ID   A0A3B3V913_9TELE        Unreviewed;       374 AA.
AC   A0A3B3V913;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Lysocardiolipin acyltransferase 1 {ECO:0000313|Ensembl:ENSPLAP00000021379.1};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000021379.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000021379.1}
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   AlphaFoldDB; A0A3B3V913; -.
DR   Ensembl; ENSPLAT00000011105.1; ENSPLAP00000021379.1; ENSPLAG00000005130.1.
DR   GeneTree; ENSGT00950000182836; -.
DR   Proteomes; UP000261500; 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:SF16; LYSOCARDIOLIPIN 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   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        335..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          78..200
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   374 AA;  43500 MW;  15BEA80BB2F690B3 CRC64;
     MNLRGLFFIM ALFLGSFFGS IVMLGPVLPL MLLSPAWYRW LTDRIVATWL TLPVSLLELV
     FGVKVVITGD GFIPGERSVI IMNHRTRLDW MFLWCCLLRY SYLRLEKICL KAALKVLPGF
     GWAMQVACFV FIQRRWEMDK AHLENMLDYF CDIREPLQLL LFPEGTDLTE NTKARSDAFA
     AQNNLPKMEY VLHPRSTGFT FIVDKLRKGD NLDAVHDITV AYPKNIPQTE RHLVLGEFPR
     EIHFHVRRYP VSLLPSSSTE LESWCRERWA EKESRLRDFY SGQPRGFDRD GVARVPPCKS
     ELRVGLIKAA SLVYWSGFIA FCFAGLWLWP SFRLYVLVMT VVFTVQQKLA GGLELIEMAC
     HRYWKEKVQE RKIQ
//