P98192

PR
Gene name
Gnpat
Protein name
Dihydroxyacetone phosphate acyltransferase
Names
DAP-AT, DHAP-AT, Acyl-CoA:dihydroxyacetonephosphateacyltransferase, Glycerone-phosphate O-acyltransferase
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:14712
EC number
2.3.1.42: 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)

1-47 (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 P98192

Entry ID Method Resolution Chain Position Source
AF-P98192-F1 Predicted AlphaFoldDB

32 variants for P98192

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389019567 15 S>* No EVA
rs3389014635 71 K>N No EVA
rs3389020152 88 S>F No EVA
rs3399234891 107 E>* No EVA
rs3399234887 107 E>A No EVA
rs232985742 149 A>V No EVA
rs3388989211 165 I>S No EVA
rs3389021477 201 R>S No EVA
rs3389021661 203 S>F No EVA
rs3389014656 269 R>I No EVA
rs238797300 299 V>I No EVA
rs232701116 304 E>D No EVA
rs3389008362 322 S>R No EVA
rs3389017734 327 F>L No EVA
rs3413147386 337 A>P No EVA
rs226298950 342 N>S No EVA
rs3399804326 372 M>T No EVA
rs242775050 414 V>L No EVA
rs13470293 421 F>L No EVA
rs3389018487 451 Q>* No EVA
rs3389017767 455 K>I No EVA
rs3399419841 462 Q>H No EVA
rs3389001501 478 S>T No EVA
rs3388989235 486 N>S No EVA
rs3389013760 522 D>N No EVA
rs3399825800 529 G>E No EVA
rs3389021737 542 L>M No EVA
rs3412536961 550 M>I No EVA
rs3389025397 581 L>V No EVA
rs3389021675 630 L>* No EVA
rs3389008358 641 K>R No EVA
rs6372367 644 V>I No EVA

No associated diseases with P98192

3 regional properties for P98192

Type Name Position InterPro Accession
domain Phospholipid/glycerol acyltransferase 143 - 284 IPR002123
domain GPAT/DHAPAT, acyltransferase domain 133 - 338 IPR041728
domain GPAT/DHAPAT, C-terminal domain 292 - 646 IPR045520

Functions

Description
EC Number 2.3.1.42 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Peroxisome membrane ; Peripheral membrane protein ; Matrix side
  • Exclusively localized to the lumenal side of the peroxisomal membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
mitochondrial membrane Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
peroxisomal matrix The volume contained within the membranes of a peroxisome; in many cells the matrix contains a crystalloid core largely composed of urate oxidase.
peroxisomal membrane The lipid bilayer surrounding a peroxisome.
peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

2 GO annotations of molecular function

Name Definition
catalytic activity Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
glycerone-phosphate O-acyltransferase activity Catalysis of the reaction: acyl-CoA + glycerone phosphate = 1-acylglycerone 3-phosphate + CoA.

13 GO annotations of biological process

Name Definition
cerebellum morphogenesis The process in which the anatomical structure of the cerebellum is generated and organized. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. The cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills.
ether lipid biosynthetic process The chemical reactions and pathways resulting in the formation of ether lipids, lipids that contain (normally) one lipid alcohol in ether linkage to one of the carbon atoms (normally C-1) of glycerol.
fatty acid metabolic process The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
glycerophospholipid metabolic process The chemical reactions and pathways involving glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue.
membrane organization A process which results in the assembly, arrangement of constituent parts, or disassembly of a membrane. A membrane is a double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins.
myelination The process in which myelin sheaths are formed and maintained around neurons. Oligodendrocytes in the brain and spinal cord and Schwann cells in the peripheral nervous system wrap axons with compact layers of their plasma membrane. Adjacent myelin segments are separated by a non-myelinated stretch of axon called a node of Ranvier.
paranodal junction assembly Formation of the junction between an axon and the glial cell that forms the myelin sheath. Paranodal junctions form at each paranode, i.e. at the ends of the unmyelinated nodes of Ranvier.
phospholipid biosynthetic process The chemical reactions and pathways resulting in the formation of a phospholipid, a lipid containing phosphoric acid as a mono- or diester.
response to fatty acid Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a fatty acid stimulus.
response to nutrient Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nutrient stimulus.
response to starvation Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of nourishment.
response to xenobiotic stimulus Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a xenobiotic, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.
synapse assembly The aggregation, arrangement and bonding together of a set of components to form a synapse. This process ends when the synapse is mature (functional).

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q61586 Gpam Glycerol-3-phosphate acyltransferase 1, mitochondrial Mus musculus (Mouse) PR
10 20 30 40 50 60
MDVPSSSSSR FSVGSASPSS VLLYAKDLKK WDEFEDLLEE RRHISDFKFA MKCYTPPLYR
70 80 90 100 110 120
GITPCKPGDI KSIVLSSEEI NYVIKQLSRE SLTGVDVLRE EASEILEEMS HKLRIGAIRF
130 140 150 160 170 180
FAFVLSKIFK QIFSKVCVNE EGIQKLQRAV QEHPVVLLPS HRSYIDFLML SFILYSYDLP
190 200 210 220 230 240
VPVIAAGMDF LGMRVVSELL RMSGAFFMRR TFGGNKLYWA VFSEYVKTML RCGYAPVEFF
250 260 270 280 290 300
LEGTRSRAAK TLTPKFGLLN IVMEPFFKRE VFDTYFVPIS ISYDKILEES LYAYEILGVP
310 320 330 340 350 360
KPKESTTGLL KARRILSENF GSIHVYFGDP VSLRSLAAGR LNRNTYNLVP RCIPQKQPED
370 380 390 400 410 420
VQAFVTEVAY KMQLLQIENL ALSPWLLVVT ILLQNQLSMD FDALVEKTLW LKGVTQVFGG
430 440 450 460 470 480
FLLWPDNKLP EEVVQSSILL HSNLASLVKD QVVLKMNSGS SQVVNGLVPE HIALLMCSAY
490 500 510 520 530 540
RNQLLNIFAR PSLVALALHM TPGLRKEDVF SCFSFLRNVF SDEFIFLPGN TLRDFEEGCY
550 560 570 580 590 600
LLCKAEAMQM AGKDIILTDK GTAVLQFLTS LFKPFVESYQ LLCRYLLHEE DYFGEKEYLV
610 620 630 640 650 660
AARKFTRQLL DQGSSQCYDA LSSELQKNAL AAFVRLGVVE KKKVDSKYVY YVNGPATSKL
670
EEMLGCKKPI GKPATAKL