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Protein

Arachidonate 5-lipoxygenase

Gene

Alox5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi17 – 171Calcium 1; via carbonyl oxygen; structuralBy similarity
Metal bindingi18 – 181Calcium 2; via carbonyl oxygen; structuralBy similarity
Metal bindingi19 – 191Calcium 2; structuralBy similarity
Metal bindingi44 – 441Calcium 2; structuralBy similarity
Metal bindingi45 – 451Calcium 2; via carbonyl oxygen; structuralBy similarity
Metal bindingi47 – 471Calcium 2; structuralBy similarity
Metal bindingi79 – 791Calcium 1; via carbonyl oxygen; structuralBy similarity
Metal bindingi80 – 801Calcium 1; via carbonyl oxygen; structuralBy similarity
Sitei103 – 1031Essential for stabilizing binding to COTL1By similarity
Metal bindingi367 – 3671Iron; catalyticPROSITE-ProRule annotation
Metal bindingi372 – 3721Iron; catalyticPROSITE-ProRule annotation
Metal bindingi550 – 5501Iron; catalyticPROSITE-ProRule annotation
Metal bindingi554 – 5541Iron; catalyticPROSITE-ProRule annotation
Metal bindingi673 – 6731Iron; via carboxylate; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. arachidonate 5-lipoxygenase activity Source: RGD
  2. iron ion binding Source: UniProtKB

GO - Biological processi

  1. acute inflammatory response Source: RGD
  2. arachidonic acid metabolic process Source: RGD
  3. leukotriene biosynthetic process Source: UniProtKB
  4. lipoxygenase pathway Source: RGD
  5. positive regulation of vasoconstriction Source: RGD
  6. response to hyperoxia Source: RGD
  7. response to nutrient Source: RGD
  8. sensory perception of pain Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Leukotriene biosynthesis

Keywords - Ligandi

Calcium, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2096. Alox5.

Subcellular locationi

Cytoplasm. Nucleus matrix. Nucleus membrane; Peripheral membrane protein
Note: Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser-271. Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. dendrite Source: RGD
  3. nuclear envelope Source: RGD
  4. nuclear envelope lumen Source: UniProtKB
  5. nuclear matrix Source: UniProtKB-SubCell
  6. nuclear membrane Source: UniProtKB
  7. nucleus Source: RGD
  8. sarcolemma Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 673673Arachidonate 5-lipoxygenasePRO_0000220696Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei271 – 2711PhosphoserineBy similarity
Modified residuei523 – 5231PhosphoserineBy similarity

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

PRIDEiP12527.

PTM databases

PhosphoSiteiP12527.

Expressioni

Gene expression databases

GenevestigatoriP12527.

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.
STRINGi10116.ENSRNOP00000017633.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 117116PLATPROSITE-ProRule annotationAdd
BLAST
Domaini118 – 673556LipoxygenasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the lipoxygenase family.Curated
Contains 1 lipoxygenase domain.PROSITE-ProRule annotation
Contains 1 PLAT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG69653.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiP12527.
KOiK00461.
PhylomeDBiP12527.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

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 22, 2007 - v3
Checksum:i536B0BC27CB0A608
GO

Sequence cautioni

The sequence AAA41538.1 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.

Cross-referencesi

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.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48659N.
STRINGi10116.ENSRNOP00000017633.

Chemistry

BindingDBiP12527.
ChEMBLiCHEMBL312.

PTM databases

PhosphoSiteiP12527.

Proteomic databases

PRIDEiP12527.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25290.
KEGGirno:25290.
UCSCiRGD:2096. rat.

Organism-specific databases

CTDi240.
RGDi2096. Alox5.

Phylogenomic databases

eggNOGiNOG69653.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiP12527.
KOiK00461.
PhylomeDBiP12527.

Enzyme and pathway databases

UniPathwayiUPA00877.
BRENDAi1.13.11.34. 5301.

Miscellaneous databases

NextBioi606033.
PROiP12527.

Gene expression databases

GenevestigatoriP12527.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation and characterization of a cDNA clone encoding rat 5-lipoxygenase."
    Balcarek J.M., Theisen T.W., Cook M.N., Varrichio A., Hwang S.-M., Strohsacker M.W., Crooke S.T.
    J. Biol. Chem. 263:13937-13941(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1."
    Minor W., Steczko J., Bolin J.T., Otwinowski Z., Axelrod B.
    Biochemistry 32:6320-6323(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 667-670.

Entry informationi

Entry nameiLOX5_RAT
AccessioniPrimary (citable) accession number: P12527
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1989
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 133 of the entry and version 3 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.