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Hydroperoxide isomerase ALOXE3 (EC 5.4.4.7) (Epidermis-type lipoxygenase 3) (Epidermal LOX-3) (e-LOX-3) (eLOX-3) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152)

 LOXE3_HUMAN             Reviewed;         711 AA.
Q9BYJ1; B2R981; B7Z3W0; Q3ZB74; Q9H4F2; Q9HC22;
27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
28-MAR-2018, entry version 146.
RecName: Full=Hydroperoxide isomerase ALOXE3;
EC=5.4.4.7 {ECO:0000269|PubMed:12881489, ECO:0000269|PubMed:17045234, ECO:0000269|PubMed:20921226, ECO:0000269|PubMed:20923767, ECO:0000269|PubMed:21558561};
AltName: Full=Epidermis-type lipoxygenase 3 {ECO:0000303|PubMed:11350124};
Short=Epidermal LOX-3;
Short=e-LOX-3;
Short=eLOX-3;
AltName: Full=Hydroperoxy icosatetraenoate dehydratase;
EC=4.2.1.152 {ECO:0000269|PubMed:12881489, ECO:0000269|PubMed:17045234, ECO:0000269|PubMed:20921226, ECO:0000269|PubMed:20923767, ECO:0000269|PubMed:21558561};
Name=ALOXE3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=11350124; DOI=10.1006/geno.2001.6519;
Krieg P., Marks F., Fuerstenberger G.;
"A gene cluster encoding human epidermis-type lipoxygenases at
chromosome 17p13.1: cloning, physical mapping, and expression.";
Genomics 73:323-330(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN HEPOXILIN A3
SYNTHESIS, CATALYTIC ACTIVITY, PATHWAY, REACTION MECHANISM, AND
KINETIC PARAMETERS.
PubMed=12881489; DOI=10.1073/pnas.1633612100;
Yu Z., Schneider C., Boeglin W.E., Marnett L.J., Brash A.R.;
"The lipoxygenase gene ALOXE3 implicated in skin differentiation
encodes a hydroperoxide isomerase.";
Proc. Natl. Acad. Sci. U.S.A. 100:9162-9167(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION AS A HYDROPEROXIDE ISOMERASE, CATALYTIC ACTIVITY, KINETIC
PARAMETERS, AND PATHWAY.
PubMed=17045234; DOI=10.1016/j.abb.2006.09.002;
Yu Z., Schneider C., Boeglin W.E., Brash A.R.;
"Human and mouse eLOX3 have distinct substrate specificities:
implications for their linkage with lipoxygenases in skin.";
Arch. Biochem. Biophys. 455:188-196(2006).
[7]
FUNCTION AS A DIOXYGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND MUTAGENESIS OF ALA-451.
PubMed=20921226; DOI=10.1074/jbc.M110.155374;
Zheng Y., Brash A.R.;
"Dioxygenase activity of epidermal lipoxygenase-3 unveiled: typical
and atypical features of its catalytic activity with natural and
synthetic polyunsaturated fatty acids.";
J. Biol. Chem. 285:39866-39875(2010).
[8]
FUNCTION AS A DIOXYGENASE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
ALA-451.
PubMed=20923767; DOI=10.1074/jbc.M110.180794;
Zheng Y., Brash A.R.;
"On the role of molecular oxygen in lipoxygenase activation:
comparison and contrast of epidermal lipoxygenase-3 with soybean
lipoxygenase-1.";
J. Biol. Chem. 285:39876-39887(2010).
[9]
FUNCTION IN CERAMIDE METABOLISM, AND CATALYTIC ACTIVITY.
PubMed=21558561; DOI=10.1074/jbc.M111.251496;
Zheng Y., Yin H., Boeglin W.E., Elias P.M., Crumrine D., Beier D.R.,
Brash A.R.;
"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.";
J. Biol. Chem. 286:24046-24056(2011).
[10]
VARIANTS ARCI3 SER-396 AND PHE-500.
