locationi
Cytosol
- cytosol By similarity
Nucleus
- Nucleus matrix By similarity
- Nucleus membrane By similarity; Peripheral membrane protein By similarity
- Nucleus envelope By similarity
- Nucleus intermembrane space By similarity
Other locations
- Cytoplasm By similarity
- perinuclear region By similarity
Note: Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser-272. Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association.By similarity
Cytosol
- cytosol Source: UniProtKB
Nucleus
- nuclear envelope Source: RGD
- nuclear envelope lumen Source: UniProtKB
- nuclear matrix Source: RGD
- nuclear membrane Source: UniProtKB
- nucleus Source: RGD
Plasma Membrane
- sarcolemma Source: RGD
Other locations
- cytoplasm Source: RGD
- dendrite Source: RGD
- perinuclear region of cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, Membrane, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000220696 | 1 – 673 | Polyunsaturated fatty acid 5-lipoxygenaseAdd BLAST | 673 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 271 | PhosphoserineBy similarity | 1 | |
Modified residuei | 523 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
PhosphoproteinProteomic databases
PaxDbi | P12527 |
PRIDEi | P12527 |
PTM databases
iPTMneti | P12527 |
PhosphoSitePlusi | P12527 |
Interactioni
Subunit structurei
Homodimer.
Interacts with ALOX5AP and LTC4S.
Interacts with COTL1, the interaction is required for stability and efficient catalytic activity.
Interacts with PIK3R1; this interaction bridges ALOX5 with CD40 after CD40 ligation in B cells and leads to the production of reactive oxygen species (ROS).
Interacts (via PLAT domain) with DICER1 (via Dicer dsRNA-binding fold domain); this interaction enhances arachidonate 5-lipoxygenase activity and modifies the miRNA precursor processing activity of DICER1.
By similarityProtein-protein interaction databases
DIPi | DIP-48659N |
IntActi | P12527, 1 interactor |
STRINGi | 10116.ENSRNOP00000017633 |
Chemistry databases
BindingDBi | P12527 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2 – 117 | PLATPROSITE-ProRule annotationAdd BLAST | 116 | |
Domaini | 118 – 673 | LipoxygenasePROSITE-ProRule annotationAdd BLAST | 556 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | ENOG502QQSP, Eukaryota |
InParanoidi | P12527 |
PhylomeDBi | P12527 |
Family and domain databases
CDDi | cd01753, PLAT_LOX, 1 hit |
InterProi | View 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 IPR042062, PLAT_LOX_verte |
PANTHERi | PTHR11771, PTHR11771, 1 hit |
Pfami | View protein in Pfam PF00305, Lipoxygenase, 1 hit PF01477, PLAT, 1 hit |
PRINTSi | PR00087, LIPOXYGENASE PR00467, MAMLPOXGNASE |
SMARTi | View protein in SMART SM00308, LH2, 1 hit |
SUPFAMi | SSF48484, SSF48484, 1 hit SSF49723, SSF49723, 1 hit |
PROSITEi | View protein in PROSITE PS00711, LIPOXYGENASE_1, 1 hit PS00081, LIPOXYGENASE_2, 1 hit PS51393, LIPOXYGENASE_3, 1 hit PS50095, PLAT, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
10 20 30 40 50
MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGG
60 70 80 90 100
RDSYDVTVDE ELGEIYLVKI EKRKYRLHDD WYLKYITLKT PHDYIEFPCY
110 120 130 140 150
RWITGEGEIV LRDGCAKLAR DDQIHILKQH RRKELETRQK QYRWMEWNPG
160 170 180 190 200
FPLSIDAKCH KDLPRDIQFD SEKGVDFVLN YSKAMENLFI NRFMHMFQSS
210 220 230 240 250
WHDFADFEKI FVKISNTISE RVKNHWQEDL MFGYQFLNGC NPVLIKRCTE
260 270 280 290 300
LPKKLPVTTE MVECSLERQL SLEQEVQEGN IFIVDYELLD GIDANKTDPC
310 320 330 340 350
THQFLAAPIC LLYKNLANKI VPIAIQLNQT PGEKNPIFLP TDSKYDWLLA
360 370 380 390 400
KIWVRSSDFH IHQTITHLLR THLVSEVFGI AMYRQLPAVH PLFKLLVAHV
