Search by BoMiProt ID - Bomi6911


Primary Information

BoMiProt ID Bomi6911
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
Organism Bos taurus
Uniprot IdQ0VCY6
Milk FractionWhey
Ref Sequence Id NP_001068620.1
Aminoacid Length 472
Molecular Weight 52765
Fasta Sequence https://www.uniprot.org/uniprot/Q0VCY6.fasta
Gene Name MBOAT7/LENG4/OACT7
Gene Id 504236
Protein Existence Status reviewed

Secondary Information

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.
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) 
PTMs Glycosylation
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
Predicted Disorder Regions (450-472)
DisProt Annotation
TM Helix Prediction 6TMHs; (7-29),(41-63),(74-96),(245-267),(340-358),(425-447)
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.
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.