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 O35052

Entry ID Method Resolution Chain Position Source
AF-O35052-F1 Predicted AlphaFoldDB

3 variants for O35052

Variant ID(s) Position Change Description Diseaes Association Provenance
rs8174641 172 R>K No EVA
rs8174642 326 L>V No EVA
rs8165620 457 P>H No EVA

No associated diseases with O35052

No regional properties for O35052

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O35052

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.
lipid droplet formation A process that results in the assembly, arrangement of constituent parts of a lipid droplet.
phosphatidylinositol biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
positive regulation of fat cell differentiation Any process that activates or increases the frequency, rate or extent of adipocyte differentiation.

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
O95674 CDS2 Phosphatidate cytidylyltransferase 2 Homo sapiens (Human) PR
Q92903 CDS1 Phosphatidate cytidylyltransferase 1 Homo sapiens (Human) PR
P98191 Cds1 Phosphatidate cytidylyltransferase 1 Mus musculus (Mouse) PR
Q99L43 Cds2 Phosphatidate cytidylyltransferase 2 Mus musculus (Mouse) 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
MLELRHRGGC PGPGGAGTPP PREGEAAGGD HETESTSDKE TDIDDRYGDL DARGDSDVPE
70 80 90 100 110 120
VPPSSDRTPE ILKKALSGLS SRWKNWWIRG ILTLTMISLF FLIIYMGSFM LMLLVLGIQV
130 140 150 160 170 180
KCFQEIITIG YRVYHSYDLP WFRTLSWYFL LCVNYFFYGE TVADYFATFV QREEQLQFLI
190 200 210 220 230 240
RYHRFISFAL YLAGFCMFVL SLVKKHYRLQ FYMFAWTHVT LLITVTQSHL VIQNLFEGMI
250 260 270 280 290 300
WFLVPISSVI CNDITAYLFG FFFGRTPLIK LSPKKTWEGF IGGFFSTVIF GFIAAYVLSK
310 320 330 340 350 360
YQYFVCPVEY RSDVNSFVTE CEPSELFQLQ NYSLPPFLQA VLSRETVSLY PFQIHSIALS
370 380 390 400 410 420
TFASLIGPFG GFFASGFKRA FKIKDFANTI PGHGGIMDRF DCQYLMATFV HVYITSFIRG
430 440 450 460
PNPSKVLQQL LVLQPEQQLN IYRTLKIHLT EKGILQPTWK V