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 Q99L43

Entry ID Method Resolution Chain Position Source
AF-Q99L43-F1 Predicted AlphaFoldDB

23 variants for Q99L43

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388591909 47 V>L No EVA
rs27261259 80 A>T No EVA
rs3388594732 104 C>F No EVA
rs3388594732 104 C>S No EVA
rs3392085034 118 S>Y No EVA
rs3388594367 125 R>S No EVA
rs3388586832 128 S>T No EVA
rs3388591863 146 D>G No EVA
rs3388596048 150 T>I No EVA
rs3392218078 152 V>D No EVA
rs3388587433 208 T>K No EVA
rs3388597971 232 I>V No EVA
rs3388596003 256 K>E No EVA
rs3388581131 260 E>V No EVA
rs3388587900 279 V>A No EVA
rs3392218030 287 V>A No EVA
rs3388586849 297 N>K No EVA
rs246560522 339 I>V No EVA
rs3388596898 342 S>F No EVA
rs3388594239 354 F>I No EVA
rs3388587434 371 T>S No EVA
rs3388587915 402 G>S No EVA
rs3388592919 411 Q>R No EVA

No associated diseases with Q99L43

No regional properties for Q99L43

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q99L43

Functions

Description
EC Number 2.7.7.41 Nucleotidyltransferases
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.

1 GO annotations of molecular function

Name Definition
phosphatidate cytidylyltransferase activity Catalysis of the reaction: CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

4 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.
glycosylation The covalent attachment and further modification of carbohydrate residues to a substrate molecule.
lipid droplet formation A process that results in the assembly, arrangement of constituent parts of a lipid droplet.
phototransduction The sequence of reactions within a cell required to convert absorbed photons into a molecular signal.

9 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P38221 CDS1 Phosphatidate cytidylyltransferase Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
A0JNC1 CDS2 Phosphatidate cytidylyltransferase 2 Bos taurus (Bovine) PR
P56079 Cds Phosphatidate cytidylyltransferase, photoreceptor-specific Drosophila melanogaster (Fruit fly) PR
Q92903 CDS1 Phosphatidate cytidylyltransferase 1 Homo sapiens (Human) PR
O95674 CDS2 Phosphatidate cytidylyltransferase 2 Homo sapiens (Human) PR
P98191 Cds1 Phosphatidate cytidylyltransferase 1 Mus musculus (Mouse) PR
O35052 Cds1 Phosphatidate cytidylyltransferase 1 Rattus norvegicus (Rat) PR
Q91XU8 Cds2 Phosphatidate cytidylyltransferase 2 Rattus norvegicus (Rat) PR
Q1PE48 CDS3 Phosphatidate cytidylyltransferase 3 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MTELRQRVVR EDAPPEDKES ESEAKLDGET ASDSESRAET APLPTSVDDT PEVLNRALSN
70 80 90 100 110 120
LSSRWKNWWV RGILTLAMIA FFFIIIYLGP MVLMMIVMCV QIKCFHEIIT IGYNVYHSYD
130 140 150 160 170 180
LPWFRTLSWY FLLCVNYFFY GETVTDYFFT LVQREEPLRI LSKYHRFISF ALYLTGFCMF
190 200 210 220 230 240
VLSLVKKHYR LQFYMFGWTH VTLLIVVTQS HLVIHNLFEG MIWFIVPISC VICNDIMAYM
250 260 270 280 290 300
FGFFFGRTPL IKLSPKKTWE GFIGGFFATV VFGLLLSYVM SGYRCFVCPV EYNNDTNSFT
310 320 330 340 350 360
VDCEPSDLFR LQEYNIPGVI QSAIGWKTVR MYPFQIHSIA LSTFASLIGP FGGFFASGFK
370 380 390 400 410 420
RAFKIKDFAN TIPGHGGIMD RFDCQYLMAT FVNVYIASFI RGPNPSKLIQ QFLTLRPDQQ
430 440
LHIFNTLKSH LTDKGILTSA LEDE