Primary Information |
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BoMiProt ID | Bomi6911 |
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Protein Name | Lysophospholipid acyltransferase 7(LPLAT 7)/Leukocyte receptor cluster member 4/Membrane-bound O-acyltransferase domain-containing protein 7/O-acyltransferase domain-containing protein 7 |
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Organism | Bos taurus |
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Uniprot ID | Q0VCY6 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_001068620.1 |
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Aminoacid Length | 472 |
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Molecular Weight | 52765 |
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FASTA Sequence |
Download |
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Gene Name | MBOAT7/LENG4/OACT7 |
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Gene ID | 504236 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | This is a lysophosphatidylinositol acyltransferase that has specificity for arachidonoyl-CoA as an acyl donor. This protein is involved in the re-acylation of phospholipids as part of the phospholipid remodeling pathway known as the Land cycle. |
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Biochemical Properties | catalyzes the transfert of an acyl group from an acyl-CoA to a lysophosphatidylinositol (1-acylglycerophosphatidylinositol or LPI) leading to the production of a phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI) |
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PTMs | Glycosylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q0VCY6|MBOA7_BOVIN Lysophospholipid acyltransferase 7 OS=Bos taurus OX=9913 GN=MBOAT7 PE=2 SV=1
MSPEEWTYLVVLLISIPIGFLFKKAGPGLKRWGAAAVGLGLTLFTCGPHTLHSLVTILGT
WALIQAQPCSCHALALAWTFSYLLFFRALSLLGLPTPTPFTNAVQLLLTLKLVSLASEVQ
DLHVAQRKEMASGFSKGPPLGLLPDVPSLMETLSYSYCYVGIMTGPFFRYRTYLDWLEQP
FPGAVPSLRPLLRRAWPAPLFGLLFLLSSHLFPLEAVREDAFYARPLPARLFYMIPVFFA
FRMRFYVAWIAAECGCIAAGFGAYPVAAKARAGGGPTLQCPPPSSPEMAASLEYDYETIR
NIDCYNTDFCVTVREGMRYWN*321MTVQWWLAQYIYKSAPARSYVLRSAWTMLLSAYWHGLHP
GYYLSFLTIPLCLAAERQLESALRWRLGPGGQKAWDWVHWFLKMRAYDYMSMGFVLLSLR
DTLRYWASVYFCVHVLALAALGLGLALGRGGPGRRKSGAPAPSPASGKLREE
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Predicted Disorder Regions | (450-472) |
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DisProt Annotation | |
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TM Helix Prediction | 6TMHs; (7-29),(41-63),(74-96),(245-267),(340-358),(425-447) |
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Additional Comments | mRNAs for MBOATs 1, 2, 5, and 7 were detected in neutrophils, and acyltransferase activities in neutrophil microsomes were found to be consistent with the activities of several MBOAT enzymes. These four members of the human MBOAT family were also expressed in yeast and assayed with a novel LC/MS/MS-based approach, producing an extensive profile of the substrate specificities and thimerosal sensitivity for each enzyme. |
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Bibliography | 1.Gijón MA, Riekhof WR, Zarini S, Murphy RC, Voelker DR (October 2008). "Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils". J. Biol. Chem. 283 (44): 30235–45. doi:10.1074/jbc.M806194200. PMC 2573059. PMID 18772128. 2. |