Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P33333

Entry ID Method Resolution Chain Position Source
AF-P33333-F1 Predicted AlphaFoldDB

5 variants for P33333

Variant ID(s) Position Change Description Diseaes Association Provenance
s04-363511 25 F>L No SGRP
44 Q>L allele suppressor SLC1-1 [UniProt] No
s04-363256 110 V>F No SGRP
s04-363194 130 R>S No SGRP
s04-362864 240 D>E No SGRP

No associated diseases with P33333

2 regional properties for P33333

Type Name Position InterPro Accession
domain Phospholipid/glycerol acyltransferase 63 - 193 IPR002123
domain 1-acyl-sn-glycerol-3-phosphate acyltransferase 60 - 191 IPR004552

Functions

Description
EC Number 2.3.1.23 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Lipid droplet
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).
lipid droplet An intracellular non-membrane-bounded organelle comprising a matrix of coalesced lipids surrounded by a phospholipid monolayer. May include associated proteins.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

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.
1-acylglycerophosphocholine O-acyltransferase activity Catalysis of the reaction: 1-acyl-sn-glycero-3-phosphocholine + acyl-CoA = phosphatidylcholine + CoA.
1-acylglycerophosphoethanolamine O-acyltransferase activity Catalysis of the reaction: a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA.

3 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.
glycerophospholipid biosynthetic process The chemical reactions and pathways resulting in the formation of glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue.
phosphatidic acid biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q95JH2 AGPAT1 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha Bos taurus (Bovine) PR
Q99943 AGPAT1 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha Homo sapiens (Human) PR
O15120 AGPAT2 1-acyl-sn-glycerol-3-phosphate acyltransferase beta Homo sapiens (Human) PR
Q8K3K7 Agpat2 1-acyl-sn-glycerol-3-phosphate acyltransferase beta Mus musculus (Mouse) PR
Q9LLY4 BAT2 1-acyl-sn-glycerol-3-phosphate acyltransferase BAT2, chloroplastic Brassica napus (Rape) PR
Q8GXU8 LPAT1 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSVIGRFLYY LRSVLVVLAL AGCGFYGVIA SILCTLIGKQ HLAQWITARC FYHVMKLMLG
70 80 90 100 110 120
LDVKVVGEEN LAKKPYIMIA NHQSTLDIFM LGRIFPPGCT VTAKKSLKYV PFLGWFMALS
130 140 150 160 170 180
GTYFLDRSKR QEAIDTLNKG LENVKKNKRA LWVFPEGTRS YTSELTMLPF KKGAFHLAQQ
190 200 210 220 230 240
GKIPIVPVVV SNTSTLVSPK YGVFNRGCMI VRILKPISTE NLTKDKIGEF AEKVRDQMVD
250 260 270 280 290 300
TLKEIGYSPA INDTTLPPQA IEYAALQHDK KVNKKIKNEP VPSVSISNDV NTHNEGSSVK
KMH