PubMed=11773004; DOI=10.1093/hmg/11.1.107;
Jobard F., Lefevre C., Karaduman A., Blanchet-Bardon C., Emre S.,
Weissenbach J., Ozguc M., Lathrop M., Prud'homme J.-F., Fischer J.;
"Lipoxygenase-3 (ALOXE3) and 12(R)-lipoxygenase (ALOX12B) are mutated
in non-bullous congenital ichthyosiform erythroderma (NCIE) linked to
chromosome 17p13.1.";
Hum. Mol. Genet. 11:107-113(2002).
[11]
CHARACTERIZATION OF VARIANTS ARCI3 SER-396 AND PHE-500.
PubMed=15629692; DOI=10.1016/j.bbalip.2004.10.007;
Yu Z., Schneider C., Boeglin W.E., Brash A.R.;
"Mutations associated with a congenital form of ichthyosis (NCIE)
inactivate the epidermal lipoxygenases 12R-LOX and eLOX3.";
Biochim. Biophys. Acta 1686:238-247(2005).
[12]
VARIANTS ARCI3 MET-237; VAL-281 AND LEU-630, AND CHARACTERIZATION OF
VARIANTS ARCI3 MET-237; VAL-281 AND LEU-630.
PubMed=16116617; DOI=10.1002/humu.20236;
Eckl K.M., Krieg P., Kuester W., Traupe H., Andre F., Wittstruck N.,
Fuerstenberger G., Hennies H.C.;
"Mutation spectrum and functional analysis of epidermis-type
lipoxygenases in patients with autosomal recessive congenital
ichthyosis.";
Hum. Mutat. 26:351-361(2005).
[13]
VARIANTS ARCI3 MET-237; 344-GLN--ALA-347 DELINS PRO AND LEU-630, AND
CHARACTERIZATION OF VARIANT 344-GLN--ALA-347 DELINS PRO.
PubMed=19131948; DOI=10.1038/jid.2008.409;
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.;
"Molecular analysis of 250 patients with autosomal recessive
congenital ichthyosis: evidence for mutation hotspots in ALOXE3 and
allelic heterogeneity in ALOX12B.";
J. Invest. Dermatol. 129:1421-1428(2009).
[14]
VARIANTS ARCI3 PRO-427 AND LEU-630.
PubMed=19890349; DOI=10.1038/jid.2009.346;
Vahlquist A., Bygum A., Gaanemo A., Virtanen M., Hellstroem-Pigg M.,
Strauss G., Brandrup F., Fischer J.;
"Genotypic and clinical spectrum of self-improving collodion
ichthyosis: ALOX12B, ALOXE3, and TGM1 mutations in Scandinavian
patients.";
J. Invest. Dermatol. 130:438-443(2010).
-!- 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.
{ECO:0000269|PubMed:12881489, ECO:0000269|PubMed:17045234,
ECO:0000269|PubMed:20921226, ECO:0000269|PubMed:20923767,
ECO:0000269|PubMed:21558561}.
-!- CATALYTIC ACTIVITY: A hydroperoxy icosatetraenoate = a hydroxy
epoxy icosatrienoate. {ECO:0000269|PubMed:12881489,
ECO:0000269|PubMed:17045234, ECO:0000269|PubMed:20921226,
ECO:0000269|PubMed:20923767, ECO:0000269|PubMed:21558561}.
