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Q9BYJ1

- LOXE3_HUMAN

UniProt

Q9BYJ1 - LOXE3_HUMAN

Protein

Hydroperoxide isomerase ALOXE3

Gene

ALOXE3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced dioxygenase activity compared to other lipoxygenases. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols. The dioxygenase activity requires a step of activation of the enzyme by molecular oxygen. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate 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. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites. Plays also a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG. Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia.5 Publications

    Catalytic activityi

    A hydroperoxy icosatetraenoate = a hydroxy epoxy icosatrienoate.
    A hydroperoxy icosatetraenoate = an oxoicosatetraenoate + H2O.

    Cofactori

    Binds 1 iron ion per subunit.PROSITE-ProRule annotation

    Kineticsi

    Has a 5 to 10 fold higher activity toward (12R)-HPETE (hydroperoxyeicosatetraenoic acid) compared to (12S)-HPETE and (15S)-HPETE. From (12R)-HPETE produces a stereoisomer of hepoxilin A3. More active on hydroperoxides with an R configuration than an S one.

    1. KM=46 µM for (12R)-HPETE3 Publications
    2. KM=28 µM for (12S)-HPETE3 Publications
    3. KM=32 µM for (15S)-HPETE3 Publications
    4. KM=50 µM for synthetic fatty acid 9E,11Z,14Z-20:3omega6 (at pH 7.5)3 Publications

    Vmax=3.256 µmol/min/mg enzyme for (12R)-HPETE (at pH 7.5)3 Publications

    Vmax=0.858 µmol/min/mg enzyme for (12S)-HPETE (at pH 7.5)3 Publications

    Vmax=0.484 µmol/min/mg enzyme for (15S)-HPETE (at pH 7.5)3 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi408 – 4081Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi413 – 4131Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi588 – 5881Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi592 – 5921Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi711 – 7111Iron; via carboxylate; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. hepoxilin A3 synthase activity Source: UniProtKB
    2. iron ion binding Source: InterPro
    3. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. arachidonic acid metabolic process Source: UniProtKB
    2. ceramide biosynthetic process Source: UniProtKB
    3. establishment of skin barrier Source: UniProtKB
    4. fat cell differentiation Source: UniProtKB
    5. hepoxilin biosynthetic process Source: UniProtKB
    6. linoleic acid metabolic process Source: UniProtKB
    7. lipoxygenase pathway Source: UniProtKB
    8. peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
    9. sensory perception of pain Source: UniProtKB
    10. sphingolipid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Isomerase, Lyase, 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:
    Hydroperoxide isomerase ALOXE3 (EC:5.4.4.7)
    Alternative name(s):
    Epidermis-type lipoxygenase 3
    Short name:
    Epidermal LOX-3
    Short name:
    e-LOX-3
    Short name:
    eLOX-3
    Hydroperoxy icosatetraenoate dehydratase (EC:4.2.1.152)
    Gene namesi
    Name:ALOXE3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:13743. ALOXE3.

    Subcellular locationi

    Cytoplasm PROSITE-ProRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Ichthyosis, congenital, autosomal recessive 3 (ARCI3) [MIM:606545]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non-bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti237 – 2371L → M in ARCI3; no effect on enzyme activity. 2 Publications
    VAR_069561
    Natural varianti281 – 2811G → V in ARCI3; complete loss of the enzyme activity. 1 Publication
    VAR_069562
    Natural varianti344 – 3474QYVA → P in ARCI3; complete loss of the enzyme activity.
    VAR_069563
    Natural varianti396 – 3961R → S in ARCI3; complete loss of the enzyme activity. 1 Publication
    VAR_015175
    Natural varianti427 – 4271L → P in ARCI3. 1 Publication
    VAR_069564
    Natural varianti500 – 5001V → F in ARCI3; complete loss of the enzyme activity. 1 Publication
    VAR_015176
    Natural varianti630 – 6301P → L in ARCI3; complete loss of the enzyme activity. 3 Publications
    VAR_069565

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi451 – 4511A → G: Increases the O2-dependent dioxygenase activity. 2 Publications

    Keywords - Diseasei

    Disease mutation, Ichthyosis

    Organism-specific databases

    MIMi606545. phenotype.
    Orphaneti79394. Congenital non-bullous ichthyosiform erythroderma.
    281122. Self-healing collodion baby.
    PharmGKBiPA24727.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 711711Hydroperoxide isomerase ALOXE3PRO_0000220691Add
    BLAST

    Proteomic databases

    PaxDbiQ9BYJ1.
    PRIDEiQ9BYJ1.

    Expressioni

    Tissue specificityi

    Predominantly expressed in skin.

