LOX4_SOYBN
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 03-AUG-2022, entry version 123.
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;
CC Evidence={ECO:0000255|PROSITE-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}.
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DR EMBL; D13999; BAA03101.1; -; Genomic_DNA.
DR PIR; T07662; T07662.
DR AlphaFoldDB; P38417; -.
DR SMR; P38417; -.
DR STRING; 3847.GLYMA13G42330.1; -.
DR BindingDB; P38417; -.
DR PRIDE; 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:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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 Gene3D; 4.10.372.10; -; 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; PTHR11771; 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; 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 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 230..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
