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Protein

Arachidonate 5-lipoxygenase

Gene

Alox5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes.

Catalytic activityi

Arachidonate + O2 = leukotriene A4 + H2O.

Cofactori

Protein has several cofactor binding sites:
  • Fe cationPROSITE-ProRule annotationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation
  • Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity

Pathwayi: leukotriene A4 biosynthesis

This protein is involved in the pathway leukotriene A4 biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway leukotriene A4 biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi17Calcium 1; via carbonyl oxygen; structuralBy similarity1
Metal bindingi18Calcium 2; via carbonyl oxygen; structuralBy similarity1
Metal bindingi19Calcium 2; structuralBy similarity1
Metal bindingi44Calcium 2; structuralBy similarity1
Metal bindingi45Calcium 2; via carbonyl oxygen; structuralBy similarity1
Metal bindingi47Calcium 2; structuralBy similarity1
Metal bindingi79Calcium 1; via carbonyl oxygen; structuralBy similarity1
Metal bindingi80Calcium 1; via carbonyl oxygen; structuralBy similarity1
Sitei103Essential for stabilizing binding to COTL1By similarity1
Metal bindingi367Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi372Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi550Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi554Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi673Iron; via carboxylate; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

  • arachidonate 5-lipoxygenase activity Source: RGD
  • iron ion binding Source: UniProtKB

GO - Biological processi

  • acute inflammatory response Source: RGD
  • arachidonic acid metabolic process Source: RGD
  • leukotriene biosynthetic process Source: UniProtKB
  • lipoxygenase pathway Source: RGD
  • positive regulation of vasoconstriction Source: RGD
  • response to hyperoxia Source: RGD
  • response to nutrient Source: RGD
  • sensory perception of pain Source: RGD

Keywordsi

Molecular functionDioxygenase, Oxidoreductase
Biological processLeukotriene biosynthesis
LigandCalcium, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.11.34 5301
UniPathwayiUPA00877

Names & Taxonomyi

Protein namesi
Recommended name:
Arachidonate 5-lipoxygenase (EC:1.13.11.34)
Short name:
5-LO
Short name:
5-lipoxygenase
Gene namesi
Name:Alox5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2096 Alox5

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

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL312

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002206961 – 673Arachidonate 5-lipoxygenaseAdd BLAST673

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei271PhosphoserineBy similarity1
Modified residuei523PhosphoserineBy similarity1

Post-translational modificationi

Serine phosphorylation by MAPKAPK2 is stimulated by arachidonic acid. Phosphorylation on Ser-523 by PKA has an inhibitory effect. Phosphorylation on Ser-271 prevents export from the nucleus (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP12527
PRIDEiP12527

PTM databases

iPTMnetiP12527
PhosphoSitePlusiP12527

Interactioni

Subunit structurei

Interacts with ALOX5AP and LTC4S. Interacts with COTL1, the interaction is required for stability and efficient catalytic activity (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-48659N
IntActiP12527, 1 interactor
STRINGi10116.ENSRNOP00000017633

Chemistry databases

BindingDBiP12527

Structurei

3D structure databases

ProteinModelPortaliP12527
SMRiP12527
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 117PLATPROSITE-ProRule annotationAdd BLAST116
Domaini118 – 673LipoxygenasePROSITE-ProRule annotationAdd BLAST556

Sequence similaritiesi

Belongs to the lipoxygenase family.Curated

Phylogenomic databases

eggNOGiENOG410IF0U Eukaryota
ENOG410YN4N LUCA
HOGENOMiHOG000234358
HOVERGENiHBG005150
InParanoidiP12527
KOiK00461
PhylomeDBiP12527

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.

P12527-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:673
Mass (Da):78,087
Last modified:January 23, 2007 - v3
Checksum:i536B0BC27CB0A608
GO

Sequence cautioni

The sequence AAA41538 differs from that shown. Reason: Frameshift at position 667.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03960 mRNA Translation: AAA41538.1 Frameshift.
PIRiA30882
RefSeqiNP_036954.1, NM_012822.1
UniGeneiRn.9662

Genome annotation databases

GeneIDi25290
KEGGirno:25290
UCSCiRGD:2096 rat

Similar proteinsi

Entry informationi

Entry nameiLOX5_RAT
AccessioniPrimary (citable) accession number: P12527
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 148 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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