MBOA7_CAEBR
ID MBOA7_CAEBR Reviewed; 452 AA.
AC A8WXS4;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Lysophospholipid acyltransferase 7 {ECO:0000250|UniProtKB:Q19468};
DE Short=LPLAT 7 {ECO:0000250|UniProtKB:Q19468};
DE EC=2.3.1.-;
DE AltName: Full=1-acylglycerophosphatidylinositol O-acyltransferase {ECO:0000250|UniProtKB:Q19468};
DE EC=2.3.1.n4;
DE AltName: Full=Lysophosphatidylinositol acyltransferase {ECO:0000250|UniProtKB:Q19468};
DE Short=LPIAT {ECO:0000250|UniProtKB:Q19468};
DE Short=Lyso-PI acyltransferase {ECO:0000250|UniProtKB:Q19468};
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 7 {ECO:0000250|UniProtKB:Q19468};
GN Name=mboa-7 {ECO:0000312|EMBL:CAP25198.1}; ORFNames=CBG04485;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP25198.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Acyltransferase which mediates the conversion of
CC lysophosphatidylinositol (1-acylglycerophosphatidylinositol or LPI)
CC into phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or
CC PI) (LPIAT activity). Prefers arachidonoyl-CoA or eicosapentaenoic acid
CC (EPA) as the acyl donor. Prefers sn-2-LPI rather than sn-1-LPI as the
CC acyl acceptor. Lysophospholipid acyltransferases (LPLATs) catalyze the
CC reacylation step of the phospholipid remodeling pathway also known as
CC the Lands cycle (By similarity). {ECO:0000250|UniProtKB:Q19468}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol) + an acyl-CoA
CC = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CoA;
CC Xref=Rhea:RHEA:33195, ChEBI:CHEBI:57287, ChEBI:CHEBI:57880,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64771;
CC Evidence={ECO:0000250|UniProtKB:Q19468};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + a fatty acyl-[ACP] = a 1,2-
CC diacyl-sn-glycero-3-phosphate + holo-[ACP]; Xref=Rhea:RHEA:42296,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:57970,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC EC=2.3.1.n4;
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000250|UniProtKB:Q19468}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000255}.
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DR EMBL; HE601277; CAP25198.1; -; Genomic_DNA.
DR RefSeq; XP_002644127.1; XM_002644081.1.
DR AlphaFoldDB; A8WXS4; -.
DR SMR; A8WXS4; -.
DR STRING; 6238.CBG04485; -.
DR EnsemblMetazoa; CBG04485.1; CBG04485.1; WBGene00027148.
DR GeneID; 8586122; -.
DR KEGG; cbr:CBG_04485; -.
DR CTD; 8586122; -.
DR WormBase; CBG04485; CBP15085; WBGene00027148; Cbr-mboa-7.
DR eggNOG; KOG2706; Eukaryota.
DR HOGENOM; CLU_011340_1_1_1; -.
DR InParanoid; A8WXS4; -.
DR OMA; EVERCWT; -.
DR OrthoDB; 881262at2759; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:EnsemblMetazoa.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IBA:GO_Central.
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; IEA:EnsemblMetazoa.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0035264; P:multicellular organism growth; IEA:EnsemblMetazoa.
DR GO; GO:0002119; P:nematode larval development; IEA:EnsemblMetazoa.
DR GO; GO:0018991; P:oviposition; IEA:EnsemblMetazoa.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..452
FT /note="Lysophospholipid acyltransferase 7"
FT /id="PRO_0000393936"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 350
FT /evidence="ECO:0000250|UniProtKB:Q19468"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 452 AA; 51714 MW; E842A121CC5A495F CRC64;
MEKIIGLMSR DDWVYTGLLL FSFAASCYVR KLGNNILASG ALGFAMALFI IGPRIAYSLG
ICAIAVGIQA FAPKKKVPFY VFLTTFTYLM FVRFAHYFLP VVEVASHTNV IQLIITLRII
GITFEENDAW LHKNDENATK RYLTRMPTLL EKFAYFYHFC GLFTGPYYTY QMLLDSQNPA
LQSWDPTPEV TSRFVRLLWS VPAFVITNHY FPLDSLRSDA IWEVSFFTRL VYAALIFVVF
KTRVYSAWAI AESICVILGI GIYPAASNPK IIVGPTDLKV FEGLRDKENV EMNSDAIVNL
DIPKVEFSDG FRDGMKAWNR SVQTWLALYV HSRVKFMRVE TTMLVSAIWH GTYAGYFMSF
GVVAMCAILE DVIFKLVPVN PETGLRPQWF RILYTHTIRC RGFEMLATGF LLKNASDVHH
FWSSIYYWLP LLCVPFYIYS VKTAAPKLKL VV
