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Q9BYJ1

- LOXE3_HUMAN

UniProt

Q9BYJ1 - LOXE3_HUMAN

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Protein

Hydroperoxide isomerase ALOXE3

Gene

ALOXE3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. lyase activity Source: UniProtKB-KW
  4. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen 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. 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
Complete GO annotation...

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-KW
Complete GO annotation...

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. 1 Publication
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

BgeeiQ9BYJ1.
CleanExiHS_ALOXE3.
ExpressionAtlasiQ9BYJ1. baseline and differential.
GenevestigatoriQ9BYJ1.

Organism-specific databases

HPAiHPA023120.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi121886. 9 interactions.
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.
GeneTreeiENSGT00550000074415.
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

        10         20         30         40         50
MAVYRLCVTT GPYLRAGTLD NISVTLVGTC GESPKQRLDR MGRDFAPGSV
60 70 80 90 100
QKYKVRCTAE LGELLLLRVH KERYAFFRKD SWYCSRICVT EPDGSVSHFP
110 120 130 140 150
CYQWIEGYCT VELRPGTART ICQDSLPLLL DHRTRELRAR QECYRWKIYA
160 170 180 190 200
PGFPCMVDVN SFQEMESDKK FALTKTTTCV DQGDSSGNRY LPGFPMKIDI
210 220 230 240 250
PSLMYMEPNV RYSATKTISL LFNAIPASLG MKLRGLLDRK GSWKKLDDMQ
260 270 280 290 300
NIFWCHKTFT TKYVTEHWCE DHFFGYQYLN GVNPVMLHCI SSLPSKLPVT
310 320 330 340 350
NDMVAPLLGQ DTCLQTELER GNIFLADYWI LAEAPTHCLN GRQQYVAAPL
360 370 380 390 400
CLLWLSPQGA LVPLAIQLSQ TPGPDSPIFL PTDSEWDWLL AKTWVRNSEF
410 420 430 440 450
LVHENNTHFL CTHLLCEAFA MATLRQLPLC HPIYKLLLPH TRYTLQVNTI
460 470 480 490 500
ARATLLNPEG LVDQVTSIGR QGLIYLMSTG LAHFTYTNFC LPDSLRARGV
510 520 530 540 550
LAIPNYHYRD DGLKIWAAIE SFVSEIVGYY YPSDASVQQD SELQAWTGEI
560 570 580 590 600
FAQAFLGRES SGFPSRLCTP GEMVKFLTAI IFNCSAQHAA VNSGQHDFGA
610 620 630 640 650
WMPNAPSSMR QPPPQTKGTT TLKTYLDTLP EVNISCNNLL LFWLVSQEPK
660 670 680 690 700
DQRPLGTYPD EHFTEEAPRR SIAAFQSRLA QISRDIQERN QGLALPYTYL
710
DPPLIENSVS I
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. 1 Publication
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. 9 interactions.
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.
GeneTreei ENSGT00550000074415.
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

Bgeei Q9BYJ1.
CleanExi HS_ALOXE3.
ExpressionAtlasi Q9BYJ1. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 122 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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