ID A0A2G5E4G4_AQUCA Unreviewed; 398 AA.
AC A0A2G5E4G4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN ORFNames=AQUCO_01200095v1 {ECO:0000313|EMBL:PIA50644.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA50644.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA50644.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ305029; PIA50644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5E4G4; -.
DR InParanoid; A0A2G5E4G4; -.
DR OrthoDB; 1079044at2759; -.
DR Proteomes; UP000230069; 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 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:UP000230069}.
FT DOMAIN 20..227
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 398 AA; 44242 MW; 817C37B280AD3043 CRC64;
MDRTSSFSKF PTYEKFYTIL SIDGGGIRGI IPGTILAFLE SELQKLDGED ARLADYFDLI
AGTSTGGLVT TMLTAPDEYG RPLYAAKDLT KFYLENCPKI FPQRSGFLSS IRKTFASAMG
PAYNGVYLRD LLKDKLKDKL LSQTLTNVAI PTFDIKLLQP IIFSNFQLTT DPTLDAQLLD
ICIGTSAAPT YLPAYCFKNI DKDGNIIRKF DLVDGGVTAN NPTMVAVTEM TQQIYNKDPD
YLSHKPMDYG KFLVISLGTG SRKIEVKKYN AKMAAKWGLW GWLTAGGSNP LIDVFTQSSE
DLVDYHLSVV FKALKSEPNY IRIQDYDLTA KQSSTDLATT ENLKDLVKVG EDLLKKKVTR
VNLETGGTKD CESGDTNEEA LIKFAKLLSD ERNCRKMN
//
