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Q2KMM4

- LX12B_RAT

UniProt

Q2KMM4 - LX12B_RAT

Protein

Arachidonate 12-lipoxygenase, 12R-type

Gene

Alox12b

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Mainly converts arachidonic acid to (12R)-hydroperoxyeicosatetraenoic acid/(12R)-HPETE and minor stereoisomers. In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. May also play a role in the regulation of the expression of airway mucins.1 Publication

    Catalytic activityi

    Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12R)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.1 Publication

    Cofactori

    Binds 1 iron ion per subunit.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi398 – 3981Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi403 – 4031Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi578 – 5781Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi582 – 5821Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi701 – 7011Iron; via carboxylate; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. arachidonate 12-lipoxygenase activity Source: UniProtKB
    2. iron ion binding Source: InterPro
    3. linoleate 9S-lipoxygenase activity Source: UniProtKB

    GO - Biological processi

    1. arachidonic acid metabolic process Source: UniProtKB
    2. ceramide biosynthetic process Source: UniProtKB
    3. establishment of skin barrier Source: UniProtKB
    4. hepoxilin biosynthetic process Source: UniProtKB
    5. linoleic acid metabolic process Source: UniProtKB
    6. lipoxygenase pathway Source: UniProtKB
    7. oxidation-reduction process Source: UniProtKB
    8. positive regulation of gene expression Source: UniProtKB
    9. positive regulation of MAPK cascade Source: UniProtKB
    10. positive regulation of mucus secretion Source: UniProtKB
    11. protein lipidation Source: UniProtKB
    12. sphingolipid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00222.
    UPA00881.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arachidonate 12-lipoxygenase, 12R-type (EC:1.13.11.-)
    Short name:
    12R-LOX
    Short name:
    12R-lipoxygenase
    Alternative name(s):
    Epidermis-type lipoxygenase 12
    Gene namesi
    Name:Alox12bImported
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 10

    Organism-specific databases

    RGDi1305330. Alox12b.

    Subcellular locationi

    Cytoplasm PROSITE-ProRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 701701Arachidonate 12-lipoxygenase, 12R-typePRO_0000244486Add
    BLAST

    Proteomic databases

    PRIDEiQ2KMM4.

    Expressioni

    Gene expression databases

    GenevestigatoriQ2KMM4.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000033009.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2KMM4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 119118PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini120 – 701582LipoxygenasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG69653.
    GeneTreeiENSGT00550000074415.
    HOGENOMiHOG000234358.
    HOVERGENiHBG005150.
    InParanoidiQ2KMM4.
    KOiK08021.
    OrthoDBiEOG7V49XR.
    PhylomeDBiQ2KMM4.

    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.

    Q2KMM4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATYKVKVAT GTDFFSGTLD SISLTIVGTQ GESHKQRLNH FGRDFATGAV    50
    DDYTVQCQQD LGELIIIRLH KEPHSFLPKD PWYCNYVQIC APNCRVYHFP 100
    AYQWMDGYET LSLREATGKT TADDTLPILL EHRQEEIRAK KDFYHWRVFV 150
    PGLPNYVDIP SYHPPPRRCR NPNRPEWNGY IPGFPILINI KATRFLNLNL 200
    RFSFVKTASF FYRLGPMALA FKLRGLVDRK RSWKRLKDIK NIFPATKTVV 250
    SEYVAEHWTE DSFFGYQYLN GINPGHIRRC MQIPDKFPVT DEMVAPFLGE 300
    GTCLQAELEK GNIYLADYRI LDGIPTVELN GQKQHHCAPI CLLHFGPDGN 350
    MMPIAIQLSQ TPGPDCPIFL PNDSEWDWLL AKTWVRYAEF YSHEAVAHLL 400
    ESHLIGEAFC LALLRNLPMC HPLYKLLIPH TRYNVQINSI GRALLLNKGG 450
    LSARAMSLGL EGFAQVMVRG LSELTYKSLC IPNDFVERGV QDLPGYYFRD 500
    DSLAVWYAME RYVTEIITYY YPNDAAVEGD PELQCWVQEI FKECLLERES 550
    SGFPTCLRTV PELIEYVTMV MYTCSARHAA VNTGQLEYTS WMPNFPSSMR 600
    NPPMQSKGLT TLQTFMDTLP DVKTTCIVLL VLWTLCREPD DRRPLGHFPD 650
    IHFVEEAPRR SMEAFRQNLN QISHNIRQRN KCLNLPYYYL DPVLIENSIS 700
    I 701
    Length:701
    Mass (Da):80,741
    Last modified:March 7, 2006 - v1
    Checksum:i6BE209D98DEB4DB9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti276 – 2761H → L in AAX85362. (PubMed:15222128)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY903231 mRNA. Translation: AAX85361.1.
    AY903232 mRNA. Translation: AAX85362.1.
    AY903233 mRNA. Translation: AAX85363.1.
    RefSeqiNP_001034466.1. NM_001039377.1.
    UniGeneiRn.160588.

    Genome annotation databases

    EnsembliENSRNOT00000039535; ENSRNOP00000033009; ENSRNOG00000022210.
    GeneIDi287425.
    KEGGirno:287425.
    UCSCiRGD:1305330. rat.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    about water - Issue 153 of September 2013

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY903231 mRNA. Translation: AAX85361.1 .
    AY903232 mRNA. Translation: AAX85362.1 .
    AY903233 mRNA. Translation: AAX85363.1 .
    RefSeqi NP_001034466.1. NM_001039377.1.
    UniGenei Rn.160588.

    3D structure databases

    ProteinModelPortali Q2KMM4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000033009.

    Proteomic databases

    PRIDEi Q2KMM4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000039535 ; ENSRNOP00000033009 ; ENSRNOG00000022210 .
    GeneIDi 287425.
    KEGGi rno:287425.
    UCSCi RGD:1305330. rat.

    Organism-specific databases

    CTDi 242.
    RGDi 1305330. Alox12b.

    Phylogenomic databases

    eggNOGi NOG69653.
    GeneTreei ENSGT00550000074415.
    HOGENOMi HOG000234358.
    HOVERGENi HBG005150.
    InParanoidi Q2KMM4.
    KOi K08021.
    OrthoDBi EOG7V49XR.
    PhylomeDBi Q2KMM4.

    Enzyme and pathway databases

    UniPathwayi UPA00222 .
    UPA00881 .

    Miscellaneous databases

    NextBioi 626105.
    PROi Q2KMM4.

    Gene expression databases

    Genevestigatori Q2KMM4.

    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. "Molecular analysis of the sex hormone-binding globulin gene in the rat hypodactylous mutation (Hd)."
      Liska F., Goesele C., Kren V., Huebner N., Krenova D.
      Folia Biol. (Praha) 50:63-68(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Brown Norway/Cub, SHR/OlaIpcvImported and Wistar Hd.
      Tissue: TestisImported.
    2. "Systematic analysis of rat 12/15-lipoxygenase enzymes reveals critical role for spinal eLOX3 hepoxilin synthase activity in inflammatory hyperalgesia."
      Gregus A.M., Dumlao D.S., Wei S.C., Norris P.C., Catella L.C., Meyerstein F.G., Buczynski M.W., Steinauer J.J., Fitzsimmons B.L., Yaksh T.L., Dennis E.A.
      FASEB J. 27:1939-1949(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiLX12B_RAT
    AccessioniPrimary (citable) accession number: Q2KMM4
    Secondary accession number(s): Q2KMM5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 56 of the entry and version 1 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3