MBOA7_XENLA
ID MBOA7_XENLA Reviewed; 474 AA.
AC Q5U4T9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Lysophospholipid acyltransferase 7;
DE Short=LPLAT 7;
DE EC=2.3.1.-;
DE AltName: Full=Leukocyte receptor cluster member 4;
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 7;
DE Short=O-acyltransferase domain-containing protein 7;
GN Name=mboat7; Synonyms=leng4, oact7;
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].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acyltransferase which catalyzes the transfert of an acyl
CC group from an acyl-CoA to a lysophosphatidylinositol (1-
CC acylglycerophosphatidylinositol or LPI) leading to the production of a
CC phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI)
CC and participates in the reacylation step of the phospholipid remodeling
CC pathway also known as the Lands cycle. Prefers arachidonoyl-CoA as the
CC acyl donor, thus contributing to the regulation of free levels
CC arachidonic acid in cell. {ECO:0000250|UniProtKB:Q8CHK3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phospho-(1D-myo-inositol) = a 1-acyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + CoA;
CC Xref=Rhea:RHEA:37015, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:64771, ChEBI:CHEBI:75243;
CC Evidence={ECO:0000250|UniProtKB:Q96N66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37016;
CC Evidence={ECO:0000250|UniProtKB:Q96N66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000250|UniProtKB:Q96N66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36000;
CC Evidence={ECO:0000250|UniProtKB:Q96N66};
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:Q8CHK3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33196;
CC Evidence={ECO:0000250|UniProtKB:Q8CHK3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-octadecanoyl-sn-
CC glycero-3-phospho-(1D-myo-inositol) = 1-octadecanoyl-2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-
CC inositol) + CoA; Xref=Rhea:RHEA:36835, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57368, ChEBI:CHEBI:74243, ChEBI:CHEBI:133606;
CC Evidence={ECO:0000250|UniProtKB:Q8CHK3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36836;
CC Evidence={ECO:0000250|UniProtKB:Q8CHK3};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000250|UniProtKB:Q96N66}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96N66}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96N66}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC084955; AAH84955.1; -; mRNA.
DR RefSeq; NP_001088606.1; NM_001095137.1.
DR AlphaFoldDB; Q5U4T9; -.
DR SMR; Q5U4T9; -.
DR MaxQB; Q5U4T9; -.
DR DNASU; 495497; -.
DR GeneID; 495497; -.
DR KEGG; xla:495497; -.
DR CTD; 495497; -.
DR Xenbase; XB-GENE-978831; mboat7.L.
DR OMA; EVERCWT; -.
DR OrthoDB; 881262at2759; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 495497; Expressed in spleen 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:0008374; F:O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0090207; P:regulation of triglyceride metabolic process; ISS:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 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..474
FT /note="Lysophospholipid acyltransferase 7"
FT /id="PRO_0000317460"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 23..33
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 34..57
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 58..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 74..93
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 94..193
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 194..211
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 212..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 231..260
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 261..427
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 449..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 474 AA; 54624 MW; 7ACC86270E03BBFF CRC64;
MSPNELTYLA ILLGSAPLGF LFKNGSPQVK QRGSAAVGVA LTLITCHIHS LHSAITILGT
WLIIKILPRS CHFPTLGWTF TYLLFFRTIT YFDIPAPTPF TNAVQLLLTL KLVSLANEVQ
DFYRAKKQEV TSFSKPSAIS TIPSIPSLRE MFYYSYCYIG LMTGPFYRYK TYYDWLHQID
PASIPSWKPL VSRLKPAPVF GVLFLIASQY FPLDYVKTDE FYEQAFLYRL FYMVPTFFIF
RMRFYVAWIF AECGCISAAF GAYPVSAKSR SGGGPTVEYA PLERNAEGAK VELEYDYETI
KNIDCYGADF CVKVKDGMRY WNMSVQWWLA QYIYKNSPVK SLVFGSAWTM LVSAYWHGIH
PGYYMSFLTI PLCLAAEGSM EAGLRRHVSD SGKMIFDWVH WFLKMRAYDY MCMGFVLLTF
TDTYRYWQSI YFSVHVLAIS LFLLGRVLAL KSPRRPRNTK EEKAEAKQEN RLQE
