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Database: UniProt
Entry: D7L1P1_ARALL
LinkDB: D7L1P1_ARALL
Original site: D7L1P1_ARALL 
ID   D7L1P1_ARALL            Unreviewed;       838 AA.
AC   D7L1P1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   22-FEB-2023, entry version 75.
DE   RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE            EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN   ORFNames=ARALYDRAFT_479752 {ECO:0000313|EMBL:EFH59620.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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.
CC       {ECO:0000256|RuleBase:RU003975}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962,
CC         ECO:0000256|RuleBase:RU003974};
CC   -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC       {ECO:0000256|RuleBase:RU003975}.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family.
CC       {ECO:0000256|ARBA:ARBA00009419, ECO:0000256|RuleBase:RU003974}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR   EMBL; GL348715; EFH59620.1; -; Genomic_DNA.
DR   RefSeq; XP_002883361.1; XM_002883315.1.
DR   AlphaFoldDB; D7L1P1; -.
DR   STRING; 81972.D7L1P1; -.
DR   EnsemblPlants; fgenesh2_kg.3__2453__AT3G22400.1; fgenesh2_kg.3__2453__AT3G22400.1; fgenesh2_kg.3__2453__AT3G22400.1.
DR   Gramene; fgenesh2_kg.3__2453__AT3G22400.1; fgenesh2_kg.3__2453__AT3G22400.1; fgenesh2_kg.3__2453__AT3G22400.1.
DR   eggNOG; ENOG502QQSP; Eukaryota.
DR   HOGENOM; CLU_004282_0_0_1; -.
DR   UniPathway; UPA00382; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:EnsemblPlants.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0010311; P:lateral root formation; IEA:EnsemblPlants.
DR   GO; GO:0034440; P:lipid oxidation; IEA:EnsemblPlants.
DR   GO; GO:1900366; P:negative regulation of defense response to insect; IEA:EnsemblPlants.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01751; PLAT_LH2; 1.
DR   Gene3D; 3.10.450.60; -; 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:SF112; LINOLEATE 9S-LIPOXYGENASE 5; 1.
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   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW   ECO:0000256|RuleBase:RU003975};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003974};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|RuleBase:RU003975};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003974};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003974};
KW   Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767,
KW   ECO:0000256|RuleBase:RU003975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT   DOMAIN          12..155
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          158..838
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
FT   REGION          206..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  95692 MW;  88C211C8200D7971 CRC64;
     MEEDVKKTTM KIEGEVVVMK KNLLDFKDVM ASLLDRVHEL FGRRVSLHLI SSHQPDPANE
     KRGRLGKAAH LEKWVTKLKT SVTAEETAFR VTFDWDESMG PPAAFVIKNH HHSQFYLKSL
     TLRGFPGGEG GPIHFVCNSW IYPSHRYRSD RVFFSNKAYL PSETPELIKE LREEELQNLR
     GNEKEGEFKE WDRVYDYAYY NDLGAPDKGP DSARPVLGGS PELPYPRRGK TGRKPTKSDP
     KSESRLALLN LNIYVPRDER FSHVKFSDFL AYALKSVTQV LVPEIASMFF TSMTVVLSSP
     NGHTISKLRD VIPWEMFREL VRNDGERFLN RSAWRTDEEF AREMLAGLNP VVISRLQEFP
     PKSNLDSAKY GNQHSSIREE HIEPNMNGLN VLEALEQNKL YILDHHDALM PYLTRINSTN
     TKTYATRTLL LLQEDGTLKP LAIELSLPHA QGESHGSVSK VFTPAEKGVE GSVWQLAKAY
     AAVNDSGYHQ LISHWLQTHA VIEPFIIASN RQLSVVHPIH KLLHPHFRDT MNINALARHI
     LINSDGVLER TVFPSRYAME MSSSIYKNWV FTDQALPKDL LKRGVAVEDP KSDNGVKLLI
     DDYPFAVDGL EIWSAIKTWV TEYCTFYYKN DKTVQTDTEI QSWWTELRTK GHGDKQHESW
     WPSMQTRDDL IETCTIIIWI ASALHAAVNF GQYPYAGFLP NRPTVSRRFM PEPGTDEYAE
     LAEDADVAFL KTITPQLQTL LGISIIEILS MHSTDEIYLG QRDSPNWTAD DEPLEAFKRF
     GKELELIENN IIRRNNDKRF KNRTGPVNIP YTLLYPNTSD YTREGGLTGK GIPNSVSI
//
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