ID I0Z3U4_COCSC Unreviewed; 297 AA.
AC I0Z3U4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN ORFNames=COCSUDRAFT_65188 {ECO:0000313|EMBL:EIE25313.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE25313.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE25313.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE25313.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
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:EIE25313.1}.
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DR EMBL; AGSI01000004; EIE25313.1; -; Genomic_DNA.
DR RefSeq; XP_005649857.1; XM_005649800.1.
DR AlphaFoldDB; I0Z3U4; -.
DR STRING; 574566.I0Z3U4; -.
DR GeneID; 17043315; -.
DR KEGG; csl:COCSUDRAFT_65188; -.
DR eggNOG; KOG3773; Eukaryota.
DR OrthoDB; 318378at2759; -.
DR Proteomes; UP000007264; 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; cd07224; Pat_like; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR033562; PLPL.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR12406; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2 IPLA2 -RELATED; 1.
DR PANTHER; PTHR12406:SF7; PATATIN-LIKE PHOSPHOLIPASE DOMAIN-CONTAINING PROTEIN 4; 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:UP000007264}.
FT DOMAIN 60..224
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 297 AA; 32779 MW; D39EFDA9B4CB7A61 CRC64;
MKFLVDRRLL AQAVNPFPAC RSRKRFHFRP RAAPLDVATS QERQQCSIVA EAHKRGTLGF
GFSAGGLLFP YYLGIVQTLR ELNIITDTTP LAGASAGSLI AACHHSGLPP EQVKEACFVL
ADNCRRKGTR GRLGSVLSQF LHDLLPQDVH ERCNNKAFVA VTRAWPRPQG ELISQFHSRE
DLIEALLTSC HIPWWFEGTL GRNFRGALHF DGGLTNFCPA VTAPGILTQR VTCFPAARLR
RAINIAISPP EQYDLNVLLG WAFQPAEEAV LEAFLEQGRR DALAWAEANG VASKAVE
//
