ID A0A0D3DEW4_BRAOL Unreviewed; 434 AA.
AC A0A0D3DEW4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Phospholipase A1 {ECO:0000256|RuleBase:RU367093};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU367093};
GN Name=106305495 {ECO:0000313|EnsemblPlants:Bo7g106120.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo7g106120.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo7g106120.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo7g106120.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-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}.
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 RefSeq; XP_013597314.1; XM_013741860.1.
DR AlphaFoldDB; A0A0D3DEW4; -.
DR STRING; 109376.A0A0D3DEW4; -.
DR EnsemblPlants; Bo7g106120.1; Bo7g106120.1; Bo7g106120.
DR GeneID; 106305495; -.
DR Gramene; Bo7g106120.1; Bo7g106120.1; Bo7g106120.
DR KEGG; boe:106305495; -.
DR eggNOG; KOG4569; Eukaryota.
DR HOGENOM; CLU_018841_0_0_1; -.
DR OMA; WKLLDHE; -.
DR OrthoDB; 1210884at2759; -.
DR Proteomes; UP000032141; Chromosome C7.
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; PHOSPHOLIPASE A1-IIGAMMA; 1.
DR PANTHER; PTHR31828:SF1; 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:UP000032141}.
FT DOMAIN 165..325
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
SQ SEQUENCE 434 AA; 49499 MW; 83EB133D0BC1DADB CRC64;
MDEEDKKVTK CFSFKRTTKK KKKEEEKLIV STEIAKRWRD LSGQNHWKGM LQPLDQDLRE
YIIHYGEMAQ AGYDTFNINT ESKFAGSSIY SRKDFFAKVG LEKAHPYTKY KVTKFLYATS
QIHVPESFLL FPLSREGWTK ESNWMGYVAV TDDQGTAVLG RRDIVVAWRG SVQPLEWVND
FEFGLVNAKN IFGEKNDQVQ IHQGWYSIYM SEDERSPFNK ANARDQVLRE IGRLLEKYKD
EEVSISICGH SLGAALATLN ATDIVANGYN RPKSRPGKSC PVTAFVFASP RVGDSDYRKL
FSGLEDLRVL RVKNLPDIVP IYPPLGYAEV GEELSIDTRK SQYMKSPGNF ATFHCLESYL
HGVAGTQGTS KNDIFRLDVK RDIGLVNKSV DGLTDECMVP GNWRVLKNKG MVQQDDGSWV
LLDHEIDDNE DFEF
//
