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 Q6NVG1

Entry ID Method Resolution Chain Position Source
AF-Q6NVG1-F1 Predicted AlphaFoldDB

18 variants for Q6NVG1

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388578419 60 L>I No EVA
rs3413066165 82 T>K No EVA
rs3388568832 146 V>I No EVA
rs3388579937 166 Q>* No EVA
rs27463438 276 L>P No EVA
rs107616303 330 A>G No EVA
rs3391769623 338 L>M No EVA
rs3392077345 339 S>P No EVA
rs3388579971 375 A>G No EVA
rs3388572512 406 E>K No EVA
rs3388575482 411 L>M No EVA
rs3388579985 416 F>I No EVA
rs3388572055 473 S>C No EVA
rs3388579976 480 G>C No EVA
rs3388579935 483 F>S No EVA
rs3388572487 493 P>T No EVA
rs3388575463 504 S>F No EVA
rs3388576262 513 N>K No EVA

No associated diseases with Q6NVG1

2 regional properties for Q6NVG1

Type Name Position InterPro Accession
domain Phospholipid/glycerol acyltransferase 108 - 234 IPR002123
domain Lysophosphatidylcholine acyltransferase LPCAT1-like 109 - 306 IPR045252

Functions

Description
EC Number 2.3.1.23 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.

6 GO annotations of molecular function

Name Definition
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.
1-acylglycerophosphoserine O-acyltransferase activity Catalysis of the reaction:a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CoA.
1-alkenylglycerophosphoethanolamine O-acyltransferase activity Catalysis of the reaction: 1-alkenylglycerophosphoethanolamine + acyl-CoA = 1-alkenyl-2-acyl-glycerophosphoethanolamine + CoA.
1-alkylglycerophosphocholine O-acetyltransferase activity Catalysis of the reaction: 1-alkyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + CoA.
lysophospholipid acyltransferase activity Catalysis of the transfer of acyl groups from an acyl-CoA to a lysophospholipid.

5 GO annotations of biological process

Name Definition
phosphatidylcholine acyl-chain remodeling Remodeling the acyl chains of phosphatidylcholine, through sequential deacylation and re-acylation reactions, to generate phosphatidylcholine containing different types of fatty acid acyl chains.
phosphatidylethanolamine acyl-chain remodeling Remodeling the acyl chains of phosphatidylethanolamine, through sequential deacylation and re-acylation reactions, to generate phosphatidylethanolamine containing different types of fatty acid acyl chains.
phosphatidylserine acyl-chain remodeling Remodeling the acyl chains of phosphatidylserine, through sequential deacylation and re-acylation reactions, to generate phosphatidylserine containing different types of fatty acid acyl chains.
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.
phospholipid metabolic process The chemical reactions and pathways involving phospholipids, any lipid containing phosphoric acid as a mono- or diester.

8 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8NF37 LPCAT1 Lysophosphatidylcholine acyltransferase 1 Homo sapiens (Human) PR
Q8C0N2 Gpat3 Glycerol-3-phosphate acyltransferase 3 Mus musculus (Mouse) PR
Q8K2C8 Gpat4 Glycerol-3-phosphate acyltransferase 4 Mus musculus (Mouse) PR
Q3TFD2 Lpcat1 Lysophosphatidylcholine acyltransferase 1 Mus musculus (Mouse) PR
Q1HAQ0 Lpcat1 Lysophosphatidylcholine acyltransferase 1 Rattus norvegicus (Rat) PR
Q8L7R3 LPEAT1 Lysophospholipid acyltransferase LPEAT1 Arabidopsis thaliana (Mouse-ear cress) PR
Q8S8S2 LPEAT2 Lysophospholipid acyltransferase LPEAT2 Arabidopsis thaliana (Mouse-ear cress) PR
Q1LWG4 lpcat1 Lysophosphatidylcholine acyltransferase 1 Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MSQGSPGAWA PLDPTSGSSA SPNPFVHELH LSGLQRVKFC LLGVLLAPIR VLLAFIVLFL
70 80 90 100 110 120
LWPFAWLQVA GLTEEQLQEP ITGWRKTVCH NGVLGLSRLL FFLLGFLRIR VRGQRASRLE
130 140 150 160 170 180
APVLVAAPHS TFFDPIVLLP CDLPKVVSRA ENLSVPVIGA LLRFNQAILV SRHDPASRRR
190 200 210 220 230 240
VVEEVRRRAT SGGKWPQVLF FPEGTCSNKK ALLKFKPGAF IAGVPVQPVL IRYPNSLDTT
250 260 270 280 290 300
SWAWRGPGVL KVLWLTASQP CSIVDVEFLP VYQPSLEESK DPTLYANNVQ RVMAQALGIP
310 320 330 340 350 360
ATECEFVGSL PVIVVGQLKV ALEPQLWELA KVLQKAGLSP GFVDMGAEPG RSRMISQEAF
370 380 390 400 410 420
AQQLQLSDPQ TVAGAFSYFQ QDAKGLVDFR NVALALAALD GGRSLEELTR LAFELFAEEQ
430 440 450 460 470 480
AEGSDRLLYK DGFSTILHLL LGSPRPAATT LHAELCQPGC SQGLSLCQFQ NFSLHDPLYG
490 500 510 520
KLFSAYLRPP HKPRSTSQIP NASSPSSPTA LANGTVQAPK QKGD