LOX5_MESAU
ID LOX5_MESAU Reviewed; 673 AA.
AC P51399;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Polyunsaturated fatty acid 5-lipoxygenase {ECO:0000250|UniProtKB:P09917};
DE EC=1.13.11.- {ECO:0000250|UniProtKB:P09917};
DE AltName: Full=Arachidonate 5-lipoxygenase {ECO:0000250|UniProtKB:P09917};
DE Short=5-LO {ECO:0000303|PubMed:8951996};
DE Short=5-lipoxygenase {ECO:0000303|PubMed:8951996};
DE EC=1.13.11.34 {ECO:0000250|UniProtKB:P09917};
GN Name=ALOX5 {ECO:0000250|UniProtKB:P09917};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Syrian;
RX PubMed=8951996; DOI=10.1016/s0952-3278(96)90008-3;
RA Kitzler J.W., Eling T.E.;
RT "Cloning, sequencing and expression of a 5-lipoxygenase from Syrian hamster
RT embryo fibroblasts.";
RL Prostaglandins Leukot. Essent. Fatty Acids 55:269-277(1996).
CC -!- FUNCTION: Catalyzes the oxygenation of arachidonate to 5-
CC hydroperoxyeicosatetraenoate (5-HPETE) followed by the dehydration to
CC 5,6- epoxyeicosatetraenoate (Leukotriene A4/LTA4), the first two steps
CC in the biosynthesis of leukotrienes, which are potent mediators of
CC inflammation. Also catalyzes the oxygenation of arachidonate into 8-
CC hydroperoxyicosatetraenoate (8-HPETE) and 12-
CC hydroperoxyicosatetraenoate (12-HPETE). Displays lipoxin synthase
CC activity being able to convert (15S)-HETE into a conjugate tetraene.
CC Although arachidonate is the preferred substrate, this enzyme can also
CC metabolize oxidized fatty acids derived from arachidonate such as
CC (15S)-HETE, eicosapentaenoate (EPA) such as (18R)- and (18S)-HEPE or
CC docosahexaenoate (DHA) which lead to the formation of specialized pro-
CC resolving mediators (SPM) lipoxin and resolvins E and D respectively,
CC therefore it participates in anti-inflammatory responses (By
CC similarity). Oxidation of DHA directly inhibits endothelial cell
CC proliferation and sprouting angiogenesis via peroxisome proliferator-
CC activated receptor gamma (PPARgamma). It does not catalyze the
CC oxygenation of linoleic acid and does not convert (5S)-HETE to lipoxin
CC isomers. In addition to inflammatory processes, it participates in
CC dendritic cell migration, wound healing through an antioxidant
CC mechanism based on heme oxygenase-1 (HO-1) regulation expression,
CC monocyte adhesion to the endothelium via ITGAM expression on monocytes.
CC Moreover, it helps establish an adaptive humoral immunity by regulating
CC primary resting B cells and follicular helper T cells and participates
CC in the CD40-induced production of reactive oxygen species (ROS) after
CC CD40 ligation in B cells through interaction with PIK3R1 that bridges
CC ALOX5 with CD40. May also play a role in glucose homeostasis,
CC regulation of insulin secretion and palmitic acid-induced insulin
CC resistance via AMPK. Can regulate bone mineralization and fat cell
CC differentiation increases in induced pluripotent stem cells (By
CC similarity). {ECO:0000250|UniProtKB:P09917,
CC ECO:0000250|UniProtKB:P48999}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = H2O + leukotriene A4;
CC Xref=Rhea:RHEA:32307, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57463; EC=1.13.11.34;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32308;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=18-HEPE + O2 = (5S)-hydroperoxy-18-hydroxy-
CC (7E,9E,11Z,14Z,16E)-eicosapentaenoate; Xref=Rhea:RHEA:48860,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:90825, ChEBI:CHEBI:90826;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48861;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(18R)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + O2 =
CC (5S)-hydroperoxy-(18R)-hydroxy-(6E,8Z,11Z,14Z,16E)-eicosapentaenoate;
CC Xref=Rhea:RHEA:51968, ChEBI:CHEBI:15379, ChEBI:CHEBI:90818,
CC ChEBI:CHEBI:132218; Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51969;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(18S)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + O2 =
CC (5S)-hydroperoxy-(18S)-hydroxy-(6E,8Z,11Z,14Z,16E)-eicosapentaenoate;
CC Xref=Rhea:RHEA:50204, ChEBI:CHEBI:15379, ChEBI:CHEBI:132083,
CC ChEBI:CHEBI:132091; Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50205;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroperoxy-(18S)-hydroxy-(6E,8Z,11Z,14Z,16E)-
CC eicosapentaenoate = (5S,6S)-epoxy-(18S)-hydroxy-(7E,9E,11Z,14Z,16E)-
CC eicosapentaenoate + H2O; Xref=Rhea:RHEA:39107, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:132091, ChEBI:CHEBI:134661;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39108;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroperoxy-(18R)-hydroxy-(6E,8Z,11Z,14Z,16E)-
CC eicosapentaenoate = (5S,6S)-epoxy-(18R)-hydroxy-(7E,9E,11Z,14Z,16E)-
CC eicosapentaenoate + H2O; Xref=Rhea:RHEA:50268, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:132218, ChEBI:CHEBI:132219;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50269;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroperoxy-18-hydroxy-(7E,9E,11Z,14Z,16E)-
