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P51399

- LOX5_MESAU

UniProt

P51399 - LOX5_MESAU

Protein

Arachidonate 5-lipoxygenase

Gene

ALOX5

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    Arachidonate + O2 = leukotriene A4 + H2O.

    Cofactori

    Binds 1 iron ion per subunit.PROSITE-ProRule annotation
    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

    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

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

    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

    Structurei

    3D structure databases

    ProteinModelPortaliP51399.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGA    50
    VDSYDVTVDE ELGEIQLVRI EKRKYWLHDD WYLKYITLKT PTDYIEFPCY 100
    RWITGEGEIV LRDGRAKLAR DDQIHILKQH RRKELEARQK QYRWMEWNPG 150
    FPLSIDAKCH KDLPRDIQFD SEKGVDFVLN YSKAMENLFI NRFMHMFQSS 200
    WNDFADFEKI FVKISNTISE RVKNHWQEDL MFGYQFLNGC NPVLIKRCRE 250
    LPQKLPVTTE MVECSLERHL SLEQEVQEGN IFIVDYELLD GIDANKTDPC 300
    THQFLAAPIC LLYKNLANKI VPIAIQLNQA PGEKNPIFLP SDAKYDWLLA 350
    KIWVRSSDFH VHQTITHLLC THLVSEVFGI AMYRQLPAVH PIFKLLVAHV 400
    RFTIAINTKA REQLICEYGL FDKANATGGG GHVQMVQRAV QDLTYSSLCF 450
    PEAIKARGMD STEDIPYYFY RDDGLLVWEA IQSFTSEVVS IYYEDDQVVM 500
    EDQELQDFVK DVYVYGMRGR KASGFPKSIK SREKLSEYLT VVIFTASAQH 550
    AAVNFGQYDW CSWIPNAPPT MRAPPATAKG VVTIEQIVAT LPDRGRSCWH 600
    LGAVWALSQF QENELFLGMY PEEHFIEKPV KEAMTRFRKN LEAIVNVIAE 650
    RNKNKKLPYY YLSPDRIPNS VAI 673
    Length:673
    Mass (Da):77,873
    Last modified:January 23, 2007 - v2
    Checksum:iA7AF63B11CDC7972
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43333 mRNA. Translation: AAA85257.1 .
    RefSeqi NP_001268516.1. NM_001281587.1.

    3D structure databases

    ProteinModelPortali P51399.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 101839970.

    Organism-specific databases

    CTDi 240.

    Phylogenomic databases

    HOVERGENi HBG005150.

    Enzyme and pathway databases

    UniPathwayi UPA00877 .

    Family and domain databases

    Gene3Di 2.60.60.20. 1 hit.
    InterProi IPR008976. Lipase_LipOase.
    IPR000907. LipOase.
    IPR013819. LipOase_C.
    IPR020834. LipOase_CS.
    IPR020833. LipOase_Fe_BS.
    IPR001885. LipOase_mml.
    IPR001024. PLAT/LH2_dom.
    [Graphical view ]
    PANTHERi PTHR11771. PTHR11771. 1 hit.
    Pfami PF00305. Lipoxygenase. 2 hits.
    PF01477. PLAT. 1 hit.
    [Graphical view ]
    PRINTSi PR00087. LIPOXYGENASE.
    PR00467. MAMLPOXGNASE.
    SMARTi SM00308. LH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48484. SSF48484. 1 hit.
    SSF49723. SSF49723. 1 hit.
    PROSITEi PS00711. LIPOXYGENASE_1. 1 hit.
    PS00081. LIPOXYGENASE_2. 1 hit.
    PS51393. LIPOXYGENASE_3. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 92 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