410 420 430 440 450
RFTIAINTKA REQLNCEYGL FDKANATGGG GHVQMVQRAV QDLTYSSLCF
460 470 480 490 500
PEAIKARGMD NTEDIPYYFY RDDGLLVWEA IQSFTTEVVS IYYEDDQVVE
510 520 530 540 550
EDQELQDFVK DVYVYGMRGR KASGFPKSIK SREKLSEYLT VVIFTASAQH
560 570 580 590 600
AAVNFGQYDW CSWIPNAPPT MRAPPPTAKG VVTIEQIVDT LPDRGRSCWH
610 620 630 640 650
LGAVWALSQF QENELFLGMY PEEHFIEKPV KEAMIRFRKN LEAIVSVIAE
660 670
RNKNKKLPYY YLSPDRIPNS VAI
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF1LMM5 | F1LMM5_RAT | Polyunsaturated fatty acid 5-lipoxy... | Alox5 | 674 | Annotation score: | ||
A0A0G2JU29 | A0A0G2JU29_RAT | Polyunsaturated fatty acid 5-lipoxy... | Alox5 | 620 | Annotation score: |
Sequence cautioni
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03960 mRNA Translation: AAA41538.1 Frameshift. |
PIRi | A30882 |
RefSeqi | NP_036954.1, NM_012822.1 |
Genome annotation databases
GeneIDi | 25290 |
KEGGi | rno:25290 |
UCSCi | RGD:2096, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03960 mRNA Translation: AAA41538.1 Frameshift. |
PIRi | A30882 |
RefSeqi | NP_036954.1, NM_012822.1 |
3D structure databases
SMRi | P12527 |
ModBasei | Search... |
Protein-protein interaction databases
DIPi | DIP-48659N |
IntActi | P12527, 1 interactor |
STRINGi | 10116.ENSRNOP00000017633 |
Chemistry databases
BindingDBi | P12527 |
ChEMBLi | CHEMBL312 |
DrugCentrali | P12527 |
PTM databases
iPTMneti | P12527 |
PhosphoSitePlusi | P12527 |
Proteomic databases
PaxDbi | P12527 |
PRIDEi | P12527 |
Genome annotation databases
GeneIDi | 25290 |
KEGGi | rno:25290 |
UCSCi | RGD:2096, rat |
Organism-specific databases
CTDi | 240 |
RGDi | 2096, Alox5 |
Phylogenomic databases
eggNOGi | ENOG502QQSP, Eukaryota |
InParanoidi | P12527 |
PhylomeDBi | P12527 |
Enzyme and pathway databases
UniPathwayi | UPA00877 |
BRENDAi | 1.13.11.34, 5301 |
Reactomei | R-RNO-2142688, Synthesis of 5-eicosatetraenoic acids R-RNO-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX) R-RNO-2142700, Synthesis of Lipoxins (LX) R-RNO-6798695, Neutrophil degranulation R-RNO-9018676, Biosynthesis of D-series resolvins R-RNO-9018682, Biosynthesis of maresins R-RNO-9018896, Biosynthesis of E-series 18(S)-resolvins R-RNO-9020265, Biosynthesis of aspirin-triggered D-series resolvins R-RNO-9023661, Biosynthesis of E-series 18(R)-resolvins R-RNO-9026286, Biosynthesis of DPAn-3-derived protectins and resolvins R-RNO-9026290, Biosynthesis of DPAn-3-derived maresins R-RNO-9026403, Biosynthesis of DPAn-3-derived 13-series resolvins R-RNO-9027604, Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives |
Miscellaneous databases
PROi | PR:P12527 |
Family and domain databases
CDDi | cd01753, PLAT_LOX, 1 hit |
InterProi | View 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 IPR042062, PLAT_LOX_verte |
PANTHERi | PTHR11771, PTHR11771, 1 hit |
Pfami | View protein in Pfam PF00305, Lipoxygenase, 1 hit PF01477, PLAT, 1 hit |
PRINTSi | PR00087, LIPOXYGENASE PR00467, MAMLPOXGNASE |
SMARTi | View protein in SMART SM00308, LH2, 1 hit |
SUPFAMi | SSF48484, SSF48484, 1 hit SSF49723, SSF49723, 1 hit |
PROSITEi | View protein in PROSITE PS00711, LIPOXYGENASE_1, 1 hit PS00081, LIPOXYGENASE_2, 1 hit PS51393, LIPOXYGENASE_3, 1 hit PS50095, PLAT, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LOX5_RAT | |
Accessioni | P12527Primary (citable) accession number: P12527 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1989 |
Last sequence update: | January 23, 2007 | |
Last modified: | December 2, 2020 | |
This is version 161 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families