Q68F37

PR
Gene name
gpat3
Protein name
Glycerol-3-phosphate acyltransferase 3
Names
GPAT-3, 1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10, AGPAT 10, 1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9, 1-AGP acyltransferase 9, 1-AGPAT 9, Lysophosphatidic acid acyltransferase theta, LPAAT-theta
Species
Xenopus laevis (African clawed frog)
KEGG Pathway
xla:447316
EC number
2.3.1.15: Transferring groups other than amino-acyl groups
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

39-110 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q68F37

Entry ID Method Resolution Chain Position Source
AF-Q68F37-F1 Predicted AlphaFoldDB

No variants for Q68F37

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q68F37

No associated diseases with Q68F37

2 regional properties for Q68F37

Type Name Position InterPro Accession
domain Phospholipid/glycerol acyltransferase 217 - 341 IPR002123
domain Lysophosphatidylcholine acyltransferase LPCAT1-like 206 - 415 IPR045252

Functions

Description
EC Number 2.3.1.15 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

3 GO annotations of molecular function

Name Definition
1-acylglycerol-3-phosphate O-acyltransferase activity Catalysis of the reaction: acyl-CoA + 1-acyl-sn-glycerol-3-phosphate = CoA + 1,2-diacyl-sn-glycerol-3-phosphate.
glycerol-3-phosphate O-acyltransferase activity Catalysis of the reaction: acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.
sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity Catalysis of the reaction: hexadecanedioyl-CoA + sn-glycerol 3-phosphate = coenzyme A + 1-C16:0-alpha,omega-dicarboxyl-2-lysophosphatidate.

2 GO annotations of biological process

Name Definition
CDP-diacylglycerol biosynthetic process The chemical reactions and pathways resulting in the formation of CDP-diacylglycerol, CDP-1,2-diacylglycerol, a substance composed of diacylglycerol in glycosidic linkage with cytidine diphosphate.
triglyceride biosynthetic process The chemical reactions and pathways resulting in the formation of a triglyceride, any triester of glycerol.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEDFKTIACN IFIIWLTLVI VLILLPSMFG SSLGISEVYM KILVKVLEWA TLRIQKGFKD
70 80 90 100 110 120
KEKLSASNGI IQRDKSPMET EIECLRQSRS QDIREGDFEL GDVFYFAKKG FEAIVEDEVT
130 140 150 160 170 180
QRFSSEELIS WNLLTRTNNN FHYVSLRVTL IWVLGLCVRY CILLPLRITL ATIGISWLVL
190 200 210 220 230 240
GATLVGQLPN SRMKSWFSEL VHLMCCRICA RALSSAIQYH NKENKPKKGG ICVANHTSPI
250 260 270 280 290 300
DIIILANDGC YAMVGQVHGG LMGIIQRAMA RACPHVWFER SEMRDRHLVT ERLREHVSDK
310 320 330 340 350 360
SKLPILIFPE GTCINNTSVM MFKKGSFEIG GTIYPVAIKY DPQFGDAFWN SSKNSMVSYL
370 380 390 400 410 420
LRMMTSWALK CNVWYLPPVN RQDGEDAVQF ANRVKSAIAK QGGLVELPWD GGLKRGKVKD
430 440
SFKEEQQKNY SRIIAGENKS LKPTTH