ID A0A3S3PGE7_9MAGN Unreviewed; 368 AA.
AC A0A3S3PGE7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN ORFNames=CKAN_01912400 {ECO:0000313|EMBL:RWR90046.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR90046.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR90046.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR90046.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(2019).
CC -!- FUNCTION: Lipolytic acyl hydrolase (LAH).
CC {ECO:0000256|RuleBase:RU361262}.
CC -!- DOMAIN: The nitrogen atoms of the two glycine residues in the GGXR
CC motif define the oxyanion hole, and stabilize the oxyanion that forms
CC during the nucleophilic attack by the catalytic serine during substrate
CC cleavage. {ECO:0000256|RuleBase:RU361262}.
CC -!- SIMILARITY: Belongs to the patatin family.
CC {ECO:0000256|ARBA:ARBA00010240, ECO:0000256|RuleBase:RU361262}.
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:RWR90046.1}.
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DR EMBL; QPKB01000008; RWR90046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3PGE7; -.
DR STRING; 337451.A0A3S3PGE7; -.
DR Proteomes; UP000283530; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07214; Pat17_isozyme_like; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR32176:SF92; PATATIN-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR32176; XYLOSE ISOMERASE; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU361262};
KW Lipid degradation {ECO:0000256|RuleBase:RU361262};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361262};
KW Reference proteome {ECO:0000313|Proteomes:UP000283530}.
FT DOMAIN 1..185
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 349..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 40570 MW; 80A1733885CA38B5 CRC64;
MEQELDGQDA RLADYFDVIA GTSTGGLITA MLTAPNENKR PLFAAKDIKD FYLEHCPKIF
PQCRGPFAPA MKLFKAISGP TYNGKYLRAL VEKKLGTTLL KETLTNVIIP AFDIKKLQPT
IFSSREVESK PYLNALLSDI CIGTSAAPTY LPAHHFKTEY SGGEEMRFDL IDGGVAANNP
ALIALSEVTK ESFRGNLDRF QNKPVDCGRC LVISLGTGSP KKHEKYTASH ASKWGLFGWF
HSGGSTPLVD VFTKASAEMV DIHISVAFQA LHSECNYLRI QDDTLSGSIS SVDIATKENL
KNLVKAGEQL LKKTVSRVNL DTGIYEPVEN AETNEVALKR FAKKLSDEKR LRKMRSPPVK
TLKSMDTS
//
