ID A0A2U9C8J1_SCOMX Unreviewed; 377 AA.
AC A0A2U9C8J1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=1-acylglycerol-3-phosphate O-acyltransferase 3 {ECO:0000313|EMBL:AWP12895.1, ECO:0000313|EMBL:AWP12896.1};
DE SubName: Full=1-acylglycerol-3-phosphate O-acyltransferase 3 isoform 3 {ECO:0000313|EMBL:AWP12897.1};
GN Name=agpat3 {ECO:0000313|Ensembl:ENSSMAP00000042288.1};
GN ORFNames=SMAX5B_018462 {ECO:0000313|EMBL:AWP12895.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP12895.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP12895.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSMAP00000042288.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; CP026256; AWP12895.1; -; Genomic_DNA.
DR EMBL; CP026256; AWP12896.1; -; Genomic_DNA.
DR EMBL; CP026256; AWP12897.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000011372; -.
DR Ensembl; ENSSMAT00000060413.1; ENSSMAP00000042288.1; ENSSMAG00000007002.2.
DR GeneTree; ENSGT00950000182836; -.
DR OMA; PTIGWAW; -.
DR OrthoDB; 921703at2759; -.
DR Proteomes; UP000246464; Chromosome 14.
DR Proteomes; UP000694558; Chromosome 14.
DR Bgee; ENSSMAG00000007002; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10983:SF9; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE GAMMA; 1.
DR PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 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|EMBL:AWP12895.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023209};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AWP12895.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..212
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 377 AA; 43575 MW; F0EA0F938FC92B78 CRC64;
MALLAYLKSL FILQLLMGFV FVVSGLIINF IQLCTCVLWP FNKQLYRRIN CRLAYSLWSQ
LVMLLEWWSG TDCTLYTDQA TVDKFGTEHA IIILNHNFEI DFLCGWTMCE RYGILGSSKV
LAKHELLKVP LIGWTWYFLE IVFCKRKWEE DRKTVFSGLD RLKDYPEYMW FLLYCEGTRF
TEQKHQISMQ IAESKGLPKL KYHLLPRTKG FTTTLQCLKG TVTAVYDVTL NFKDNQTPTL
LGIVNGKKYK ADLSVRRFSV EEIPDDEKEC ANWLHKLYQE KDALQEHYSK EGKFPGPTII
PPRRPWTLLN FLFWATLLLS PLINFACGVA VSGSPLLIIG FIIFLIIASI AIRRLIGVTE
VKKTGSSYGN QEAKKQN
//