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Protein

Glycerol-3-phosphate acyltransferase 3

Gene

gpat3

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

May transfer the acyl-group from acyl-coA to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Also transfers the acyl-group from acyl-coA to the sn-2 position of 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid, or LPA), forming 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid, or PA) (By similarity).By similarity

Catalytic activityi

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.
Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

Pathwayi: triacylglycerol biosynthesis

This protein is involved in the pathway triacylglycerol biosynthesis, which is part of Glycerolipid metabolism.
View all proteins of this organism that are known to be involved in the pathway triacylglycerol biosynthesis and in Glycerolipid metabolism.

Pathwayi: CDP-diacylglycerol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glycerol-3-phosphate acyltransferase 3 (gpat3), Glycerol-3-phosphate acyltransferase 3-like (agpat9l)
  2. Lysocardiolipin acyltransferase 1 (lclat1)
  3. Phosphatidate cytidylyltransferase (cds2), Phosphatidate cytidylyltransferase (cds2), Phosphatidate cytidylyltransferase (cds1), Phosphatidate cytidylyltransferase, mitochondrial (tamm41), Phosphatidate cytidylyltransferase (cds1), Phosphatidate cytidylyltransferase (cds2)
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00282.
UPA00557; UER00612.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase 3By similarity (EC:2.3.1.15)
Short name:
GPAT-3
Alternative name(s):
1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9 (EC:2.3.1.51)
Short name:
1-AGP acyltransferase 9
Short name:
1-AGPAT 9
Lysophosphatidic acid acyltransferase theta
Short name:
LPAAT-theta
Gene namesi
Name:gpat3By similarity
Synonyms:agpat9
ORF Names:si:ch211-85e10.5, zgc:91857
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Unplaced

Organism-specific databases

ZFINiZDB-GENE-040718-436. gpat3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei9 – 2921HelicalSequence analysisAdd
BLAST
Transmembranei146 – 16621HelicalSequence analysisAdd
BLAST
Transmembranei170 – 19021HelicalSequence analysisAdd
BLAST
Transmembranei358 – 37821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Glycerol-3-phosphate acyltransferase 3PRO_0000291575Add
BLAST

Proteomic databases

PaxDbiQ6DG38.

Expressioni

Gene expression databases

BgeeiQ6DG38.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000115935.

Structurei

3D structure databases

ProteinModelPortaliQ6DG38.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi238 – 2436HXXXXD motif

Domaini

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2898. Eukaryota.
COG0204. LUCA.
HOGENOMiHOG000265725.
InParanoidiQ6DG38.
KOiK13506.
OMAiFVRYCVL.
OrthoDBiEOG70GMFG.
PhylomeDBiQ6DG38.
TreeFamiTF315039.

Family and domain databases

InterProiIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6DG38-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGAWDVAFV LLHVWMSIVA GLIVLPAMFG VSLGFTDIYI KLLVKTLEWA
60 70 80 90 100
TLRIQRGQKE QPTLPLQLAN GIIEKDDGSM EEEIVELRRS HPKNLAEGNF
110 120 130 140 150
TLCDAFYFCK KGIENIVEDQ VTQRFSSEEL ASWNLLTRTN NNFRYISVRL
160 170 180 190 200
TIIWGLGVFV RYCVLLPLRI TLAVIGLSWL VIGTTLVGFL PNSKVKNWLS
210 220 230 240 250
DLVHITCYRI CARGLSATIR YHNKENRPKK GGICVANHTS PIDIVILAND
260 270 280 290 300
GCYAMVGQVH GGLMGVIQRS MVRSCPHVWF ERSEMKDRHA VAKRLKDHIS
310 320 330 340 350
DKTKLPILIF PEGTCINNTS VMMFKKGSFE FGGTIYPVAI KYDPRFGDAF
360 370 380 390 400
WNSAKYNMVS YILRMMTSWA IVCNVWYLPP MTQQDGEDAV HFANRVKSAI
410 420 430 440
AHQGGLVDLS WDGGLKRSKV KESFKEEQQK MYSSMIVGLD SHEATVGPA
Length:449
Mass (Da):50,633
Last modified:August 16, 2004 - v1
Checksum:i94FF3F8FB2A04B7C
GO

Sequence cautioni

The sequence CAK05016.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX649525 Genomic DNA. Translation: CAK05016.1. Different initiation.
BC076515 mRNA. Translation: AAH76515.1.
RefSeqiNP_001002685.1. NM_001002685.1.
UniGeneiDr.106485.

Genome annotation databases

GeneIDi436958.
KEGGidre:436958.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX649525 Genomic DNA. Translation: CAK05016.1. Different initiation.
BC076515 mRNA. Translation: AAH76515.1.
RefSeqiNP_001002685.1. NM_001002685.1.
UniGeneiDr.106485.

3D structure databases

ProteinModelPortaliQ6DG38.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000115935.

Proteomic databases

PaxDbiQ6DG38.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi436958.
KEGGidre:436958.

Organism-specific databases

CTDi84803.
ZFINiZDB-GENE-040718-436. gpat3.

Phylogenomic databases

eggNOGiKOG2898. Eukaryota.
COG0204. LUCA.
HOGENOMiHOG000265725.
InParanoidiQ6DG38.
KOiK13506.
OMAiFVRYCVL.
OrthoDBiEOG70GMFG.
PhylomeDBiQ6DG38.
TreeFamiTF315039.

Enzyme and pathway databases

UniPathwayiUPA00282.
UPA00557; UER00612.

Miscellaneous databases

NextBioi20831382.
PROiQ6DG38.

Gene expression databases

BgeeiQ6DG38.

Family and domain databases

InterProiIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tuebingen.
  2. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiGPAT3_DANRE
AccessioniPrimary (citable) accession number: Q6DG38
Secondary accession number(s): Q1LVP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: August 16, 2004
Last modified: January 20, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Despite its name, the human ortholog of this protein appears to lack measurable glycerol-3-phosphate acyltransferase activity under some conditions (PMID:19318427).Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.