LPAT2_BRAOL
ID LPAT2_BRAOL Reviewed; 391 AA.
AC Q6IWY1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase 2;
DE EC=2.3.1.51;
DE AltName: Full=Lysophosphatidyl acyltransferase 2;
GN Name=LPAT2; Synonyms=LPAAT2;
OS Brassica oleracea (Wild cabbage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3712;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mietkiewska E., Brost J.M., Wang S., Giblin E.M., Pedersen K., Taylor D.C.;
RT "Isolation of 1-acylglycerol-3-phosphate acyltransferase cDNA from Brassica
RT oleracea embryo.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; AY616009; AAT36638.1; -; mRNA.
DR AlphaFoldDB; Q6IWY1; -.
DR UniPathway; UPA00557; UER00613.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..391
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase 2"
FT /id="PRO_0000208181"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 358..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 92..97
FT /note="HXXXXD motif"
FT COMPBIAS 367..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 43796 MW; 681D3F379BB398AF CRC64;
MAMAAAAVIV PLGILFFISG LVVNLLQAVC YVLIRPLSKN TYRKINRVVA ETLWLELVWI
VDWWAGVKIQ VFADDETFNR MGKEHALVVC NHRSDIDWLV GWILAQRSGC LGSALAVMKK
SSKFLPVIGW SMWFSEYLFL ERNWAKDEST LKSGLQRLND FPRPFWLALF VEGTRFTEAK
LKAAQEYAAT SQLPVPRNVL IPRTKGFVSA VSNMRSFVPA IYDMTVAIPK TSPPPTMLRL
FKGQPSVVHV HIKCHSMKDL PESEDEIAQW CRDQFVAKDA LLDKHIAADT FPGQKEQNID
RPIKSLAVVV SWACLLTLGA MKFLHWSNLF SSLKGIALSA LGLGIITLCM QILIRSSQSE
RSTPAKVAPA KPKDKHQSGS SSQTEVEEKQ K
