ID M3YWN7_MUSPF Unreviewed; 370 AA.
AC M3YWN7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Lysophosphatidylglycerol acyltransferase 1 {ECO:0000313|Ensembl:ENSMPUP00000015747.1, ECO:0000313|RefSeq:XP_004756915.1, ECO:0000313|RefSeq:XP_044940627.1};
GN Name=LPGAT1 {ECO:0000313|Ensembl:ENSMPUP00000015747.1,
GN ECO:0000313|RefSeq:XP_004756915.1, ECO:0000313|RefSeq:XP_044940627.1,
GN ECO:0000313|RefSeq:XP_044940628.1, ECO:0000313|RefSeq:XP_044940629.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000015747.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000015747.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004756915.1, ECO:0000313|RefSeq:XP_044940627.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004756915.1,
RC ECO:0000313|RefSeq:XP_044940627.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; AEYP01042223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01042224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01042225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004756914.1; XM_004756857.2.
DR RefSeq; XP_004756915.1; XM_004756858.3.
DR RefSeq; XP_044940627.1; XM_045084692.1.
DR RefSeq; XP_044940628.1; XM_045084693.1.
DR RefSeq; XP_044940629.1; XM_045084694.1.
DR STRING; 9669.ENSMPUP00000015747; -.
DR Ensembl; ENSMPUT00000015988.1; ENSMPUP00000015747.1; ENSMPUG00000015854.1.
DR GeneID; 101674241; -.
DR CTD; 9926; -.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR HOGENOM; CLU_046804_2_0_1; -.
DR OMA; PLDIQTW; -.
DR OrthoDB; 3012482at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0047190; F:2-acylglycerophosphocholine O-acyltransferase activity; IEA:Ensembl.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IEA:Ensembl.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR10983:SF2; ACYL-COA:LYSOPHOSPHATIDYLGLYCEROL ACYLTRANSFERASE 1; 1.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|RefSeq:XP_004756915.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..219
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 370 AA; 42958 MW; D2401F6EC5B920E3 CRC64;
MAVTLEDAPW LGWILVKALM RFAFMVANNL VAISSYICYV IILQPLRLLD SKRFWYIEGI
MYKWLLGMVA SWGWYAGYTV MEWGDDIKAV SQDEAVMLVN HQATGDVCTL MMCLQDKGLV
VAQMMWLMDH IFKYTNFGIV SLIHGDFFIR QGKSHRDQQL LLLKKHLEKN YRSRDRKWIV
LFPEGGFLRK RRETSQAFAK KNNLPFLTHV TLPRIGATNI ILSALVARQE NGSPAGGDAK
ELGSKSKGLQ WIIDTTIAYP KAEPIDIQTW ILGYRKPTIT HVHYRIFPIK DVPLETDGLA
DWLYQRFIEK EELLSHFYET GAFPPPKGHN EAVSREMTLS NMWIFLIQSF AFLSGYMWYN
IIQYFYHCLF
//