-!- CATALYTIC ACTIVITY: A hydroperoxy icosatetraenoate = an
oxoicosatetraenoate + H(2)O. {ECO:0000269|PubMed:12881489,
ECO:0000269|PubMed:17045234, ECO:0000269|PubMed:20921226,
ECO:0000269|PubMed:20923767, ECO:0000269|PubMed:21558561}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00726};
Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00726};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=46 uM for (12R)-HPETE {ECO:0000269|PubMed:12881489,
ECO:0000269|PubMed:17045234, ECO:0000269|PubMed:20921226};
KM=28 uM for (12S)-HPETE {ECO:0000269|PubMed:12881489,
ECO:0000269|PubMed:17045234, ECO:0000269|PubMed:20921226};
KM=32 uM for (15S)-HPETE {ECO:0000269|PubMed:12881489,
ECO:0000269|PubMed:17045234, ECO:0000269|PubMed:20921226};
KM=50 uM for synthetic fatty acid 9E,11Z,14Z-20:3omega6 (at pH
7.5) {ECO:0000269|PubMed:12881489, ECO:0000269|PubMed:17045234,
ECO:0000269|PubMed:20921226};
Vmax=3.256 umol/min/mg enzyme for (12R)-HPETE (at pH 7.5)
{ECO:0000269|PubMed:12881489, ECO:0000269|PubMed:17045234,
ECO:0000269|PubMed:20921226};
Vmax=0.858 umol/min/mg enzyme for (12S)-HPETE (at pH 7.5)
{ECO:0000269|PubMed:12881489, ECO:0000269|PubMed:17045234,
ECO:0000269|PubMed:20921226};
Vmax=0.484 umol/min/mg enzyme for (15S)-HPETE (at pH 7.5)
{ECO:0000269|PubMed:12881489, ECO:0000269|PubMed:17045234,
ECO:0000269|PubMed:20921226};
Note=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.;
-!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid
biosynthesis.
-!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
-!- INTERACTION:
O75342:ALOX12B; NbExp=2; IntAct=EBI-6925949, EBI-6925925;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-
ProRule:PRU00726}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BYJ1-1; Sequence=Displayed;
Name=2;
IsoId=Q9BYJ1-2; Sequence=VSP_043287;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in skin.
-!- 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. {ECO:0000269|PubMed:11773004,
ECO:0000269|PubMed:15629692, ECO:0000269|PubMed:16116617,
ECO:0000269|PubMed:19131948, ECO:0000269|PubMed:19890349}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=about water - Issue 153
of September 2013;
URL="https://web.expasy.org/spotlight/back_issues/153/";
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EMBL; AJ269499; CAC12843.1; -; mRNA.
EMBL; AJ305020; CAC34518.1; -; Genomic_DNA.
EMBL; AJ305021; CAC34518.1; JOINED; Genomic_DNA.
EMBL; AJ305023; CAC34518.1; JOINED; Genomic_DNA.
EMBL; AJ305025; CAC34518.1; JOINED; Genomic_DNA.
EMBL; AF182218; AAG16899.1; -; mRNA.
EMBL; AK296416; BAH12346.1; -; mRNA.
EMBL; AK313677; BAG36428.1; -; mRNA.
EMBL; CH471108; EAW90094.1; -; Genomic_DNA.
EMBL; BC101938; AAI01939.1; -; mRNA.
EMBL; BC101939; AAI01940.1; -; mRNA.
EMBL; BC103508; AAI03509.1; -; mRNA.
EMBL; BC104724; AAI04725.1; -; mRNA.
CCDS; CCDS11130.1; -. [Q9BYJ1-1]
CCDS; CCDS54084.1; -. [Q9BYJ1-2]
RefSeq; NP_001159432.1; NM_001165960.1. [Q9BYJ1-2]
RefSeq; NP_067641.2; NM_021628.2. [Q9BYJ1-1]
UniGene; Hs.232770; -.
ProteinModelPortal; Q9BYJ1; -.
SMR; Q9BYJ1; -.
BioGrid; 121886; 29.
IntAct; Q9BYJ1; 2.
STRING; 9606.ENSP00000314879; -.
SwissLipids; SLP:000000656; -.
iPTMnet; Q9BYJ1; -.
PhosphoSitePlus; Q9BYJ1; -.
BioMuta; ALOXE3; -.
DMDM; 27923803; -.
PaxDb; Q9BYJ1; -.
PeptideAtlas; Q9BYJ1; -.
PRIDE; Q9BYJ1; -.
Ensembl; ENST00000318227; ENSP00000314879; ENSG00000179148. [Q9BYJ1-2]
Ensembl; ENST00000448843; ENSP00000400581; ENSG00000179148. [Q9BYJ1-1]
GeneID; 59344; -.
KEGG; hsa:59344; -.
