ID A0A118K2V1_CYNCS Unreviewed; 455 AA.
AC A0A118K2V1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, 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=Ccrd_016721 {ECO:0000313|EMBL:KVI04953.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVI04953.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVI04953.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVI04953.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
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|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:KVI04953.1}.
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DR EMBL; LEKV01001894; KVI04953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A118K2V1; -.
DR EnsemblPlants; KVI04953; KVI04953; Ccrd_016721.
DR Gramene; KVI04953; KVI04953; Ccrd_016721.
DR OMA; PCKPSID; -.
DR OrthoDB; 518048at2759; -.
DR Proteomes; UP000243975; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd07199; Pat17_PNPLA8_PNPLA9_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; PTHR32241:SF23; PATATIN; 1.
DR PANTHER; PTHR32241; PATATIN-LIKE PROTEIN 6; 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, ECO:0000313|EMBL:KVI04953.1};
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:UP000243975};
KW Transferase {ECO:0000313|EMBL:KVI04953.1}.
FT DOMAIN 74..289
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 455 AA; 49408 MW; 56071229E8AF3BAA CRC64;
MDSNRESSEE PSIVTDKLSY EIFSILESKF LFGYNDPKLW KPKQVSPEIS VTPTQSDDGG
VLSMKNQRGK ICLLSIDGGG MRGILAGKAL AQFEKALKAK SGNPNARIAD YIDVAAGTGV
GGVFTAMLFG SKSQRVPIFK AEETWRFLAE QGKRLYHQKS SSAGGGGGGG GLWKRLFRGG
GGISHATTAF ENAMKEAFEV NGRSLTLKDT LKPVLIPCYD LSSSAPFLFS RADALETDSF
DFRLWEVCRA TSAEPDLFEP VSMKSIDGKT RCVAVDGGLA MSNPTAAAIT HVIHNKQEFP
FVRGVEDLLV LSLGTGQLLE GNYDYDQVKG WKAKDWARPM ARISGDSSAD MVDHAVAMAF
GQSRCSNYVR IQANSSNMDG SRVNVDSDAN VKALMGIGEE MLRQKNVESV LFGGKKIGEE
TNLEKLEWFA GEVVLEHERR SGRIAPTVAF KQPTS
//
