MBOA5_CAEEL
ID MBOA5_CAEEL Reviewed; 473 AA.
AC O01925; Q86DC4;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Lysophospholipid acyltransferase 5;
DE Short=LPLAT 5;
DE EC=2.3.1.-;
DE AltName: Full=Probable 1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23;
DE AltName: Full=Probable 1-acylglycerophosphoethanolamine O-acyltransferase;
DE EC=2.3.1.n7;
DE AltName: Full=Probable 1-acylglycerophosphoserine O-acyltransferase;
DE EC=2.3.1.n6;
DE AltName: Full=Probable lysophosphatidylcholine acyltransferase;
DE Short=LPCAT;
DE Short=Lyso-PC acyltransferase;
DE AltName: Full=Probable lysophosphatidylethanolamine acyltransferase;
DE Short=LPEAT;
DE Short=Lyso-PE acyltransferase;
DE AltName: Full=Probable lysophosphatidylserine acyltransferase;
DE Short=LPSAT;
DE Short=Lyso-PS acyltransferase;
GN Name=mboa-6; ORFNames=R155.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=18782225; DOI=10.1111/j.1365-2443.2008.01212.x;
RA Matsuda S., Inoue T., Lee H.C., Kono N., Tanaka F., Gengyo-Ando K.,
RA Mitani S., Arai H.;
RT "Member of the membrane-bound O-acyltransferase (MBOAT) family encodes a
RT lysophospholipid acyltransferase with broad substrate specificity.";
RL Genes Cells 13:879-888(2008).
CC -!- FUNCTION: Probable acyltransferase which may mediate the conversion of
CC lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC)
CC into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC)
CC (LPCAT activity). May also catalyze the conversion of
CC lysophosphatidylethanolamine (1-acyl-2-hydroxy-sn-glycero-3-
CC phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-
CC sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity), as well as
CC the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-
CC 3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-
CC glycero-3-phospho-L-serine or PS) (LPSAT activity). Required for
CC incorporation of arachidonic acid into PC, PE, and PS.
CC {ECO:0000269|PubMed:18782225}.
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 Evidence={ECO:0000269|PubMed:18782225};
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 Evidence={ECO:0000269|PubMed:18782225};
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 Evidence={ECO:0000269|PubMed:18782225};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:18782225}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=O01925-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O01925-2; Sequence=VSP_053557;
CC -!- DOMAIN: The di-lysine motif may confer endoplasmic reticulum
CC localization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; FO081449; CCD71668.1; -; Genomic_DNA.
DR EMBL; FO081449; CCD71669.1; -; Genomic_DNA.
DR PIR; T15281; T15281.
DR RefSeq; NP_001022735.1; NM_001027564.3. [O01925-1]
DR RefSeq; NP_001022736.1; NM_001027565.3.
DR AlphaFoldDB; O01925; -.
DR SMR; O01925; -.
DR BioGRID; 40593; 2.
DR DIP; DIP-26801N; -.
DR STRING; 6239.R155.1a; -.
DR EPD; O01925; -.
DR PaxDb; O01925; -.
DR PeptideAtlas; O01925; -.
DR EnsemblMetazoa; R155.1a.1; R155.1a.1; WBGene00020115. [O01925-1]
DR EnsemblMetazoa; R155.1b.1; R155.1b.1; WBGene00020115. [O01925-2]
DR EnsemblMetazoa; R155.1b.2; R155.1b.2; WBGene00020115. [O01925-2]
DR GeneID; 175339; -.
DR KEGG; cel:CELE_R155.1; -.
DR UCSC; R155.1a.1; c. elegans.
DR CTD; 175339; -.
DR WormBase; R155.1a; CE32713; WBGene00020115; mboa-6. [O01925-1]
DR WormBase; R155.1b; CE33935; WBGene00020115; mboa-6. [O01925-2]
DR eggNOG; KOG2705; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_6_0_1; -.
DR InParanoid; O01925; -.
DR OMA; CILVLRM; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; O01925; -.
DR BRENDA; 2.3.1.23; 1045.
DR Reactome; R-CEL-1482788; Acyl chain remodelling of PC.
DR Reactome; R-CEL-1482801; Acyl chain remodelling of PS.
DR Reactome; R-CEL-1482839; Acyl chain remodelling of PE.
DR UniPathway; UPA00085; -.
DR PRO; PR:O01925; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00020115; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:WormBase.
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:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IBA:GO_Central.
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:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0008374; F:O-acyltransferase activity; ISS:WormBase.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IMP:WormBase.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:WormBase.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IMP:WormBase.
DR GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase.
DR GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:WormBase.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..473
FT /note="Lysophospholipid acyltransferase 5"
FT /id="PRO_0000424900"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 470..473
FT /note="Di-lysine motif"
FT /evidence="ECO:0000250"
FT ACT_SITE 315
FT /evidence="ECO:0000250"
FT ACT_SITE 351
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..132
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_053557"
SQ SEQUENCE 473 AA; 54113 MW; 2198AA79247D1A77 CRC64;
MGVVGALSEV TSASEDALRL LISVLAGYPL AVVHRTFFYN KPAQHQHLFF VIVGLSLWMF
NCGSSVIHPI LSIFGAFFIT NFMAGTDASI YAAHIVFLGH LLIGYWFHET DTYDITWTTP
FCIMTLRFIG LVMDVYDGAQ KPEHLKPDQK LTAISDKPGL LEIAAFGLFF QGTLVGPQFT
LSKFRSFVNG DWLDSDGQPP KSAFLPSIGR FLAGCTYMVL HQWGQFWIPD QYFNSDAYNN
LSFFWRWSWV TLWFRLTMYK YCAMWLITEG ASILSGLGHN GKDAEGNDRW DGVRDLHIIK
WETGHDYNSV VESFNCGTNT FAKNHIHRRL RWVNNKLASH VITLSYLAIW HGYHLGYFLL
FGVELGCVQA QNQLYALIKR TPGWSEAISK PISRPFIWIF GKLTISYSMG FAFLMFGLIK
TKYWIGPVKS LYFIGFIIYF IVWPILHMVL LRVLPRHPKK AAAEKPEEVK KEL
