ID A0A165XYK0_DAUCS Unreviewed; 499 AA.
AC A0A165XYK0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=DCAR_013970 {ECO:0000313|EMBL:KZM98668.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM98668.1};
RN [1] {ECO:0000313|EMBL:KZM98668.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM98668.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937}.
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:KZM98668.1}.
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DR EMBL; LNRQ01000004; KZM98668.1; -; Genomic_DNA.
DR RefSeq; XP_017243856.1; XM_017388367.1.
DR AlphaFoldDB; A0A165XYK0; -.
DR STRING; 79200.A0A165XYK0; -.
DR EnsemblPlants; KZM98668; KZM98668; DCAR_013970.
DR GeneID; 108215793; -.
DR Gramene; KZM98668; KZM98668; DCAR_013970.
DR KEGG; dcr:108215793; -.
DR OMA; VAMSNRM; -.
DR OrthoDB; 383266at2759; -.
DR Proteomes; UP000077755; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR CDD; cd06551; LPLAT; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.20.1440.100; SG protein - dephosphorylation function; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR15486; ANCIENT UBIQUITOUS PROTEIN; 1.
DR PANTHER; PTHR15486:SF25; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE RAM2; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF12710; HAD; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077755};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 310..411
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 499 AA; 54899 MW; BFC5A9C6D7CB0D9A CRC64;
MDKQEESCSS FDFPTIDQCE SIGRDKQTVV ADMDGTLIRG RSSFPYFALV AFEVGGALRL
LFLLLASPLA GLLYYNISES AGIQVLIFAT FCGMKVSEIE AVARAVLPKF YSADLHPESW
RVFSSCGTRY VLTANPRIMV EGFLKEYLGA DVVLGTEIET FRGRATGFLT SPGVLVGKNK
ALALQKAFSD TGAPDIGLGD RKTDFPFMKL CKESYVVPAH PQVEAVTHDK LPKPIIFHDG
RLVKKPTPLT ALLILFWIPV GFILACMRIA AGALLPMSLV YYAFRALGVR VTIKGTPPPT
AQNSTNQTGN LFICSHRTLL DPIFLSAALG RPIPAVTYSL SRLSEIISPI KTVRLSRDRV
TDASMIKKLL QKGDLVLCPE GTTCREPFLL RFSALFAELT DELVPVAMSN RMSMFHGTTA
RGWKGMDPFY FFMNPSPAYE VTFLNKLPKE LTCGTGQSSH VVANYIQRTI ASTLSYECTN
FTRKDKYRAL AGNDGIVAR
//
