LPCT4_XENLA
ID LPCT4_XENLA Reviewed; 522 AA.
AC Q6DCK1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Lysophospholipid acyltransferase LPCAT4;
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 7;
DE Short=1-AGP acyltransferase 7;
DE Short=1-AGPAT 7;
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23;
DE AltName: Full=1-acylglycerophosphoserine O-acyltransferase;
DE EC=2.3.1.n6;
DE AltName: Full=1-alkenylglycerophosphoethanolamine O-acyltransferase;
DE EC=2.3.1.121;
DE AltName: Full=1-alkylglycerophosphocholine O-acetyltransferase;
DE EC=2.3.1.67;
DE AltName: Full=Acyltransferase-like 3;
DE AltName: Full=Lysophosphatidylcholine acyltransferase 4;
DE AltName: Full=Lysophosphatidylethanolamine acyltransferase 2;
DE EC=2.3.1.n7;
GN Name=lpcat4; Synonyms=agpat7, aytl3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Displays acyl-CoA-dependent lysophospholipid acyltransferase
CC activity with a subset of lysophospholipids as substrates. Prefers long
CC chain acyl-CoAs (C16, C18) as acyl donors (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + an acyl-
CC CoA = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:16245, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:77288, ChEBI:CHEBI:77290; EC=2.3.1.121;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-sn-glycero-3-phosphocholine + acetyl-CoA = a 1-O-
CC alkyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:18461, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.67;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:33191,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64379; EC=2.3.1.n6;
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH78014.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC078014; AAH78014.1; ALT_INIT; mRNA.
DR RefSeq; NP_001153513.1; NM_001160041.1.
DR AlphaFoldDB; Q6DCK1; -.
DR SMR; Q6DCK1; -.
DR GeneID; 446240; -.
DR KEGG; xla:446240; -.
DR CTD; 446240; -.
DR Xenbase; XB-GENE-5731213; lpcat4.S.
DR OMA; MINXDAR; -.
DR OrthoDB; 1266853at2759; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 446240; Expressed in egg cell and 19 other tissues.
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:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0047166; F:1-alkenylglycerophosphoethanolamine O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..522
FT /note="Lysophospholipid acyltransferase LPCAT4"
FT /id="PRO_0000247056"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 496..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 130..135
FT /note="HXXXXD motif"
FT COMPBIAS 498..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 522 AA; 58195 MW; FC0EF2C75ACBA972 CRC64;
MSEADPVGEK GPAEDDGEES VPFNPFLHEF EPKGLWQNAR FYILGPILFP LRFLLAAVFL
FLMWPIAALR VAGLTDKELS CSIRHRRTIL HHLIYLLSRT MFFMCGFHWI TIRGRRAPAS
EAPILVVAPH STFFDPIVTV VCDLPSVVSR VENLNIPVIG ALLRFNQSIL VSRQDPSSRK
KVVEEVKRRA TSNGEWPQVL FFPEGTNGNG KVLLKFKPGA FVAGVPVQPV LMRYPNKLPA
TIWTWKGNGV FKVLWLTMSQ FYINLEIEFL PVYHPTAEER ADPTLYAFKV QKIMADALAK
PATEFELIGD TPVSPLGHLK VALDPKIWEL GNILKKAGFS LDSVQGLIDL CLEGVCSRVG
LDELAEKLGV TQHDVISRVF NYFNKDAAGM IDFREVSLVL AAQDATRSAE ELAKLAFDLF
STCDADGRSL LSADGFASVL RSLLGSPPAE SGKVFTELYT YTELQGLTQD GFVRFAIRHP
CYRHLFLFYL RPPSSGRRKP PQIQQNGGCS GKNNPGKQSK MD
