ID   M1C4I9_SOLTU            Unreviewed;       401 AA.
AC   M1C4I9;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Phospholipase A1 {ECO:0000256|RuleBase:RU367093};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU367093};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400059647, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|Proteomes:UP000011115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400059647}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400059647};
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: Acylhydrolase that catalyzes the hydrolysis of phospholipids
CC       at the sn-1 position. {ECO:0000256|RuleBase:RU367093}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU367093}.
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DR   AlphaFoldDB; M1C4I9; -.
DR   STRING; 4113.M1C4I9; -.
DR   PaxDb; 4113-PGSC0003DMT400059647; -.
DR   EnsemblPlants; PGSC0003DMT400059647; PGSC0003DMT400059647; PGSC0003DMG400023182.
DR   Gramene; PGSC0003DMT400059647; PGSC0003DMT400059647; PGSC0003DMG400023182.
DR   Gramene; RHC02H1G0301.2.1; RHC02H1G0301.2.1; RHC02H1G0301.2.
DR   eggNOG; KOG4569; Eukaryota.
DR   HOGENOM; CLU_018841_0_0_1; -.
DR   InParanoid; M1C4I9; -.
DR   OMA; HSIYMSE; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00519; Lipase_3; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002921; Fungal_lipase-like.
DR   InterPro; IPR033556; PLA.
DR   PANTHER; PTHR31828:SF37; PHOSPHOLIPASE A1; 1.
DR   PANTHER; PTHR31828; PHOSPHOLIPASE A1-IIGAMMA; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU367093};
KW   Lipid degradation {ECO:0000256|RuleBase:RU367093};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU367093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011115}.
FT   DOMAIN          144..295
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
SQ   SEQUENCE   401 AA;  45605 MW;  2D103C89CCBCDB81 CRC64;
     MKKSTEKTDS TIAKRWMLLS GKNNWEGLMD PLNYDLRRYI IHYGEMAQAS YDNFNSNKAS
     KNAGNNRYSK NNLFTKVGLD KDHNPFKYRV TKYLYATSSI QVPEAFIVKS LSRESWSKES
     NWIGFIAVCT DEGKIALGRR EILISWRGTV QTLDWVNDLD FFQVSAPEIF RGNTDPQIHR
     GWYSIYTSED PRSPFNNTSV RDQVVEEVKR LVEEYKSEKM SITITGHSMG AAVGTLNAID
     IVVNGFNKGC LVTAILFASP RVGDSSFVNA FSKLENLRIL RVTNCLDIIP NYPLIDYSEI
     GVELAIDTTK SKYLKVPGDI RSWHSLEAHM HGVAGYQGAN GGFKLEVRRD ISLVNKHLNA
     LKDEYCVPTC WWVEKNNGMV QQDDGSWKLM DHEDDDDSVY A
//