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Database: UniProt
Entry: A0A498K7G9_MALDO
LinkDB: A0A498K7G9_MALDO
Original site: A0A498K7G9_MALDO 
ID   A0A498K7G9_MALDO        Unreviewed;       260 AA.
AC   A0A498K7G9;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=PLAT domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DVH24_015194 {ECO:0000313|EMBL:RXI01845.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXI01845.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXI01845.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXI01845.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family.
CC       {ECO:0000256|ARBA:ARBA00009419}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RXI01845.1}.
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DR   EMBL; RDQH01000330; RXI01845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498K7G9; -.
DR   STRING; 3750.A0A498K7G9; -.
DR   Proteomes; UP000290289; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0034440; P:lipid oxidation; IEA:InterPro.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01751; PLAT_LH2; 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; IPR001246; LipOase_plant.
DR   InterPro; IPR042057; Lipoxy_PLAT/LH2.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   PANTHER; PTHR11771:SF126; LINOLEATE 9S-LIPOXYGENASE 1; 1.
DR   PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR   Pfam; PF00305; Lipoxygenase; 1.
DR   Pfam; PF01477; PLAT; 1.
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; PS51393; LIPOXYGENASE_3; 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289}.
FT   DOMAIN          56..177
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          180..260
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
FT   REGION          238..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   260 AA;  29556 MW;  CDB07982F95A7DEF CRC64;
     MLQNIVEKLT GHQQNENHGK INGTVVLMKK NVLDFNDFNA SVLDRVHELV GQRVSLQLIS
     AVHADDSGEF IFSLQDYTVS VHENGLKGKL GQPAYLEDWI TTITPLTAGE SAFKVTFDYE
     EEVGVPGAFL IKNNHHSEFF LKTVTLENVP GEGRVHFVCN SWVYPTEKYT KDRVFFVNKT
     YLPSETPLPL RKYIEEELVH LRGDGKGELQ EWERVYDYAY YNDLGKPDKG AKYVRPILGG
     SSEYPYPRRG RTGRPPTKTG
//
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