UCSC; uc010cnr.4; human. [Q9BYJ1-1]
CTD; 59344; -.
DisGeNET; 59344; -.
EuPathDB; HostDB:ENSG00000179148.9; -.
GeneCards; ALOXE3; -.
GeneReviews; ALOXE3; -.
HGNC; HGNC:13743; ALOXE3.
HPA; HPA023120; -.
MalaCards; ALOXE3; -.
MIM; 606545; phenotype.
MIM; 607206; gene.
neXtProt; NX_Q9BYJ1; -.
OpenTargets; ENSG00000179148; -.
Orphanet; 79394; Congenital non-bullous ichthyosiform erythroderma.
Orphanet; 281122; Self-healing collodion baby.
PharmGKB; PA24727; -.
eggNOG; ENOG410IF0U; Eukaryota.
eggNOG; ENOG410YN4N; LUCA.
GeneTree; ENSGT00550000074415; -.
HOGENOM; HOG000234358; -.
HOVERGEN; HBG005150; -.
InParanoid; Q9BYJ1; -.
KO; K18684; -.
PhylomeDB; Q9BYJ1; -.
TreeFam; TF105320; -.
Reactome; R-HSA-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
UniPathway; UPA00222; -.
UniPathway; UPA00881; -.
ChiTaRS; ALOXE3; human.
GeneWiki; ALOXE3; -.
GenomeRNAi; 59344; -.
PRO; PR:Q9BYJ1; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000179148; -.
CleanEx; HS_ALOXE3; -.
ExpressionAtlas; Q9BYJ1; baseline and differential.
Genevisible; Q9BYJ1; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0051120; F:hepoxilin A3 synthase activity; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:UniProtKB.
GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
GO; GO:0046513; P:ceramide biosynthetic process; ISS:UniProtKB.
GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
GO; GO:0051122; P:hepoxilin biosynthetic process; IDA:UniProtKB.
GO; GO:0043651; P:linoleic acid metabolic process; IDA:UniProtKB.
GO; GO:0019372; P:lipoxygenase pathway; IDA:UniProtKB.
GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; ISS:UniProtKB.
GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
GO; GO:0006665; P:sphingolipid metabolic process; IDA:UniProtKB.
InterPro; IPR000907; LipOase.
InterPro; IPR013819; LipOase_C.
InterPro; IPR036226; LipOase_C_sf.
InterPro; IPR020834; LipOase_CS.
InterPro; IPR020833; LipOase_Fe_BS.
InterPro; IPR001885; LipOase_mml.
InterPro; IPR001024; PLAT/LH2_dom.
InterPro; IPR036392; PLAT/LH2_dom_sf.
PANTHER; PTHR11771; PTHR11771; 1.
Pfam; PF00305; Lipoxygenase; 1.
Pfam; PF01477; PLAT; 1.
PRINTS; PR00087; LIPOXYGENASE.
PRINTS; PR00467; MAMLPOXGNASE.
SMART; SM00308; LH2; 1.
SUPFAM; SSF48484; SSF48484; 1.
SUPFAM; SSF49723; SSF49723; 1.
PROSITE; PS00711; LIPOXYGENASE_1; 1.
PROSITE; PS00081; LIPOXYGENASE_2; 1.
PROSITE; PS51393; LIPOXYGENASE_3; 1.
PROSITE; PS50095; PLAT; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Dioxygenase;
Disease mutation; Fatty acid metabolism; Ichthyosis; Iron; Isomerase;
Lipid metabolism; Lyase; Metal-binding; Oxidoreductase;
Reference proteome.
CHAIN 1 711 Hydroperoxide isomerase ALOXE3.
/FTId=PRO_0000220691.
DOMAIN 2 119 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
DOMAIN 120 711 Lipoxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 408 408 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 413 413 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 588 588 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 592 592 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 711 711 Iron; via carboxylate; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00726}.
