ID G3I349_CRIGR Unreviewed; 126 AA.
AC G3I349;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Lysophospholipid acyltransferase 7 {ECO:0000256|ARBA:ARBA00039722};
DE AltName: Full=Leukocyte receptor cluster member 4 {ECO:0000256|ARBA:ARBA00041667};
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 7 {ECO:0000256|ARBA:ARBA00041626};
GN ORFNames=I79_017850 {ECO:0000313|EMBL:EGW07372.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW07372.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
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:0000256|ARBA:ARBA00035964};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36000;
CC Evidence={ECO:0000256|ARBA:ARBA00035964};
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:0000256|ARBA:ARBA00037016};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36836;
CC Evidence={ECO:0000256|ARBA:ARBA00037016};
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:0000256|ARBA:ARBA00035860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37016;
CC Evidence={ECO:0000256|ARBA:ARBA00035860};
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:0000256|ARBA:ARBA00036730};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33196;
CC Evidence={ECO:0000256|ARBA:ARBA00036730};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000256|ARBA:ARBA00005074}.
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000256|ARBA:ARBA00010323}.
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DR EMBL; JH001168; EGW07372.1; -; Genomic_DNA.
DR AlphaFoldDB; G3I349; -.
DR STRING; 10029.G3I349; -.
DR PaxDb; 10029-XP_007634535-1; -.
DR eggNOG; KOG2706; Eukaryota.
DR InParanoid; G3I349; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR InterPro; IPR004299; MBOAT_fam.
DR PANTHER; PTHR13906:SF16; LYSOPHOSPHOLIPID ACYLTRANSFERASE 7; 1.
DR PANTHER; PTHR13906; PORCUPINE; 1.
DR Pfam; PF03062; MBOAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:EGW07372.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGW07372.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 103..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 126 AA; 14378 MW; FCFAAD2479DA970F CRC64;
MLLSAYWHGL HPGYYLSFMT IPLCLAAEGY LESALRRHLS PRGQRAWDWV HWFLKMRAYD
YMCMGFVLLS MGDTLRYWAS IYYWIHFLAL ACLGLGLALG GGSPSKRKTG APPAASSQAR
EKLREE
//
