LPAT2_BRANA
ID LPAT2_BRANA Reviewed; 390 AA.
AC Q9XFW4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 64.
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 napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Silique;
RA Graefin zu Muenster A., Wolter F.P., Frentzen M.;
RT "A cDNA encoding a microsomal 1-acylglycerol-3-phosphate acyltransferase of
RT Brassica napus L.";
RL Submitted (MAY-1997) 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; Z95637; CAB09138.1; -; mRNA.
DR AlphaFoldDB; Q9XFW4; -.
DR BRENDA; 2.3.1.51; 944.
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..390
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase 2"
FT /id="PRO_0000208180"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 358..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 91..96
FT /note="HXXXXD motif"
SQ SEQUENCE 390 AA; 43771 MW; F1446E1B30009C37 CRC64;
MAMAAAVIVP LGILFFISGL VVNLLQAVCY VLVRPMSKNT YRKINRVVAE TLWLELVWIV
DWWAGVKIQV FADDETFNRM GKEHALVVCN HRSDIDWLVG WILAQRSGCL GSALAVMKKS
SKFLPVIGWS MWFSEYLFLE RNWAKDESTL QSGLQRLNDF PRPFWLALFV EGTRFTEAKL
KAAQEYAASS ELPVPRNVLI PRTKGFVSAV SNMRSFVPAI YDMTVAIPKT SPPPTMLRLF
KGQPSVVHVH IKCHSMKDLP EPEDEIAQWC RDQFVAKDAL LDKHIAADTF PGQKEQNIGR
PIKSLAVVVS WACLLTLGAM KFLHWSNLFS SWKGIALSAF GLGIITLCMQ ILIRSSQSER
STPAKVAPAK PKDNHQSGPS SQTEVEEKQK
