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LPCT4_XENTR
ID   LPCT4_XENTR             Reviewed;         522 AA.
AC   Q28C60; Q5FWS1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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; ORFNames=TEgg023j17.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-522.
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2005) 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}.
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DR   EMBL; CR942439; CAJ81339.1; -; mRNA.
DR   EMBL; BC089229; AAH89229.1; -; mRNA.
DR   RefSeq; NP_001037863.1; NM_001044398.1.
DR   AlphaFoldDB; Q28C60; -.
DR   SMR; Q28C60; -.
DR   PaxDb; Q28C60; -.
DR   Ensembl; ENSXETT00000037017; ENSXETP00000037017; ENSXETG00000016994.
DR   GeneID; 548367; -.
DR   KEGG; xtr:548367; -.
DR   CTD; 254531; -.
DR   Xenbase; XB-GENE-5731127; lpcat4.
DR   eggNOG; KOG4666; Eukaryota.
DR   InParanoid; Q28C60; -.
DR   OrthoDB; 1266853at2759; -.
DR   Reactome; R-XTR-1482788; Acyl chain remodelling of PC.
DR   Reactome; R-XTR-1482801; Acyl chain remodelling of PS.
DR   Reactome; R-XTR-1482839; Acyl chain remodelling of PE.
DR   Reactome; R-XTR-1482925; Acyl chain remodelling of PG.
DR   Reactome; R-XTR-1483166; Synthesis of PA.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000016994; Expressed in neurula embryo and 15 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_0000247057"
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        506..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"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   522 AA;  58376 MW;  C0EFD498422A2E8A CRC64;
     MSEAEPVGEK GPAEDDGEES VPFNPFLHEF EPEGFWQKAR FYILGFTLFP LRFLLAAIFL
     FLMWPIAALR VAGLTEEELS RSIRHRRTIL HHLIYLLSRT MFFMCGFHWI TIRGRRAPAS
     EAPLLVVAPH STFFDPIVTV VCDLPSVVSR VENLNIPVIG ALLRFNQSIL VSRQDPSSRK
     KVVEEVKKRA TSNGDWPQVL FFPEGTNGNG KVLLKFKPGA FVAGVPVQPV LMRYPNKLPA
     TIWTWKGNGV FKVLWLTMSQ FYINLEIEFL PVYHPTAEER ADPTLYASKV QKIMADALAK
     PATEFELIGD TPVTPVGHLK VALDPKIWEL GNILEKAGFS LDSVQGLIDL CLEGVCSRVG
     LDELAEKLGV TQHDVISRVF NYFHKDASGM IDFREVSLVL AAQDATRSAE ELAKLAFDLF
     STCDADGRFL LSADGFAAIL RSVVGSPPAE SGKVFSELCT YTELHGLTQD GFVRFAIRHP
     CYRHLFLFYL RPPSSGRRKP PHIQQNGGCS GKNNPRNQSK MD
 
 
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