    Gene expression databases

    ArrayExpressiQ9BYJ1.
    BgeeiQ9BYJ1.
    CleanExiHS_ALOXE3.
    GenevestigatoriQ9BYJ1.

    Organism-specific databases

    HPAiHPA023120.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ALOX12BO753422EBI-6925949,EBI-6925925

    Protein-protein interaction databases

    BioGridi121886. 1 interaction.
    IntActiQ9BYJ1. 2 interactions.
    STRINGi9606.ENSP00000314879.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BYJ1.
    SMRiQ9BYJ1. Positions 2-711.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 119118PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini120 – 711592LipoxygenasePROSITE-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.
    InParanoidiQ9BYJ1.
    OrthoDBiEOG7V49XR.
    PhylomeDBiQ9BYJ1.
    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. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BYJ1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAVYRLCVTT GPYLRAGTLD NISVTLVGTC GESPKQRLDR MGRDFAPGSV    50
    QKYKVRCTAE LGELLLLRVH KERYAFFRKD SWYCSRICVT EPDGSVSHFP 100
    CYQWIEGYCT VELRPGTART ICQDSLPLLL DHRTRELRAR QECYRWKIYA 150
    PGFPCMVDVN SFQEMESDKK FALTKTTTCV DQGDSSGNRY LPGFPMKIDI 200
    PSLMYMEPNV RYSATKTISL LFNAIPASLG MKLRGLLDRK GSWKKLDDMQ 250
    NIFWCHKTFT TKYVTEHWCE DHFFGYQYLN GVNPVMLHCI SSLPSKLPVT 300
    NDMVAPLLGQ DTCLQTELER GNIFLADYWI LAEAPTHCLN GRQQYVAAPL 350
    CLLWLSPQGA LVPLAIQLSQ TPGPDSPIFL PTDSEWDWLL AKTWVRNSEF 400
    LVHENNTHFL CTHLLCEAFA MATLRQLPLC HPIYKLLLPH TRYTLQVNTI 450
    ARATLLNPEG LVDQVTSIGR QGLIYLMSTG LAHFTYTNFC LPDSLRARGV 500
    LAIPNYHYRD DGLKIWAAIE SFVSEIVGYY YPSDASVQQD SELQAWTGEI 550
    FAQAFLGRES SGFPSRLCTP GEMVKFLTAI IFNCSAQHAA VNSGQHDFGA 600
    WMPNAPSSMR QPPPQTKGTT TLKTYLDTLP EVNISCNNLL LFWLVSQEPK 650
    DQRPLGTYPD EHFTEEAPRR SIAAFQSRLA QISRDIQERN QGLALPYTYL 700
    DPPLIENSVS I 711
    Length:711
    Mass (Da):80,543
    Last modified:June 1, 2001 - v1
    Checksum:iBDED1E4ED5CF6783
    GO
    Isoform 2 (identifier: Q9BYJ1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MPRGAFRPCL...PGHPFLLPIM

    Note: No experimental confirmation available.

    Show »
    Length:843
    Mass (Da):95,186
    Checksum:i75C69C336513F82C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti155 – 1551C → R in CAC12843. (PubMed:11350124)Curated
    Sequence conflicti194 – 1941F → L in AAG16899. (PubMed:12881489)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti237 – 2371L → M in ARCI3; no effect on enzyme activity. 2 Publications
    VAR_069561
    Natural varianti281 – 2811G → V in ARCI3; complete loss of the enzyme activity. 1 Publication
    VAR_069562
    Natural varianti344 – 3474QYVA → P in ARCI3; complete loss of the enzyme activity.
    VAR_069563
    Natural varianti396 – 3961R → S in ARCI3; complete loss of the enzyme activity. 1 Publication
    VAR_015175
    Natural varianti427 – 4271L → P in ARCI3. 1 Publication
    VAR_069564
    Natural varianti500 – 5001V → F in ARCI3; complete loss of the enzyme activity. 1 Publication
    VAR_015176
    Natural varianti630 – 6301P → L in ARCI3; complete loss of the enzyme activity. 3 Publications
    VAR_069565

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MPRGAFRPCLPALYFAFLTC PTPEQRMSGTQAPDIHLGEP ARGTGCVRGKQTSIRVQDCG RREEARAASRELRREKAQEH PRESWAHPQPYPAPQPLALR PETQPCPACRSSPPGRLLLR PALPGHPFLLPIM in isoform 2. 1 PublicationVSP_043287

