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Q9BYJ1 (LOXE3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hydroperoxide isomerase ALOXE3

EC=5.4.4.-
Alternative name(s):
Epidermis-type lipoxygenase 3
Short name=Epidermal LOX-3
Short name=e-LOX-3
Short name=eLOX-3
EC=1.13.11.-
Gene names
Name:ALOXE3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length711 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.6 Ref.7 Ref.8 Ref.9

Catalytic activity

(5Z,8Z,10E,14Z)-(12R)-12-hydroperoxyicosa-5,8,10,14-tetraenoate = (5Z,9E,14Z)-(8R,11R,12R)-8-hydroxy-11,12-hydroperoxyicosa-5,9,14-trienoate. Ref.2 Ref.6 Ref.7 Ref.8 Ref.9

Cofactor

Binds 1 iron ion per subunit By similarity.

Pathway

Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. Ref.2 Ref.6

Lipid metabolism; sphingolipid metabolism. Ref.2 Ref.6

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Predominantly expressed in skin.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Biophysicochemical properties

Kinetic parameters:

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.

KM=46 µM for (12R)-HPETE Ref.2 Ref.6 Ref.7

KM=28 µM for (12S)-HPETE

KM=32 µM for (15S)-HPETE

KM=50 µM for synthetic fatty acid 9E,11Z,14Z-20:3omega6 (at pH 7.5)

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

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

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

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Ichthyosis
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Isomerase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Inferred from direct assay Ref.2Ref.6. Source: UniProtKB

ceramide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of skin barrier

Inferred from sequence or structural similarity. Source: UniProtKB

fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

hepoxilin biosynthetic process

Inferred from direct assay Ref.2Ref.6. Source: UniProtKB

linoleic acid metabolic process

Inferred from direct assay Ref.2Ref.6. Source: UniProtKB

lipoxygenase pathway

Inferred from direct assay Ref.7. Source: UniProtKB

peroxisome proliferator activated receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

sensory perception of pain

Inferred from sequence or structural similarity. Source: UniProtKB

sphingolipid metabolic process

Inferred from direct assay Ref.9. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhepoxilin A3 synthase activity

Inferred from direct assay Ref.2Ref.6. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen

Inferred from direct assay Ref.7. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 22622417. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ALOX12BO753422EBI-6925949,EBI-6925925

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BYJ1-1)

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.
Isoform 2 (identifier: Q9BYJ1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPRGAFRPCL...PGHPFLLPIM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 711711Hydroperoxide isomerase ALOXE3
PRO_0000220691

Regions

Domain2 – 119118PLAT
Domain120 – 711592Lipoxygenase

Sites

Metal binding4081Iron; catalytic By similarity
Metal binding4131Iron; catalytic By similarity
Metal binding5881Iron; catalytic By similarity
Metal binding5921Iron; catalytic By similarity
Metal binding7111Iron; via carboxylate; catalytic By similarity

Natural variations

Alternative sequence11M → MPRGAFRPCLPALYFAFLTC PTPEQRMSGTQAPDIHLGEP ARGTGCVRGKQTSIRVQDCG RREEARAASRELRREKAQEH PRESWAHPQPYPAPQPLALR PETQPCPACRSSPPGRLLLR PALPGHPFLLPIM in isoform 2.
VSP_043287
Natural variant2371L → M in ARCI3; no effect on enzyme activity. Ref.12 Ref.13
VAR_069561
Natural variant2811G → V in ARCI3; complete loss of the enzyme activity. Ref.12
VAR_069562
Natural variant344 – 3474QYVA → P in ARCI3; complete loss of the enzyme activity.
VAR_069563
Natural variant3961R → S in ARCI3; complete loss of the enzyme activity. Ref.10 Ref.11
VAR_015175
Natural variant4271L → P in ARCI3. Ref.14
VAR_069564
Natural variant5001V → F in ARCI3; complete loss of the enzyme activity. Ref.10 Ref.11
VAR_015176
Natural variant6301P → L in ARCI3; complete loss of the enzyme activity. Ref.12 Ref.13 Ref.14
VAR_069565

Experimental info

Mutagenesis4511A → G: Increases the O2-dependent dioxygenase activity. Ref.7 Ref.8
Sequence conflict1551C → R in CAC12843. Ref.1
Sequence conflict1941F → L in AAG16899. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: BDED1E4ED5CF6783

FASTA71180,543
        10         20         30         40         50         60 
MAVYRLCVTT GPYLRAGTLD NISVTLVGTC GESPKQRLDR MGRDFAPGSV QKYKVRCTAE 

        70         80         90        100        110        120 
LGELLLLRVH KERYAFFRKD SWYCSRICVT EPDGSVSHFP CYQWIEGYCT VELRPGTART 

