ID LOX4_SOYBN Reviewed; 853 AA. AC P38417; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 04-NOV-2026, entry version 134. DE RecName: Full=Linoleate 9S-lipoxygenase-4; DE EC=1.13.11.58; DE AltName: Full=Lipoxygenase-4; DE Short=L-4; DE AltName: Full=VSP94; GN Name=LOX1.5; Synonyms=LOX4; OS Glycine max (Soybean) (Glycine hispida). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine; OC Glycine subgen. Soja. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Enrei; RA Kato T., Shirano Y., Iwamoto H., Shibata D.; RT "Soybean lipoxygenase L-4, a major component of the 94-kilodalton storage RT protein in vegetative tissues: expression and accumulation in leaves RT induced by pod removal and by methyl jasmonate."; RL Plant Cell Physiol. 34:1063-1072(1993). RN [2] RP PARTIAL PROTEIN SEQUENCE. RC TISSUE=Cotyledon; RX PubMed=16668631; DOI=10.1104/pp.98.1.324; RA Kato T., Ohta H., Tanaka K., Shibata D.; RT "Appearance of new lipoxygenases in soybean cotyledons after germination RT and evidence for expression of a major new lipoxygenase gene."; RL Plant Physiol. 98:324-330(1992). CC -!- FUNCTION: Plant lipoxygenase may be involved in a number of diverse CC aspects of plant physiology including growth and development, pest CC resistance, and senescence or responses to wounding. It catalyzes the CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene CC structure. CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)- CC octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00726}; CC Note=Binds 1 Fe cation per subunit. Iron is tightly bound. CC {ECO:0000255|PROSITE-ProRule:PRU00726}; CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE- CC ProRule:PRU00726}. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Found in maturing and developing seeds. In young CC seedlings it is found in cotyledons, hypocotyls, roots and primary CC leaves. CC -!- DEVELOPMENTAL STAGE: Developmentally regulated. Expression is high 3 to CC 5 days after germination and returns to basal level by day 9. CC -!- INDUCTION: By pod removal and methyl jasmonate. CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D13999; BAA03101.1; -; Genomic_DNA. DR PIR; T07662; T07662. DR AlphaFoldDB; P38417; -. DR SMR; P38417; -. DR STRING; 3847.P38417; -. DR BindingDB; P38417; -. DR PaxDb; 3847-P38417; -. DR ProMEX; P38417; -. DR eggNOG; ENOG502QQSP; Eukaryota. DR InParanoid; P38417; -. DR UniPathway; UPA00382; -. DR Proteomes; UP000008827; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-ARBA. DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central. DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central. DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01751; PLAT_LH2; 1. DR FunFam; 1.20.245.10:FF:000002; Lipoxygenase; 1. DR FunFam; 3.10.450.60:FF:000002; Lipoxygenase; 1. DR FunFam; 4.10.375.10:FF:000001; Lipoxygenase; 1. DR Gene3D; 3.10.450.60; -; 1. DR Gene3D; 4.10.375.10; Lipoxygenase-1, Domain 2; 1. DR Gene3D; 4.10.372.10; Lipoxygenase-1, Domain 3; 1. DR Gene3D; 1.20.245.10; Lipoxygenase-1, Domain 5; 1. DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 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; IPR001246; LipOase_plant. DR InterPro; IPR042057; Lipoxy_PLAT/LH2. DR InterPro; IPR027433; Lipoxygenase_dom_3. DR InterPro; IPR001024; PLAT/LH2_dom. DR InterPro; IPR036392; PLAT/LH2_dom_sf. DR PANTHER; PTHR11771; LIPOXYGENASE; 1. DR Pfam; PF00305; Lipoxygenase; 1. DR Pfam; PF01477; PLAT; 1. DR PRINTS; PR00087; LIPOXYGENASE. DR PRINTS; PR00468; PLTLPOXGNASE. DR SMART; SM00308; LH2; 1. DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1. DR SUPFAM; SSF48484; Lipoxigenase; 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 1: Evidence at protein level; KW Cytoplasm; Dioxygenase; Direct protein sequencing; Fatty acid biosynthesis; KW Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism; KW Metal-binding; Oxidoreductase; Oxylipin biosynthesis; Reference proteome. FT CHAIN 1..853 FT /note="Linoleate 9S-lipoxygenase-4" FT /id="PRO_0000220720" FT DOMAIN 34..159 FT /note="PLAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152" FT DOMAIN 162..853 FT /note="Lipoxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT REGION 213..250 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 228..250 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 513 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 518 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 704 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 708 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 853 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" SQ SEQUENCE 853 AA; 96535 MW; 533175EE1CFB34FC CRC64; MFPFGQKGQK IKGTMVVMQK NVLDINSITS VGGIVDQGLG FIGSAVDALT FAATKISIQL ISATKADGGK GKIGKSTNLR GKITLPTLGA GEQAYDVNFE WDSDFGIPGA FYIKNFMQNE FYLKSLILED IPNHGTIHFV CNSWVYNSKN YKTDRIFFAN NTYLPSETPA PLLKYREEEL KNVRGDGTGE RKEWDRIYDY DVYNDLGNPD SGDKYARPVL GGSALPYPRR ERTGRGKTRK DPNSEKPSDF VYLPRDEAFG HLKSSDFLAY GIKSVSQDVL PVLTDAFDGN ILSLEFDNFA EVHKLYEGGV TLPTNFLSKI APIPVIKEIF RTDGEQFLKY PPPKVMQVDK SAWMTDEEFA RETIAGLNPN VIKIIEEFPL SSKLDTQAYG DHTCIIAKEH LEPNLGGLTV EQAIQNKKLF ILDHHDYLIP YLRKINANTT KTYATRTIFF LKDDGTLTPL AIELSKPHPQ GEEYGPVSEV YVPASEGVEA YIWLLAKAYV VVNDACYHQI ISHWLSTHAI VEPFVIATNR QLSVVHPIYK LLFPHYRDTM NINSLARKAL VNADGIIEKT FLWGRYSMEM SAVIYKDWVF TDQALPNDLV KRGVAVKDPS APHGVRLLIE DYPYASDGLE IWDAIKSWVQ EYVSFYYKSD EELQKDPELQ AWWKELVEVG HGDLKDKPWW QKMQTREELV EASAILIWIA SALHAAVNFG QYPYGGLILN RPTISRRFMP EKGSPEYDAL AKNPEKEFLK TITGKKETLI DLTVIEILSR HASDEFYLGQ RDGGDYWTSD AGPLEAFKRF GKKLEEIEKK LIEKNKDETL RNRYGPAKMP YTLLYPSSEE GLTFRGIPNS ISI //