GPT3L_DANRE
ID GPT3L_DANRE Reviewed; 443 AA.
AC A3KGT9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 3-like;
DE EC=2.3.1.15;
DE AltName: Full=1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9-like;
DE Short=1-AGP acyltransferase 9-like;
DE Short=1-AGPAT 9-like;
DE EC=2.3.1.51;
DE AltName: Full=Lysophosphatidic acid acyltransferase theta-like;
DE Short=LPAAT-theta-like;
GN Name=agpat9l; ORFNames=si:ch211-155m12.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: May transfer the acyl-group from acyl-coA to the sn-1
CC position of glycerol-3-phosphate, an essential step in glycerolipid
CC biosynthesis. Also transfers the acyl-group from acyl-coA to the sn-2
CC position of 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid, or
CC LPA), forming 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid, or
CC PA) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
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 -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- CAUTION: Despite its name, the human homolog of this protein appears to
CC lack measurable glycerol-3-phosphate acyltransferase activity under
CC some conditions (PMID:19318427). {ECO:0000305}.
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DR EMBL; AL928901; CAM46900.1; -; Genomic_DNA.
DR RefSeq; NP_001092920.1; NM_001099450.1.
DR AlphaFoldDB; A3KGT9; -.
DR STRING; 7955.ENSDARP00000046439; -.
DR PaxDb; A3KGT9; -.
DR Ensembl; ENSDART00000046440; ENSDARP00000046439; ENSDARG00000006491.
DR Ensembl; ENSDART00000183981; ENSDARP00000152295; ENSDARG00000109952.
DR Ensembl; ENSDART00000190537; ENSDARP00000157263; ENSDARG00000112415.
DR GeneID; 567414; -.
DR KEGG; dre:567414; -.
DR CTD; 567414; -.
DR ZFIN; ZDB-GENE-060531-19; agpat9l.
DR eggNOG; KOG2898; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_031080_0_1_1; -.
DR InParanoid; A3KGT9; -.
DR OMA; WASKIHE; -.
DR OrthoDB; 526132at2759; -.
DR PhylomeDB; A3KGT9; -.
DR TreeFam; TF315039; -.
DR UniPathway; UPA00282; -.
DR UniPathway; UPA00557; UER00612.
DR PRO; PR:A3KGT9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000006491; Expressed in intestine and 17 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISS:UniProtKB.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..443
FT /note="Glycerol-3-phosphate acyltransferase 3-like"
FT /id="PRO_0000291574"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 238..243
FT /note="HXXXXD motif"
SQ SEQUENCE 443 AA; 50522 MW; 34F445FFB2C393AD CRC64;
MEGYWAVLFP VLKVWFSCVI VLIMLPAMFG ISLGITETYM KLLIKTLEWA THRIQRASRA
EEILKESASN GLIQRDNSSL EQEIEELRRN RPKSADRGDF TLSDVLYFSR KGFESIVEDD
VTQRFTSEEL VSWNLLTRTN NNFQYISLRL TVLWVVGVVV RYCILLPLRI TLTTIGLTWL
VIGTTTVGFL PNCRVKNWLS ELVHLMCYRI CARGLSATIH FHNKQNRPKK GGICVANHTS
PIDVVILAND GCYAMVGQVH GGLMGVLQRA MERSCPHIWF ERSEMRDRHL VTQRLKDHVN
AKTKLPILIF PEGTCINNTS VMMFKKGSFE IGGTIYPVAI KYDPQFGDAF WNSSKYSIMS
YLLRMMTSWA IVCNVWYLPP MTHEEGEDAV QFANRVKSTI AQQGGLVDLA WDGGLKRAKV
KDSFKEQQQK KYSHMVVGED SSD
