ID   PLSC_COCNU              Reviewed;         308 AA.
AC   Q42670;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase;
DE            Short=1-AGP acyltransferase;
DE            Short=1-AGPAT;
DE            EC=2.3.1.51;
DE   AltName: Full=Lysophosphatidic acid acyltransferase;
DE            Short=LPAAT;
OS   Cocos nucifera (Coconut palm).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Arecaceae; Arecoideae; Cocoseae;
OC   Attaleinae; Cocos.
OX   NCBI_TaxID=13894;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Endosperm;
RX   PubMed=8552723; DOI=10.1104/pp.109.3.999;
RA   Knutzon D.S., Lardizabal K.D., Nelsen J.S., Bleibaum J.L., Davies H.M.,
RA   Metz J.G.;
RT   "Cloning of a coconut endosperm cDNA encoding a 1-acyl-sn-glycerol-3-
RT   phosphate acyltransferase that accepts medium-chain-length substrates.";
RL   Plant Physiol. 109:999-1006(1995).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC       by incorporating acyl moiety at the 2 position. This enzyme shows a
CC       preference for medium-chain-length fatty acyl-coenzyme a substrates.
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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; U29657; AAC49119.1; -; mRNA.
DR   AlphaFoldDB; Q42670; -.
DR   SMR; Q42670; -.
DR   BRENDA; 2.3.1.51; 1556.
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:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004552; AGP_acyltrans.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Direct protein sequencing; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..308
FT                   /note="1-acyl-sn-glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000208185"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           130..135
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   308 AA;  34809 MW;  3773CF8C03C3C0FE CRC64;
     MDASGASSFL RGRCLESCFK ASFGMSQPKD AAGQPSRRPA DADDFVDDDR WITVILSVVR
     IAACFLSMMV TTIVWNMIML ILLPWPYARI RQGNLYGHVT GRMLMWILGN PITIEGSEFS
     NTRAIYICNH ASLVDIFLIM WLIPKGTVTI AKKEIIWYPL FGQLYVLANH QRIDRSNPSA
     AIESIKEVAR AVVKKNLSLI IFPEGTRSKT GRLLPFKKGF IHIALQTRLP IVPMVLTGTH
     LAWRKNSLRV RPAPITVKYF SPIKTDDWEE EKINHYVEMI HALYVDHLPE SQKPLVSKGR
     DASGRSNS