ID A0A3Q3AHD5_KRYMA Unreviewed; 385 AA.
AC A0A3Q3AHD5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Lysocardiolipin acyltransferase 1 {ECO:0000313|Ensembl:ENSKMAP00000015555.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000015555.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000015555.1}
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 RefSeq; XP_017274444.1; XM_017418955.1.
DR AlphaFoldDB; A0A3Q3AHD5; -.
DR STRING; 37003.ENSKMAP00000015555; -.
DR Ensembl; ENSKMAT00000015779.1; ENSKMAP00000015555.1; ENSKMAG00000011632.1.
DR GeneID; 108237502; -.
DR KEGG; kmr:108237502; -.
DR CTD; 253558; -.
DR GeneTree; ENSGT00950000182836; -.
DR OrthoDB; 2906776at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0001885; P:endothelial cell development; IEA:Ensembl.
DR GO; GO:0060217; P:hemangioblast cell differentiation; IEA:Ensembl.
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 Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..202
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 385 AA; 44400 MW; B6A8A371F631A258 CRC64;
MAVSVRGLYF VITLFLGSFF GSIFMLGPVL PLLLLSPAWY RWITDRIVAT WLTLPVSLLE
LVFGVKVVIT GDGFIPGERS VIIMNHRTRL DWMFLWCCLL RYSYLRLEKI CLKAGLKAVP
GFGWAMQVAC FVFIQRRWEA DKKHLGNMLD YFCDIREPLQ LLLFPEGTDL TENTRAKSDV
FAVQNNLPKM EYVLHPRTTG FTFIVDRLRK GDNLDAIHDI TVAYPKNIPQ TERHLIMGQF
PREIHFHVRR YPVSSLPASS SDLESWCQER WAEKEIRLRD FYSGQPRAFD RDGVARVPPC
KSELRVALIK AASLLYWSSF IALCFTGLWL WAPFRLYVLV MAVVYVAQLK LFGGLELLEM
ACHRYWKSMG AEGGEKQKVL DGKIQ
//