       130        140        150        160        170        180 
ICQDSLPLLL DHRTRELRAR QECYRWKIYA PGFPCMVDVN SFQEMESDKK FALTKTTTCV 

       190        200        210        220        230        240 
DQGDSSGNRY LPGFPMKIDI PSLMYMEPNV RYSATKTISL LFNAIPASLG MKLRGLLDRK 

       250        260        270        280        290        300 
GSWKKLDDMQ NIFWCHKTFT TKYVTEHWCE DHFFGYQYLN GVNPVMLHCI SSLPSKLPVT 

       310        320        330        340        350        360 
NDMVAPLLGQ DTCLQTELER GNIFLADYWI LAEAPTHCLN GRQQYVAAPL CLLWLSPQGA 

       370        380        390        400        410        420 
LVPLAIQLSQ TPGPDSPIFL PTDSEWDWLL AKTWVRNSEF LVHENNTHFL CTHLLCEAFA 

       430        440        450        460        470        480 
MATLRQLPLC HPIYKLLLPH TRYTLQVNTI ARATLLNPEG LVDQVTSIGR QGLIYLMSTG 

       490        500        510        520        530        540 
LAHFTYTNFC LPDSLRARGV LAIPNYHYRD DGLKIWAAIE SFVSEIVGYY YPSDASVQQD 

       550        560        570        580        590        600 
SELQAWTGEI FAQAFLGRES SGFPSRLCTP GEMVKFLTAI IFNCSAQHAA VNSGQHDFGA 

       610        620        630        640        650        660 
WMPNAPSSMR QPPPQTKGTT TLKTYLDTLP EVNISCNNLL LFWLVSQEPK DQRPLGTYPD 

       670        680        690        700        710 
EHFTEEAPRR SIAAFQSRLA QISRDIQERN QGLALPYTYL DPPLIENSVS I 

« Hide

Isoform 2 [UniParc].

Checksum: 75C69C336513F82C
Show »

FASTA84395,186

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Web resources

Protein Spotlight

about water - Issue 153 of September 2013

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ269499 mRNA. Translation: CAC12843.1.
AJ305020 expand/collapse EMBL AC list , 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.
CCDSCCDS11130.1. [Q9BYJ1-1]
CCDS54084.1. [Q9BYJ1-2]
RefSeqNP_001159432.1. NM_001165960.1. [Q9BYJ1-2]
NP_067641.2. NM_021628.2. [Q9BYJ1-1]
UniGeneHs.232770.

3D structure databases

ProteinModelPortalQ9BYJ1.
SMRQ9BYJ1. Positions 2-711.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121886. 1 interaction.
IntActQ9BYJ1. 2 interactions.
STRING9606.ENSP00000314879.

Polymorphism databases

DMDM27923803.

Proteomic databases

PaxDbQ9BYJ1.
PRIDEQ9BYJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318227; ENSP00000314879; ENSG00000179148. [Q9BYJ1-2]
ENST00000448843; ENSP00000400581; ENSG00000179148. [Q9BYJ1-1]
GeneID59344.
KEGGhsa:59344.
UCSCuc010cnr.3. human. [Q9BYJ1-1]
uc010vuo.2. human. [Q9BYJ1-2]

Organism-specific databases

CTD59344.
GeneCardsGC17M007999.
GeneReviewsALOXE3.
HGNCHGNC:13743. ALOXE3.
HPAHPA023120.
MIM606545. phenotype.
607206. gene.
neXtProtNX_Q9BYJ1.
Orphanet79394. Congenital non-bullous ichthyosiform erythroderma.
281122. Self-healing collodion baby.
PharmGKBPA24727.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69653.
HOGENOMHOG000234358.
HOVERGENHBG005150.
InParanoidQ9BYJ1.
OrthoDBEOG7V49XR.
PhylomeDBQ9BYJ1.
TreeFamTF105320.

Enzyme and pathway databases

UniPathwayUPA00222.
UPA00881.

Gene expression databases

ArrayExpressQ9BYJ1.
BgeeQ9BYJ1.
CleanExHS_ALOXE3.
GenevestigatorQ9BYJ1.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11771. PTHR11771. 1 hit.
PfamPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALOXE3. human.
GeneWikiALOXE3.
GenomeRNAi59344.
NextBio65242.
PROQ9BYJ1.
SOURCESearch...

Entry information

Entry nameLOXE3_HUMAN
AccessionPrimary (citable) accession number: Q9BYJ1
Secondary accession number(s): B2R981 expand/collapse secondary AC list , B7Z3W0, Q3ZB74, Q9H4F2, Q9HC22
Entry history
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM