ID A0A3Q3CF18_HAPBU Unreviewed; 365 AA.
AC A0A3Q3CF18;
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=1-acylglycerol-3-phosphate O-acyltransferase 5 {ECO:0000313|Ensembl:ENSHBUP00000020787.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000020787.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000020787.1}
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_005950180.1; XM_005950118.2.
DR AlphaFoldDB; A0A3Q3CF18; -.
DR STRING; 8153.ENSHBUP00000020787; -.
DR Ensembl; ENSHBUT00000030499.1; ENSHBUP00000020787.1; ENSHBUG00000023071.1.
DR GeneID; 102303854; -.
DR CTD; 55326; -.
DR GeneTree; ENSGT00950000182836; -.
DR OMA; CPRIHIH; -.
DR OrthoDB; 2906776at2759; -.
DR Proteomes; UP000264840; 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:SF76; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE EPSILON; 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 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:UP000264840};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..212
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 365 AA; 41969 MW; FE83B79B8F600D5B CRC64;
MLLSLVVHTY SLRYWFPATI MLGTAPAYLL SWGAWRLLST ILPSSLYHKI DDRLYCVYQS
MVLFFFENYT GVEIVIYGDI PKNKENVVYL SNHQCTADWI IADMLAIRQS ALGHVRYVLK
DGLKWLPLYG WYFSEHGGIY VKRSSKFNEK AMRKKLLAQT QRGAPMYLVI FPEGTRYNPD
LKNVIADSQA FAAKEGLTVL KHTLTPRMKA AHVAIDTMKG HLDAVYDVTV AYEGTLDSSG
QRRSAPAMPE FLCKECRRIH IHFDRVDIKE IPSEPAFFRR WLHDRFEIKD RLLTNFYESQ
DSDKLCKFPG EGKPSPLNLS KTLPSLVILG GLTLPMLLTE KGRKLYVRTW VCGTLLGWLW
VNIFP
//
