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P48999

- LOX5_MOUSE

UniProt

P48999 - LOX5_MOUSE

Protein

Arachidonate 5-lipoxygenase

Gene

Alox5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes.1 Publication

    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 bindingi368 – 3681Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi373 – 3731Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi551 – 5511Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi555 – 5551Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi674 – 6741Iron; via carboxylate; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. arachidonate 5-lipoxygenase activity Source: UniProtKB-EC
    2. iron ion binding Source: UniProtKB
    3. protein binding Source: MGI

    GO - Biological processi

    1. inflammatory response Source: MGI
    2. leukotriene biosynthetic process Source: MGI
    3. leukotriene metabolic process Source: MGI
    4. leukotriene production involved in inflammatory response Source: MGI

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Leukotriene biosynthesis

    Keywords - Ligandi

    Calcium, Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196544. Synthesis of Lipoxins (LX).
    REACT_206751. Synthesis of 5-eicosatetraenoic acids.
    REACT_215561. Synthesis of Leukotrienes (LT) and Eoxins (EX).
    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:87999. Alox5.

    Subcellular locationi

    Cytoplasm 1 PublicationPROSITE-ProRule annotation. Nucleus matrix 1 Publication. Nucleus membrane By similarity; Peripheral membrane protein By similarity
    Note: Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser-272. 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. cytoplasm Source: MGI
    2. cytosol Source: UniProtKB
    3. nuclear envelope lumen Source: UniProtKB
    4. nuclear matrix Source: UniProtKB-SubCell
    5. nuclear membrane Source: UniProtKB
    6. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi672 – 6721V → M: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 674674Arachidonate 5-lipoxygenasePRO_0000220695Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei272 – 2721PhosphoserineBy similarity
    Modified residuei524 – 5241PhosphoserineBy similarity

    Post-translational modificationi

    Serine phosphorylation by MAPKAPK2 is stimulated by arachidonic acid. Phosphorylation on Ser-524 by PKA has an inhibitory effect. Phosphorylation on Ser-272 prevents export from the nucleus By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP48999.
    PaxDbiP48999.
    PRIDEiP48999.

    PTM databases

    PhosphoSiteiP48999.

    Expressioni

    Gene expression databases

    BgeeiP48999.
    CleanExiMM_ALOX5.
    GenevestigatoriP48999.

    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

    BioGridi198076. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP48999.
    SMRiP48999. Positions 2-674.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 118117PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini119 – 674556LipoxygenasePROSITE-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.
    GeneTreeiENSGT00550000074415.
    HOGENOMiHOG000234358.
    HOVERGENiHBG005150.
    InParanoidiQ3TB75.
    KOiK00461.
    OMAiNYSKAME.
    OrthoDBiEOG7B05CG.
    TreeFamiTF105320.

    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.

    P48999-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGA    50
    VDSYDVTVDE ELGEIYLVKI EKRKYWLHDD WYLKYITLKT PHGDYIEFPC 100
    YRWITGEGEI VLRDGRAKLA RDDQIHILKQ HRRKELEARQ KQYRWMEWNP 150
    GFPLSIDAKC HKDLPRDIQF DSEKGVDFVL NYSKAMENLF INRFMHMFQS 200
    SWHDFADFEK IFVKISNTIS ERVKNHWQED LMFGYQFLNG CNPVLIKRCT 250
    ALPPKLPVTT EMVECSLERQ LSLEQEVQEG NIFIVDYELL DGIDANKTDP 300
    CTHQFLAAPI CLLYKNLANK IVPIAIQLNQ TPGESNPIFL PTDSKYDWLL 350
    AKIWVRSSDF HVHQTITHLL RTHLVSEVFG IAMYRQLPAV HPLFKLLVAH 400
    VRFTIAINTK AREQLICEYG LFDKANATGG GGHVQMVQRA VQDLTYSSLC 450
    FPEAIKARGM DSTEDIPFYF YRDDGLLVWE AIQSFTMEVV SIYYENDQVV 500
    EEDQELQDFV KDVYVYGMRG KKASGFPKSI KSREKLSEYL TVVIFTASAQ 550
    HAAVNFGQYD WCSWIPNAPP TMRAPPPTAK GVVTIEQIVD TLPDRGRSCW 600
    HLGAVWALSQ FQENELFLGM YPEEHFIEKP VKEAMIRFRK NLEAIVSVIA 650
    ERNKNKKLPY YYLSPDRIPN SVAI 674
    Length:674
    Mass (Da):77,967
    Last modified:July 27, 2011 - v3
    Checksum:i130F27F9A77A3D88
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti466 – 4661I → M in AAC37673. (PubMed:7629107)Curated
    Sequence conflicti646 – 6461V → I in AAC37673. (PubMed:7629107)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42198 mRNA. Translation: AAC37673.1.
    AK137481 mRNA. Translation: BAE23373.1.
    AK171413 mRNA. Translation: BAE42439.1.
    BC139102 mRNA. Translation: AAI39103.1.
    BC141213 mRNA. Translation: AAI41214.1.
    CCDSiCCDS20452.1.
    PIRiI49479.
    RefSeqiNP_033792.1. NM_009662.2.
    UniGeneiMm.41072.