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ269499 mRNA. Translation: CAC12843.1.
    AJ305020
    , AJ305021, AJ305023, AJ305025 Genomic DNA. Translation: CAC34518.1.
    AF182218 mRNA. Translation: AAG16899.1.
    AK296416 mRNA. Translation: BAH12346.1.
    AK313677 mRNA. Translation: BAG36428.1.
    CH471108 Genomic DNA. Translation: EAW90094.1.
    BC101938 mRNA. Translation: AAI01939.1.
    BC101939 mRNA. Translation: AAI01940.1.
    BC103508 mRNA. Translation: AAI03509.1.
    BC104724 mRNA. Translation: AAI04725.1.
    CCDSiCCDS11130.1. [Q9BYJ1-1]
    CCDS54084.1. [Q9BYJ1-2]
    RefSeqiNP_001159432.1. NM_001165960.1. [Q9BYJ1-2]
    NP_067641.2. NM_021628.2. [Q9BYJ1-1]
    UniGeneiHs.232770.

    Genome annotation databases

    EnsembliENST00000318227; ENSP00000314879; ENSG00000179148. [Q9BYJ1-2]
    ENST00000448843; ENSP00000400581; ENSG00000179148. [Q9BYJ1-1]
    GeneIDi59344.
    KEGGihsa:59344.
    UCSCiuc010cnr.3. human. [Q9BYJ1-1]
    uc010vuo.2. human. [Q9BYJ1-2]

    Polymorphism databases

    DMDMi27923803.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    about water - Issue 153 of September 2013

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ269499 mRNA. Translation: CAC12843.1 .
    AJ305020
    , AJ305021 , AJ305023 , AJ305025 Genomic DNA. Translation: CAC34518.1 .
    AF182218 mRNA. Translation: AAG16899.1 .
    AK296416 mRNA. Translation: BAH12346.1 .
    AK313677 mRNA. Translation: BAG36428.1 .
    CH471108 Genomic DNA. Translation: EAW90094.1 .
    BC101938 mRNA. Translation: AAI01939.1 .
    BC101939 mRNA. Translation: AAI01940.1 .
    BC103508 mRNA. Translation: AAI03509.1 .
    BC104724 mRNA. Translation: AAI04725.1 .
    CCDSi CCDS11130.1. [Q9BYJ1-1 ]
    CCDS54084.1. [Q9BYJ1-2 ]
    RefSeqi NP_001159432.1. NM_001165960.1. [Q9BYJ1-2 ]
    NP_067641.2. NM_021628.2. [Q9BYJ1-1 ]
    UniGenei Hs.232770.

    3D structure databases

    ProteinModelPortali Q9BYJ1.
    SMRi Q9BYJ1. Positions 2-711.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121886. 1 interaction.
    IntActi Q9BYJ1. 2 interactions.
    STRINGi 9606.ENSP00000314879.

    Polymorphism databases

    DMDMi 27923803.

    Proteomic databases

    PaxDbi Q9BYJ1.
    PRIDEi Q9BYJ1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318227 ; ENSP00000314879 ; ENSG00000179148 . [Q9BYJ1-2 ]
    ENST00000448843 ; ENSP00000400581 ; ENSG00000179148 . [Q9BYJ1-1 ]
    GeneIDi 59344.
    KEGGi hsa:59344.
    UCSCi uc010cnr.3. human. [Q9BYJ1-1 ]
    uc010vuo.2. human. [Q9BYJ1-2 ]

    Organism-specific databases

    CTDi 59344.
    GeneCardsi GC17M007999.
    GeneReviewsi ALOXE3.
    HGNCi HGNC:13743. ALOXE3.
    HPAi HPA023120.
    MIMi 606545. phenotype.
    607206. gene.
    neXtProti NX_Q9BYJ1.
    Orphaneti 79394. Congenital non-bullous ichthyosiform erythroderma.
    281122. Self-healing collodion baby.
    PharmGKBi PA24727.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG69653.
    HOGENOMi HOG000234358.
    HOVERGENi HBG005150.
    InParanoidi Q9BYJ1.
    OrthoDBi EOG7V49XR.
    PhylomeDBi Q9BYJ1.
    TreeFami TF105320.

    Enzyme and pathway databases

    UniPathwayi UPA00222 .
    UPA00881 .

    Miscellaneous databases

    ChiTaRSi ALOXE3. human.
    GeneWikii ALOXE3.
    GenomeRNAii 59344.
    NextBioi 65242.
    PROi Q9BYJ1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BYJ1.
    Bgeei Q9BYJ1.
    CleanExi HS_ALOXE3.
    Genevestigatori Q9BYJ1.

