ID A0A3Q1ITG1_ANATE Unreviewed; 372 AA.
AC A0A3Q1ITG1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Lysophosphatidylglycerol acyltransferase 1 {ECO:0000313|Ensembl:ENSATEP00000023720.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000023720.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000023720.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3Q1ITG1; -.
DR STRING; 64144.ENSATEP00000023720; -.
DR Ensembl; ENSATET00000024102.2; ENSATEP00000023720.1; ENSATEG00000016453.2.
DR GeneTree; ENSGT00950000182836; -.
DR InParanoid; A0A3Q1ITG1; -.
DR OMA; PLDIQTW; -.
DR OrthoDB; 3012482at2759; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
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 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:UP000265040};
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 DOMAIN 95..218
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 372 AA; 43309 MW; 352B889BFB1B2CD3 CRC64;
MAQLLDGAGK LGWVLLKSLL RFVFMFFNNC VAIPSYCLYL LLLQPLRIWD SSTFWHIEGV
MFKWLLAMVS SWGWIAGYTV TEWGDDVRPI SEEEAMVIVN HQSTGDVCTL MMCLQDKGTV
VRKMMWLMDH VFKYTNFGLV SLIHGDFFIR QGKAHRDKQL IYLKNHLDKY YHSRNRKWIV
LFPEGGFLRK RRETSQLFAK KNSLPHLTHV TLPRLGATQV ILKSLSAPLE NGSVGSETNT
PNQTGNKRKG LQWVIDVTIA YPKARPMDIQ TWIFGYRPPT VTHVHYRMYP IKEVPLETEA
LTDWLYQRFV EKEELLTHFY DTGSFPSPEG QKEAASRQMT LDPVWLCLVQ SFAFASGYIW
YNALQYLYYC LF
//