MBOA7_BOVIN
ID MBOA7_BOVIN Reviewed; 472 AA.
AC Q0VCY6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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. In liver, participates in the regulation of
CC triglyceride metabolism through the phosphatidylinositol acyl-chain
CC remodeling regulation. {ECO:0000250|UniProtKB:Q8CHK3}.
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 + 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=(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 -!- SUBUNIT: Interacts with SPTSSA; the interaction facilitates MBOAT7
CC location to mitochondria-associated membranes (MAMs).
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}. Note=Localized in specific membrane
CC structures termed mitochondria-associated membranes (MAMs) which
CC connect the endoplasmic reticulum (ER) and the mitochondria.
CC {ECO:0000250|UniProtKB:Q96N66}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BC119932; AAI19933.1; -; mRNA.
DR RefSeq; NP_001068620.1; NM_001075152.1.
DR RefSeq; XP_005219813.1; XM_005219756.3.
DR RefSeq; XP_010813839.1; XM_010815537.2.
DR AlphaFoldDB; Q0VCY6; -.
DR SMR; Q0VCY6; -.
DR STRING; 9913.ENSBTAP00000021152; -.
DR PaxDb; Q0VCY6; -.
DR PRIDE; Q0VCY6; -.
DR Ensembl; ENSBTAT00000021152; ENSBTAP00000021152; ENSBTAG00000015908.
DR Ensembl; ENSBTAT00000068283; ENSBTAP00000061023; ENSBTAG00000015908.
DR GeneID; 504236; -.
DR KEGG; bta:504236; -.
DR CTD; 79143; -.
DR VEuPathDB; HostDB:ENSBTAG00000015908; -.
DR VGNC; VGNC:31289; MBOAT7.
DR eggNOG; KOG2706; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_1_1_1; -.
DR InParanoid; Q0VCY6; -.
DR OMA; EVERCWT; -.
DR OrthoDB; 881262at2759; -.
DR TreeFam; TF320024; -.
DR Reactome; R-BTA-1482922; Acyl chain remodelling of PI.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000015908; Expressed in Ammon's horn and 105 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:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008374; F:O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0021819; P:layer formation in cerebral cortex; 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 GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
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..472
FT /note="Lysophospholipid acyltransferase 7"
FT /id="PRO_0000317456"
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..194
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 195..212
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 213..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 232..261
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 262..426
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 448..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT REGION 450..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 472 AA; 52765 MW; 0A22BEBAF23B5795 CRC64;
MSPEEWTYLV VLLISIPIGF LFKKAGPGLK RWGAAAVGLG LTLFTCGPHT LHSLVTILGT
WALIQAQPCS CHALALAWTF SYLLFFRALS LLGLPTPTPF TNAVQLLLTL KLVSLASEVQ
DLHVAQRKEM ASGFSKGPPL GLLPDVPSLM ETLSYSYCYV GIMTGPFFRY RTYLDWLEQP
FPGAVPSLRP LLRRAWPAPL FGLLFLLSSH LFPLEAVRED AFYARPLPAR LFYMIPVFFA
FRMRFYVAWI AAECGCIAAG FGAYPVAAKA RAGGGPTLQC PPPSSPEMAA SLEYDYETIR
NIDCYNTDFC VTVREGMRYW NMTVQWWLAQ YIYKSAPARS YVLRSAWTML LSAYWHGLHP
GYYLSFLTIP LCLAAERQLE SALRWRLGPG GQKAWDWVHW FLKMRAYDYM SMGFVLLSLR
DTLRYWASVY FCVHVLALAA LGLGLALGRG GPGRRKSGAP APSPASGKLR EE
