ID A0A103XWV6_CYNCS Unreviewed; 789 AA.
AC A0A103XWV6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN ORFNames=Ccrd_023425 {ECO:0000313|EMBL:KVH98361.1};
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:KVH98361.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVH98361.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVH98361.1};
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|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:KVH98361.1}.
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DR EMBL; LEKV01003801; KVH98361.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A103XWV6; -.
DR EnsemblPlants; KVH98361; KVH98361; Ccrd_023425.
DR Gramene; KVH98361; KVH98361; Ccrd_023425.
DR OMA; YHISIVF; -.
DR Proteomes; UP000243975; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; 2.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR32176:SF80; ACYL TRANSFERASE_ACYL HYDROLASE_LYSOPHOSPHOLIPASE-RELATED; 1.
DR PANTHER; PTHR32176; XYLOSE ISOMERASE; 1.
DR Pfam; PF01734; Patatin; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR PROSITE; PS51635; PNPLA; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU361262, ECO:0000313|EMBL:KVH98361.1};
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:KVH98361.1}.
FT DOMAIN 23..228
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT DOMAIN 436..648
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 789 AA; 87591 MW; EDF48C1DF2E21EEF CRC64;
MSFKEEPRSP LQPPTYGNLI TILSIDGGGV RGIIPSVILE FLESELQKLD GENARLADYF
DVMAGTSTGG LVTGMLATPN EQNRPVFAAK DVKDFYLEHC PKIFPHDDNL LAPATKVVKA
LSGPRYDGEH LHKIIEEKLQ KRRLHETLTN VVIPTFDIKY MQPMIFSSYQ KNSSLDAKLS
DICIGTSAAP TYLPSHSFQI EDSEGNLLRE FNLIDGAVAA NNPTLVAISE VTNEITRGSP
NFFPIKPTEY GRFLVLSLGT GSQKFQERYD ATKSSNWGIL GWLAGEGSTP LVDVFTQASG
DMVDYHISTV FQALHSEENY LRIQDDNLSG DLASLDLATK ENLENLVKVG EELLKKPVTR
VNLGTGITEP YYHTTNEMAL KKFAKILHHE KNVREARSPS TNKGPFNRSD SIEDRIAQEL
RSPLQPPTYG NLITILSIDG RGVRGIIPSV VLEFLESELQ ELDGENARLA DYFDVMAGTS
TGGLVTAMLT TPNEENHANV VAMNWKIVNY VIRHLKYPCF WCNICSNPLA PATKVVKALS
GPKHNGEHLH KVIREKLQER RLNEELTNVV IPTFDIKYLQ PTIFSSYELK KNPSLDAKLS
DICIRTSAAP TYLPSHSFQT EDPEGKLLRD FNLIDGGVAA NNPTLVAISE VTKEITSGSP
NFFPIKPTEY SRFLVLSMGT GSLEFQEKYD ATKSSNWGIL GWLAGGGSTP LVDVFTQASG
DMVDYHISIV FQALHSQDNY LRIQDDTLSG DLASMDLATE ENLENLVKVS EDLLKKPVNH
TIRLRTRWL
//
