MBOA7_DANRE
ID MBOA7_DANRE Reviewed; 467 AA.
AC Q7SZQ0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) 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}.
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DR EMBL; BC056305; AAH56305.1; -; mRNA.
DR RefSeq; NP_956831.1; NM_200537.1.
DR AlphaFoldDB; Q7SZQ0; -.
DR SMR; Q7SZQ0; -.
DR STRING; 7955.ENSDARP00000106817; -.
DR PaxDb; Q7SZQ0; -.
DR GeneID; 393509; -.
DR KEGG; dre:393509; -.
DR CTD; 79143; -.
DR ZFIN; ZDB-GENE-040426-1516; mboat7.
DR eggNOG; KOG2706; Eukaryota.
DR InParanoid; Q7SZQ0; -.
DR PhylomeDB; Q7SZQ0; -.
DR Reactome; R-DRE-1482922; Acyl chain remodelling of PI.
DR UniPathway; UPA00085; -.
DR PRO; PR:Q7SZQ0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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: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; ISS:UniProtKB.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
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..467
FT /note="Lysophospholipid acyltransferase 7"
FT /id="PRO_0000317459"
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..421
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 443..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT REGION 447..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 467 AA; 53317 MW; C79EB8C5010DBB0E CRC64;
MSPDELVYLG ILAATIPVGF LFRYLSPPVK QGAALLLGLI ISIATCGIHT LHSLCTVLGT
WIIIKINWRS APALSLAWTF LYLLFFRLVT WFGLPQPTPF ANAIQLLLTL KMVSLANEVQ
SYHLERKKEV STFTKSPVVA GLSHEPSLYD IISYSYCYVG IMTGPFFRYQ TYADWLQQSS
PLSLPGKEPC LQRLKMVPVY GLLFIAVNSV FPLSYVRTED FLEHNYFYRF FYMVAIFFVF
RMRFYSAWCG AEAGCISAGL GCYPQGALSK PGGGPTVKYS PDPETAVEYD FKTIQNIDCY
NTDFCVKVRH GMRYWNMTVQ WWLHHYIYPN APFRAYALRA GWTMLISAYW HGLHAGYYLS
FLTIPLCIAA ETAMEASVRA RLGPAGQNIF DWIHWFLKMR AYDYMCMGFV LLKASDTISY
WSSIYFVIHI IAIVCIAVGQ FMKGGRKREK RERGEGEKED AVREKAE
