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Database: UniProt
Entry: A0A3Q1ITG1_ANATE
LinkDB: A0A3Q1ITG1_ANATE
Original site: A0A3Q1ITG1_ANATE 
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}.
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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
//
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