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Database: UniProt
Entry: A0A3B5B8Z6_9TELE
LinkDB: A0A3B5B8Z6_9TELE
Original site: A0A3B5B8Z6_9TELE 
ID   A0A3B5B8Z6_9TELE        Unreviewed;       374 AA.
AC   A0A3B5B8Z6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase delta {ECO:0000256|ARBA:ARBA00040981};
DE            EC=2.3.1.51 {ECO:0000256|ARBA:ARBA00013211};
DE   AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 4 {ECO:0000256|ARBA:ARBA00041272};
DE   AltName: Full=Lysophosphatidic acid acyltransferase delta {ECO:0000256|ARBA:ARBA00042940};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000029540.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000029540.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-(9Z-
CC         octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z-octadecenoyl)-2-
CC         (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:55312, ChEBI:CHEBI:57287, ChEBI:CHEBI:74298,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:138723;
CC         Evidence={ECO:0000256|ARBA:ARBA00036892};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55313;
CC         Evidence={ECO:0000256|ARBA:ARBA00036892};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-hexadecanoyl-
CC         sn-glycero-3-phosphate = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC         docosahexaenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:55300,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57518, ChEBI:CHEBI:74298,
CC         ChEBI:CHEBI:82928; Evidence={ECO:0000256|ARBA:ARBA00035935};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55301;
CC         Evidence={ECO:0000256|ARBA:ARBA00035935};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-octadecanoyl-
CC         sn-glycero-3-phosphate = 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC         docosahexaenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:55308,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:74298, ChEBI:CHEBI:74565,
CC         ChEBI:CHEBI:77130; Evidence={ECO:0000256|ARBA:ARBA00036865};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55309;
CC         Evidence={ECO:0000256|ARBA:ARBA00036865};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC         phosphate = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:55304, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57383, ChEBI:CHEBI:74565, ChEBI:CHEBI:77098;
CC         Evidence={ECO:0000256|ARBA:ARBA00036903};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55305;
CC         Evidence={ECO:0000256|ARBA:ARBA00036903};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC         ChEBI:CHEBI:58608; EC=2.3.1.51;
CC         Evidence={ECO:0000256|ARBA:ARBA00000300};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC         Evidence={ECO:0000256|ARBA:ARBA00000300};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004728}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR   AlphaFoldDB; A0A3B5B8Z6; -.
DR   STRING; 144197.ENSSPAP00000029540; -.
DR   Ensembl; ENSSPAT00000030012.1; ENSSPAP00000029540.1; ENSSPAG00000022207.1.
DR   GeneTree; ENSGT00950000182836; -.
DR   Proteomes; UP000261400; 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:SF8; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE DELTA; 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   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        308..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        335..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          90..212
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   374 AA;  43264 MW;  E905D2E5B8AFDB6D CRC64;
     MGLLQLLKSQ VLCLLIICYV FLASGLIVNL LQFCTLPLWL INKQLARKIN IRLAYCISSQ
     MVATLEWWSG TECTLYTDPK TYPLYGKENA IVVLNHMFEI DFLCGWTFCD RFGVLGSSKV
     LAKKDLAYVP VIGWMWYFLE IVFCKRKWEE DRITVAQSLQ RLQDYPENFW FLLYCEGTRF
     TPKKHQISMQ VAETKGLPKL KYHLLPRTKG FWVTVQNLRG KAAAVYDSTL NFRNNESPTL
     LEILSGKKFH ADLYVRRIPL ESIPEDEAEC AAWLHKLYQE KDSFQEHYEQ TGRFPGPTLS
     PPRRPWSLIN WLFWSFLLLC PLGLLLTQLI SSGSVFTIVF SLVVSTVAVR WMIGQTEIDR
     GSNYGNKEAP LNNN
//
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