VAR_SEQ 1 1 M -> MPRGAFRPCLPALYFAFLTCPTPEQRMSGTQAPDIH
LGEPARGTGCVRGKQTSIRVQDCGRREEARAASRELRREKA
QEHPRESWAHPQPYPAPQPLALRPETQPCPACRSSPPGRLL
LRPALPGHPFLLPIM (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043287.
VARIANT 237 237 L -> M (in ARCI3; no effect on enzyme
activity; dbSNP:rs121434235).
{ECO:0000269|PubMed:16116617,
ECO:0000269|PubMed:19131948}.
/FTId=VAR_069561.
VARIANT 281 281 G -> V (in ARCI3; complete loss of the
enzyme activity; dbSNP:rs786205120).
{ECO:0000269|PubMed:16116617}.
/FTId=VAR_069562.
VARIANT 344 347 QYVA -> P (in ARCI3; complete loss of the
enzyme activity).
{ECO:0000269|PubMed:19131948}.
/FTId=VAR_069563.
VARIANT 396 396 R -> S (in ARCI3; complete loss of the
enzyme activity; dbSNP:rs121434234).
{ECO:0000269|PubMed:11773004,
ECO:0000269|PubMed:15629692}.
/FTId=VAR_015175.
VARIANT 427 427 L -> P (in ARCI3).
{ECO:0000269|PubMed:19890349}.
/FTId=VAR_069564.
VARIANT 500 500 V -> F (in ARCI3; complete loss of the
enzyme activity; dbSNP:rs121434232).
{ECO:0000269|PubMed:11773004,
ECO:0000269|PubMed:15629692}.
/FTId=VAR_015176.
VARIANT 630 630 P -> L (in ARCI3; complete loss of the
enzyme activity; dbSNP:rs147149459).
{ECO:0000269|PubMed:16116617,
ECO:0000269|PubMed:19131948,
ECO:0000269|PubMed:19890349}.
/FTId=VAR_069565.
MUTAGEN 451 451 A->G: Increases the O2-dependent
dioxygenase activity.
{ECO:0000269|PubMed:20921226,
ECO:0000269|PubMed:20923767}.
CONFLICT 155 155 C -> R (in Ref. 1; CAC12843).
{ECO:0000305}.
CONFLICT 194 194 F -> L (in Ref. 2; AAG16899).
{ECO:0000305}.
SEQUENCE 711 AA; 80543 MW; BDED1E4ED5CF6783 CRC64;
MAVYRLCVTT GPYLRAGTLD NISVTLVGTC GESPKQRLDR MGRDFAPGSV QKYKVRCTAE
LGELLLLRVH KERYAFFRKD SWYCSRICVT EPDGSVSHFP CYQWIEGYCT VELRPGTART
ICQDSLPLLL DHRTRELRAR QECYRWKIYA PGFPCMVDVN SFQEMESDKK FALTKTTTCV
DQGDSSGNRY LPGFPMKIDI PSLMYMEPNV RYSATKTISL LFNAIPASLG MKLRGLLDRK
GSWKKLDDMQ NIFWCHKTFT TKYVTEHWCE DHFFGYQYLN GVNPVMLHCI SSLPSKLPVT
NDMVAPLLGQ DTCLQTELER GNIFLADYWI LAEAPTHCLN GRQQYVAAPL CLLWLSPQGA
LVPLAIQLSQ TPGPDSPIFL PTDSEWDWLL AKTWVRNSEF LVHENNTHFL CTHLLCEAFA
MATLRQLPLC HPIYKLLLPH TRYTLQVNTI ARATLLNPEG LVDQVTSIGR QGLIYLMSTG
LAHFTYTNFC LPDSLRARGV LAIPNYHYRD DGLKIWAAIE SFVSEIVGYY YPSDASVQQD
SELQAWTGEI FAQAFLGRES SGFPSRLCTP GEMVKFLTAI IFNCSAQHAA VNSGQHDFGA
WMPNAPSSMR QPPPQTKGTT TLKTYLDTLP EVNISCNNLL LFWLVSQEPK DQRPLGTYPD
EHFTEEAPRR SIAAFQSRLA QISRDIQERN QGLALPYTYL DPPLIENSVS I


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