    Genome annotation databases

    EnsembliENSMUST00000026795; ENSMUSP00000026795; ENSMUSG00000025701.
    GeneIDi11689.
    KEGGimmu:11689.
    UCSCiuc009dkd.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42198 mRNA. Translation: AAC37673.1 .
    AK137481 mRNA. Translation: BAE23373.1 .
    AK171413 mRNA. Translation: BAE42439.1 .
    BC139102 mRNA. Translation: AAI39103.1 .
    BC141213 mRNA. Translation: AAI41214.1 .
    CCDSi CCDS20452.1.
    PIRi I49479.
    RefSeqi NP_033792.1. NM_009662.2.
    UniGenei Mm.41072.

    3D structure databases

    ProteinModelPortali P48999.
    SMRi P48999. Positions 2-674.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198076. 1 interaction.

    Chemistry

    BindingDBi P48999.
    ChEMBLi CHEMBL5211.

    PTM databases

    PhosphoSitei P48999.

    Proteomic databases

    MaxQBi P48999.
    PaxDbi P48999.
    PRIDEi P48999.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026795 ; ENSMUSP00000026795 ; ENSMUSG00000025701 .
    GeneIDi 11689.
    KEGGi mmu:11689.
    UCSCi uc009dkd.1. mouse.

    Organism-specific databases

    CTDi 240.
    MGIi MGI:87999. Alox5.

    Phylogenomic databases

    eggNOGi NOG69653.
    GeneTreei ENSGT00550000074415.
    HOGENOMi HOG000234358.
    HOVERGENi HBG005150.
    InParanoidi Q3TB75.
    KOi K00461.
    OMAi NYSKAME.
    OrthoDBi EOG7B05CG.
    TreeFami TF105320.

    Enzyme and pathway databases

    UniPathwayi UPA00877 .
    Reactomei REACT_196544. Synthesis of Lipoxins (LX).
    REACT_206751. Synthesis of 5-eicosatetraenoic acids.
    REACT_215561. Synthesis of Leukotrienes (LT) and Eoxins (EX).

    Miscellaneous databases

    NextBioi 279339.
    PROi P48999.
    SOURCEi Search...

    Gene expression databases

    Bgeei P48999.
    CleanExi MM_ALOX5.
    Genevestigatori P48999.

    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. "cDNA cloning, expression, mutagenesis, intracellular localization, and gene chromosomal assignment of mouse 5-lipoxygenase."
      Chen X.-S., Naumann T.A., Kurre U., Jenkins N.A., Copeland N.G., Funk C.D.
      J. Biol. Chem. 270:17993-17999(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-672.
      Strain: C57BL/6 X 129/Sv.
      Tissue: Peritoneal cavity.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.

    Entry informationi

    Entry nameiLOX5_MOUSE
    AccessioniPrimary (citable) accession number: P48999
    Secondary accession number(s): Q3TB75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 122 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, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3