    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. "A gene cluster encoding human epidermis-type lipoxygenases at chromosome 17p13.1: cloning, physical mapping, and expression."
      Krieg P., Marks F., Fuerstenberger G.
      Genomics 73:323-330(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    2. "The lipoxygenase gene ALOXE3 implicated in skin differentiation encodes a hydroperoxide isomerase."
      Yu Z., Schneider C., Boeglin W.E., Marnett L.J., Brash A.R.
      Proc. Natl. Acad. Sci. U.S.A. 100:9162-9167(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN HEPOXILIN A3 SYNTHESIS, CATALYTIC ACTIVITY, PATHWAY, REACTION MECHANISM, KINETIC PARAMETERS.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Thalamus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
    6. "Human and mouse eLOX3 have distinct substrate specificities: implications for their linkage with lipoxygenases in skin."
      Yu Z., Schneider C., Boeglin W.E., Brash A.R.
      Arch. Biochem. Biophys. 455:188-196(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A HYDROPEROXIDE ISOMERASE, CATALYTIC ACTIVITY, KINETIC PARAMETERS, PATHWAY.
    7. "Dioxygenase activity of epidermal lipoxygenase-3 unveiled: typical and atypical features of its catalytic activity with natural and synthetic polyunsaturated fatty acids."
      Zheng Y., Brash A.R.
      J. Biol. Chem. 285:39866-39875(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A DIOXYGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ALA-451.
    8. "On the role of molecular oxygen in lipoxygenase activation: comparison and contrast of epidermal lipoxygenase-3 with soybean lipoxygenase-1."
      Zheng Y., Brash A.R.
      J. Biol. Chem. 285:39876-39887(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A DIOXYGENASE, CATALYTIC ACTIVITY, MUTAGENESIS OF ALA-451.
    9. "Lipoxygenases mediate the effect of essential fatty acid in skin barrier formation: a proposed role in releasing omega-hydroxyceramide for construction of the corneocyte lipid envelope."
      Zheng Y., Yin H., Boeglin W.E., Elias P.M., Crumrine D., Beier D.R., Brash A.R.
      J. Biol. Chem. 286:24046-24056(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CERAMIDE METABOLISM, CATALYTIC ACTIVITY.
    10. "Lipoxygenase-3 (ALOXE3) and 12(R)-lipoxygenase (ALOX12B) are mutated in non-bullous congenital ichthyosiform erythroderma (NCIE) linked to chromosome 17p13.1."
      Jobard F., Lefevre C., Karaduman A., Blanchet-Bardon C., Emre S., Weissenbach J., Ozguc M., Lathrop M., Prud'homme J.-F., Fischer J.
      Hum. Mol. Genet. 11:107-113(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARCI3 SER-396 AND PHE-500.
    11. "Mutations associated with a congenital form of ichthyosis (NCIE) inactivate the epidermal lipoxygenases 12R-LOX and eLOX3."
      Yu Z., Schneider C., Boeglin W.E., Brash A.R.
      Biochim. Biophys. Acta 1686:238-247(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS ARCI3 SER-396 AND PHE-500.
    12. "Mutation spectrum and functional analysis of epidermis-type lipoxygenases in patients with autosomal recessive congenital ichthyosis."
      Eckl K.M., Krieg P., Kuester W., Traupe H., Andre F., Wittstruck N., Fuerstenberger G., Hennies H.C.
      Hum. Mutat. 26:351-361(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARCI3 MET-237; VAL-281 AND LEU-630, CHARACTERIZATION OF VARIANTS ARCI3 MET-237; VAL-281 AND LEU-630.
    13. "Molecular analysis of 250 patients with autosomal recessive congenital ichthyosis: evidence for mutation hotspots in ALOXE3 and allelic heterogeneity in ALOX12B."
      Eckl K.M., de Juanes S., Kurtenbach J., Naetebus M., Lugassy J., Oji V., Traupe H., Preil M.L., Martinez F., Smolle J., Harel A., Krieg P., Sprecher E., Hennies H.C.
      J. Invest. Dermatol. 129:1421-1428(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARCI3 MET-237; 344-GLN--ALA-347 DELINS PRO AND LEU-630, CHARACTERIZATION OF VARIANT 344-GLN--ALA-347 DELINS PRO.
    14. "Genotypic and clinical spectrum of self-improving collodion ichthyosis: ALOX12B, ALOXE3, and TGM1 mutations in Scandinavian patients."
      Vahlquist A., Bygum A., Gaanemo A., Virtanen M., Hellstroem-Pigg M., Strauss G., Brandrup F., Fischer J.
      J. Invest. Dermatol. 130:438-443(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARCI3 PRO-427 AND LEU-630.

    Entry informationi

    Entry nameiLOXE3_HUMAN
    AccessioniPrimary (citable) accession number: Q9BYJ1
    Secondary accession number(s): B2R981
    , B7Z3W0, Q3ZB74, Q9H4F2, Q9HC22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 27, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

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