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P12527

- LOX5_RAT

UniProt

P12527 - LOX5_RAT

Protein

Arachidonate 5-lipoxygenase

Gene

Alox5

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (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: RGD
    2. iron ion binding Source: UniProtKB
    3. protein binding Source: RGD

    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

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: 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

    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.

    Structurei

    3D structure databases

    ProteinModelPortaliP12527.
    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

    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

    MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGG    50
    RDSYDVTVDE ELGEIYLVKI EKRKYRLHDD WYLKYITLKT PHDYIEFPCY 100
    RWITGEGEIV LRDGCAKLAR DDQIHILKQH RRKELETRQK QYRWMEWNPG 150
    FPLSIDAKCH KDLPRDIQFD SEKGVDFVLN YSKAMENLFI NRFMHMFQSS 200
    WHDFADFEKI FVKISNTISE RVKNHWQEDL MFGYQFLNGC NPVLIKRCTE 250
    LPKKLPVTTE MVECSLERQL SLEQEVQEGN IFIVDYELLD GIDANKTDPC 300
    THQFLAAPIC LLYKNLANKI VPIAIQLNQT PGEKNPIFLP TDSKYDWLLA 350
    KIWVRSSDFH IHQTITHLLR THLVSEVFGI AMYRQLPAVH PLFKLLVAHV 400
    RFTIAINTKA REQLNCEYGL FDKANATGGG GHVQMVQRAV QDLTYSSLCF 450
    PEAIKARGMD NTEDIPYYFY RDDGLLVWEA IQSFTTEVVS IYYEDDQVVE 500
    EDQELQDFVK DVYVYGMRGR KASGFPKSIK SREKLSEYLT VVIFTASAQH 550
    AAVNFGQYDW CSWIPNAPPT MRAPPPTAKG VVTIEQIVDT LPDRGRSCWH 600
    LGAVWALSQF QENELFLGMY PEEHFIEKPV KEAMIRFRKN LEAIVSVIAE 650
    RNKNKKLPYY YLSPDRIPNS VAI 673
    Length:673
    Mass (Da):78,087
    Last modified:January 23, 2007 - v3
    Checksum:i536B0BC27CB0A608
    GO

    Sequence cautioni

    The sequence AAA41538.1 differs from that shown. Reason: Frameshift at position 667.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03960 mRNA. Translation: AAA41538.1 . Frameshift.
    PIRi A30882.
    RefSeqi NP_036954.1. NM_012822.1.
    UniGenei Rn.9662.

    3D structure databases

    ProteinModelPortali P12527.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48659N.
    STRINGi 10116.ENSRNOP00000017633.

    Chemistry

    BindingDBi P12527.
    ChEMBLi CHEMBL312.

    PTM databases

    PhosphoSitei P12527.

    Proteomic databases

    PRIDEi P12527.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25290.
    KEGGi rno:25290.
    UCSCi RGD:2096. rat.

    Organism-specific databases

    CTDi 240.
    RGDi 2096. Alox5.

    Phylogenomic databases

    eggNOGi NOG69653.
    HOGENOMi HOG000234358.
    HOVERGENi HBG005150.
    InParanoidi P12527.
    KOi K00461.
    PhylomeDBi P12527.

    Enzyme and pathway databases

    UniPathwayi UPA00877 .

    Miscellaneous databases

    NextBioi 606033.
    PROi P12527.

    Gene expression databases

    Genevestigatori P12527.

    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. 1 hit.
    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. "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(1988) [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(1993) [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: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 128 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