CC eicosapentaenoate = (5S,6S)-epoxy-18-hydroxy-(7E,9E,11Z,14Z,16E)-
CC eicosapentaenoate + H2O; Xref=Rhea:RHEA:50844, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:90826, ChEBI:CHEBI:133812;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50845;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (5S)-hydroperoxy-
CC (6E,8Z,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:17485,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57450;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17486;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate + O2 = (5S)-
CC hydroperoxy-(15S)-hydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate;
CC Xref=Rhea:RHEA:48624, ChEBI:CHEBI:15379, ChEBI:CHEBI:57409,
CC ChEBI:CHEBI:131564; Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48625;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = H2O +
CC leukotriene A4; Xref=Rhea:RHEA:17961, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57450, ChEBI:CHEBI:57463;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17962;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (8S)-hydroperoxy-
CC (5Z,9E,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:38675,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:75322;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38676;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12S)-hydroperoxy-
CC (5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:10428,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57444;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10429;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z)-eicosadienoate + O2 = (5S)-hydroperoxy-(6E,8Z)-
CC eicosadienoate; Xref=Rhea:RHEA:62644, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:145835, ChEBI:CHEBI:145836;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + O2 = (5S)-
CC hydroperoxy-(12S)-hydroxy-(6E,8Z,10E,14Z)-eicosatetraenoate;
CC Xref=Rhea:RHEA:62648, ChEBI:CHEBI:15379, ChEBI:CHEBI:90680,
CC ChEBI:CHEBI:145837; Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 = 5-hydroperoxy-
CC (6E,8Z,11Z,14Z,17Z)-eicosapentaenoate; Xref=Rhea:RHEA:62600,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:58562, ChEBI:CHEBI:145815;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62601;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (14S)-
CC hydroperoxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate;
CC Xref=Rhea:RHEA:41332, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:78048; Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41333;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (7S)-
CC hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoate;
CC Xref=Rhea:RHEA:64668, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:156049; Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64669;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (17S)-
CC hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate;
CC Xref=Rhea:RHEA:50840, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:133795; Evidence={ECO:0000250|UniProtKB:P09917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50841;
CC Evidence={ECO:0000250|UniProtKB:P09917};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:P09917,
CC ECO:0000255|PROSITE-ProRule:PRU00726};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:P09917,
CC ECO:0000255|PROSITE-ProRule:PRU00726};
CC -!- PATHWAY: Lipid metabolism; leukotriene A4 biosynthesis.
CC {ECO:0000250|UniProtKB:P09917}.
CC -!- SUBUNIT: Homodimer. Interacts with ALOX5AP and LTC4S. Interacts with
CC COTL1, the interaction is required for stability and efficient
CC catalytic activity. Interacts with PIK3R1; this interaction bridges
CC ALOX5 with CD40 after CD40 ligation in B cells and leads to the
CC production of reactive oxygen species (ROS). Interacts (via PLAT
CC domain) with DICER1 (via Dicer dsRNA-binding fold domain); this
CC interaction enhances arachidonate 5-lipoxygenase activity and modifies
CC the miRNA precursor processing activity of DICER1.
CC {ECO:0000250|UniProtKB:P09917}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P09917,
CC ECO:0000250|UniProtKB:P48999}. Nucleus matrix
CC {ECO:0000250|UniProtKB:P09917}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P09917}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P09917}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P09917}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P09917}. Nucleus envelope
CC {ECO:0000250|UniProtKB:P09917}. Nucleus intermembrane space
CC {ECO:0000250|UniProtKB:P09917}. Note=Shuttles between cytoplasm and
CC nucleus. Found exclusively in the nucleus, when phosphorylated on Ser-
CC 272. Calcium binding promotes translocation from the cytosol and the
CC nuclear matrix to the nuclear envelope and membrane association.
