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Protein

Arachidonate 5-lipoxygenase

Gene

ALOX5

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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: UniProtKB
  2. iron ion binding Source: UniProtKB

GO - Biological processi

  1. leukotriene biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Leukotriene biosynthesis

Keywords - Ligandi

Calcium, Iron, Metal-binding

Enzyme and pathway databases

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
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

  1. Cytoplasm PROSITE-ProRule annotation
  2. Nucleus matrix By similarity
  3. Nucleus membrane By similarity; Peripheral membrane protein By similarity

  4. 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 (By similarity).By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. nuclear envelope lumen Source: UniProtKB
  3. nuclear matrix Source: UniProtKB-SubCell
  4. nuclear membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 673673Arachidonate 5-lipoxygenasePRO_0000220694Add
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

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

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

HOVERGENiHBG005150.

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. 2 hits.
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.

P51399-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGA
60 70 80 90 100
VDSYDVTVDE ELGEIQLVRI EKRKYWLHDD WYLKYITLKT PTDYIEFPCY
110 120 130 140 150
RWITGEGEIV LRDGRAKLAR DDQIHILKQH RRKELEARQK QYRWMEWNPG
160 170 180 190 200
FPLSIDAKCH KDLPRDIQFD SEKGVDFVLN YSKAMENLFI NRFMHMFQSS
210 220 230 240 250
WNDFADFEKI FVKISNTISE RVKNHWQEDL MFGYQFLNGC NPVLIKRCRE
260 270 280 290 300
LPQKLPVTTE MVECSLERHL SLEQEVQEGN IFIVDYELLD GIDANKTDPC
310 320 330 340 350
THQFLAAPIC LLYKNLANKI VPIAIQLNQA PGEKNPIFLP SDAKYDWLLA
360 370 380 390 400
KIWVRSSDFH VHQTITHLLC THLVSEVFGI AMYRQLPAVH PIFKLLVAHV
410 420 430 440 450
RFTIAINTKA REQLICEYGL FDKANATGGG GHVQMVQRAV QDLTYSSLCF
460 470 480 490 500
PEAIKARGMD STEDIPYYFY RDDGLLVWEA IQSFTSEVVS IYYEDDQVVM
510 520 530 540 550
EDQELQDFVK DVYVYGMRGR KASGFPKSIK SREKLSEYLT VVIFTASAQH
560 570 580 590 600
AAVNFGQYDW CSWIPNAPPT MRAPPATAKG VVTIEQIVAT LPDRGRSCWH
610 620 630 640 650
LGAVWALSQF QENELFLGMY PEEHFIEKPV KEAMTRFRKN LEAIVNVIAE
660 670
RNKNKKLPYY YLSPDRIPNS VAI
Length:673
Mass (Da):77,873
Last modified:January 23, 2007 - v2
Checksum:iA7AF63B11CDC7972
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43333 mRNA. Translation: AAA85257.1.
RefSeqiNP_001268516.1. NM_001281587.1.

Genome annotation databases

GeneIDi101839970.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43333 mRNA. Translation: AAA85257.1.
RefSeqiNP_001268516.1. NM_001281587.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101839970.

Organism-specific databases

CTDi240.

Phylogenomic databases

HOVERGENiHBG005150.

Enzyme and pathway databases

UniPathwayiUPA00877.

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. 2 hits.
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. "Cloning, sequencing and expression of a 5-lipoxygenase from Syrian hamster embryo fibroblasts."
    Kitzler J.W., Eling T.E.
    Prostaglandins Leukot. Essent. Fatty Acids 55:269-277(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Syrian.

Entry informationi

Entry nameiLOX5_MESAU
AccessioniPrimary (citable) accession number: P51399
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.