ID   LOX14_SOLTU             Reviewed;         860 AA.
AC   Q43190;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Probable linoleate 9S-lipoxygenase 4;
DE            EC=1.13.11.58;
DE   AltName: Full=Root lipoxygenase;
GN   Name=LOX1.4; Synonyms=POTLX-2;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Superior;
RA   Kolomiets M.V., Hannapel D.J., Gladon R.J.;
RT   "Potato lipoxygenase genes expressed during the early stages of
RT   tuberization.";
RL   (er) Plant Gene Register PGR96-065(1996).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=11080289; DOI=10.1104/pp.124.3.1121;
RA   Kolomiets M.V., Chen H., Gladon R.J., Braun E.J., Hannapel D.J.;
RT   "A leaf lipoxygenase of potato induced specifically by pathogen
RT   infection.";
RL   Plant Physiol. 124:1121-1130(2000).
CC   -!- FUNCTION: Plant lipoxygenases 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. Catalyzes the
CC       hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC       structure. {ECO:0000255|PROSITE-ProRule:PRU00726}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
CC   -!- TISSUE SPECIFICITY: Expressed in tubers and roots. Not detected in
CC       leaves, flowers, stems, shoot tips, or axillary buds.
CC       {ECO:0000269|PubMed:11080289, ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR   EMBL; U60201; AAB67860.1; -; mRNA.
DR   RefSeq; NP_001305607.1; NM_001318678.1.
DR   AlphaFoldDB; Q43190; -.
DR   SMR; Q43190; -.
DR   PRIDE; Q43190; -.
DR   GeneID; 102602528; -.
DR   KEGG; sot:102602528; -.
DR   InParanoid; Q43190; -.
DR   OrthoDB; 385042at2759; -.
DR   UniPathway; UPA00382; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q43190; baseline.
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   2: Evidence at transcript level;
KW   Cytoplasm; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW   Oxylipin biosynthesis; Reference proteome.
FT   CHAIN           1..860
FT                   /note="Probable linoleate 9S-lipoxygenase 4"
FT                   /id="PRO_0000412922"
FT   DOMAIN          29..159
FT                   /note="PLAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DOMAIN          162..860
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   REGION          209..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         521
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         526
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         712
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         716
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         860
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ   SEQUENCE   860 AA;  96969 MW;  11FD0D769921053E CRC64;
     MLGQIVGGLI GGHHDSKKVK GTVVMMKKNA LDFTDLAGSL TDKIFEALGQ KVSFQLISSV
     QSDPANGLQG KHSNPAYLEN FLFTLTPLAA GETAFGVTFD WNEEFGVPGA FIIKNTHINE
     FFLKSLTLED VPNHGKVHFV CNSWVYPSFR YKSDRIFFAN QPYLPSETPE LLRKYRENEL
     LTLRGDGTGK REAWDRIYDY DVYNDLGNPD QGKENVRTTL GGSADYPYPR RGRTGRPPTR
     TDPKSESRIP LILSLDIYVP RDERFGHLKM SDFLTYALKS IVQFILPELH ALFDGTPNEF
     DSFEDVLRLY EGGIRLPQGP LFKALTDAIP LEMIRELLRT DGEGILRFPT PLVIKDSKTA
     WRTDEEFARE MLAGVNPIII SRLQEFPPKS KLDPEAYGNQ NSTITAEHIE DKLDGLTVDE
     AMNNNKLFIL NHHDVLIPYL RRINTTTTKT YASRTLLFLQ DNGSLKPLAI ELSLPHPDGD
     QFGVTSKVYT PSDQGVESSI WQLAKAYVAV NDSGVHQLIS HWLNTHAVIE PFVIATNRQL
     SVLHPIHKLL YPHFRDTMNI NAMARQILIN AGGVLESTVF PSKFAMEMSA VVYKDWVFPD
     QALPADLVKR GVAVEDSSSP HGVRLLIEDY PYAVDGLEIW SAIKSWVTDY CSFYYGSDEE
     ILKDNELQAW WKELREVGHG DKKNEPWWPE METPQELIDS CTTIIWIASA LHAAVNFGQY
     PYAGYLPNRP TVSRRFMPEP GTPEYEELKK NPDKAFLKTI TAQLQTLLGV SLIEILSRHT
     TDEIYLGQRE SPEWTKDKEP LAAFDKFGKK LTDIEKQIIQ RNGDNILINR SGPVNAPYTL
     LFPTSEGGLT GKGIPNSVSI