CC {ECO:0000250|UniProtKB:P09917}.
CC -!- PTM: Serine phosphorylation by MAPKAPK2 is stimulated by arachidonic
CC acid. Phosphorylation on Ser-523 by PKA has an inhibitory effect.
CC Phosphorylation on Ser-271 prevents export from the nucleus.
CC Phosphorylation at Ser-523 is stimulated by 8-bromo-3',5'-cyclic AMP or
CC prostaglandin E2. {ECO:0000250|UniProtKB:P09917}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; U43333; AAA85257.1; -; mRNA.
DR RefSeq; NP_001268516.1; NM_001281587.1.
DR AlphaFoldDB; P51399; -.
DR SMR; P51399; -.
DR STRING; 10036.XP_005066151.1; -.
DR GeneID; 101839970; -.
DR CTD; 240; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR OrthoDB; 385042at2759; -.
DR UniPathway; UPA00877; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005641; C:nuclear envelope lumen; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0004052; F:arachidonate 12(S)-lipoxygenase activity; IEA:RHEA.
DR GO; GO:0004051; F:arachidonate 5-lipoxygenase activity; ISS:UniProtKB.
DR GO; GO:0036403; F:arachidonate 8(S)-lipoxygenase activity; IEA:RHEA.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0036336; P:dendritic cell migration; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0006959; P:humoral immune response; ISS:UniProtKB.
DR GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:1901753; P:leukotriene A4 biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019370; P:leukotriene biosynthetic process; ISS:UniProtKB.
DR GO; GO:2001301; P:lipoxin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0061044; P:negative regulation of vascular wound healing; ISS:UniProtKB.
DR GO; GO:0061045; P:negative regulation of wound healing; ISS:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:1904999; P:positive regulation of leukocyte adhesion to arterial endothelial cell; ISS:UniProtKB.
DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0045598; P:regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0106014; P:regulation of inflammatory response to wounding; ISS:UniProtKB.
DR GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR CDD; cd01753; PLAT_LOX; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001885; LipOase_mml.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR042062; PLAT_LOX_verte.
DR PANTHER; PTHR11771; PTHR11771; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00467; MAMLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF48484; SSF48484; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Dioxygenase; Hydrolase; Iron; Leukotriene biosynthesis;
KW Lipid metabolism; Membrane; Metal-binding; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..673
FT /note="Polyunsaturated fatty acid 5-lipoxygenase"
FT /id="PRO_0000220694"
FT DOMAIN 2..117
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 118..673
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 17
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P09917,
FT ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 372
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P09917,
FT ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 550
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P09917,
FT ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 554
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P09917,
FT ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 673
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P09917,
FT ECO:0000255|PROSITE-ProRule:PRU00726"
FT SITE 103
FT /note="Essential for stabilizing binding to COTL1"
FT /evidence="ECO:0000250"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09917"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09917"
SQ SEQUENCE 673 AA; 77873 MW; A7AF63B11CDC7972 CRC64;
MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGA VDSYDVTVDE
ELGEIQLVRI EKRKYWLHDD WYLKYITLKT PTDYIEFPCY RWITGEGEIV LRDGRAKLAR
DDQIHILKQH RRKELEARQK QYRWMEWNPG FPLSIDAKCH KDLPRDIQFD SEKGVDFVLN
YSKAMENLFI NRFMHMFQSS WNDFADFEKI FVKISNTISE RVKNHWQEDL MFGYQFLNGC
NPVLIKRCRE LPQKLPVTTE MVECSLERHL SLEQEVQEGN IFIVDYELLD GIDANKTDPC
THQFLAAPIC LLYKNLANKI VPIAIQLNQA PGEKNPIFLP SDAKYDWLLA KIWVRSSDFH
VHQTITHLLC THLVSEVFGI AMYRQLPAVH PIFKLLVAHV RFTIAINTKA REQLICEYGL
FDKANATGGG GHVQMVQRAV QDLTYSSLCF PEAIKARGMD STEDIPYYFY RDDGLLVWEA
IQSFTSEVVS IYYEDDQVVM EDQELQDFVK DVYVYGMRGR KASGFPKSIK SREKLSEYLT
VVIFTASAQH AAVNFGQYDW CSWIPNAPPT MRAPPATAKG VVTIEQIVAT LPDRGRSCWH
LGAVWALSQF QENELFLGMY PEEHFIEKPV KEAMTRFRKN LEAIVNVIAE RNKNKKLPYY
YLSPDRIPNS VAI
