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 O80458

Entry ID Method Resolution Chain Position Source
AF-O80458-F1 Predicted AlphaFoldDB

49 variants for O80458

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_2_9967734_G_C 3 S>C No 1000Genomes
tmp_2_9967732_G_C 4 L>V No 1000Genomes
ENSVATH05566276 13 S>P No 1000Genomes
tmp_2_9967674_A_G 23 L>P No 1000Genomes
ENSVATH13349160 24 F>Y No 1000Genomes
ENSVATH13349158 33 V>E No 1000Genomes
ENSVATH13349159 33 V>M No 1000Genomes
ENSVATH00243512 38 L>V No 1000Genomes
ENSVATH13349157 41 L>F No 1000Genomes
ENSVATH13349156 48 R>G No 1000Genomes
ENSVATH14537486 50 N>H No 1000Genomes
tmp_2_9967142_C_G 59 V>L No 1000Genomes
ENSVATH05566269 63 D>E No 1000Genomes
ENSVATH13349129 70 M>I No 1000Genomes
tmp_2_9967099_T_G 73 H>P No 1000Genomes
ENSVATH05566267 79 D>Y No 1000Genomes
ENSVATH14537482 84 W>* No 1000Genomes
ENSVATH14537481 89 G>R No 1000Genomes
tmp_2_9967043_T_C 92 T>A No 1000Genomes
ENSVATH05566266 94 Q>R No 1000Genomes
ENSVATH05566265 108 E>D No 1000Genomes
tmp_2_9966944_T_A 125 T>S No 1000Genomes
tmp_2_9966932_C_T 129 G>R No 1000Genomes
ENSVATH01874545 133 I>T No 1000Genomes
tmp_2_9966812_G_C 143 Q>E No 1000Genomes
tmp_2_9966689_G_T 157 S>* No 1000Genomes
tmp_2_9966690_A_T 157 S>T No 1000Genomes
tmp_2_9966684_C_A 159 V>F No 1000Genomes
tmp_2_9966662_T_C 166 N>S No 1000Genomes
tmp_2_9966657_T_A 168 T>S No 1000Genomes
tmp_2_9966633_T_G 176 K>Q No 1000Genomes
tmp_2_9966632_T_C 176 K>R No 1000Genomes
tmp_2_9966628_T_A 177 E>D No 1000Genomes
tmp_2_9966629_T_A 177 E>V No 1000Genomes
tmp_2_9966624_G_T 179 H>N No 1000Genomes
ENSVATH13349112 192 H>Q No 1000Genomes
ENSVATH05566260 195 M>V No 1000Genomes
tmp_2_9966570_C_G 197 V>L No 1000Genomes
tmp_2_9966558_C_T 201 G>R No 1000Genomes
tmp_2_9966554_T_C 202 K>R No 1000Genomes
ENSVATH05566257 218 K>N No 1000Genomes
ENSVATH05566256 222 R>Q No 1000Genomes
ENSVATH14537476 229 A>T No 1000Genomes
ENSVATH05566254 268 S>T No 1000Genomes
tmp_2_9966344_A_T 272 F>Y No 1000Genomes
ENSVATH01874536 274 P>L No 1000Genomes
ENSVATH13349108 276 F>L No 1000Genomes
ENSVATH05566253 287 E>K No 1000Genomes
ENSVATH13349105 294 R>S No 1000Genomes

No associated diseases with O80458

1 regional properties for O80458

Type Name Position InterPro Accession
conserved_site Di-trans-poly-cis-decaprenylcistransferase-like, conserved site 246 - 263 IPR018520

Functions

Description
EC Number 2.5.1.87 Transferring alkyl or aryl groups, other than methyl groups
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
chloroplast stroma The space enclosed by the double membrane of a chloroplast but excluding the thylakoid space. It contains DNA, ribosomes and some temporary products of photosynthesis.
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.

2 GO annotations of molecular function

Name Definition
dehydrodolichyl diphosphate synthase activity Catalysis of the condensation of isopentenyl diphosphate and farnesyl diphosphate in the cis-configuration to form dehydrodolichyl diphosphate.
polyprenyltransferase activity Catalysis of the transfer of multiple prenyl groups from one compound (donor) to another (acceptor).

5 GO annotations of biological process

Name Definition
dolichol biosynthetic process The chemical reactions and pathways resulting in the formation of dolichols, any 2,3-dihydropolyprenol derived from four or more linked isoprene units.
plastid membrane organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of either of the lipid bilayers surrounding a plastid.
polyprenol biosynthetic process The chemical reactions and pathways resulting in the formation of polyprenols, prenols with more than 4 isoprenoid residues, which may be all-trans, or a mixture of cis and trans.
protein glycosylation A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins.
response to cold 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 cold stimulus, a temperature stimulus below the optimal temperature for that organism.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q86SQ9 DHDDS Dehydrodolichyl diphosphate synthase complex subunit DHDDS Homo sapiens (Human) PR
Q570Q8 At5g58784 Dehydrodolichyl diphosphate synthase 5 Arabidopsis thaliana (Mouse-ear cress) PR
Q8GY03 At5g58782 Dehydrodolichyl diphosphate synthase 4 Arabidopsis thaliana (Mouse-ear cress) PR
Q8LAR7 At5g60510 Dehydrodolichyl diphosphate synthase 8 Arabidopsis thaliana (Mouse-ear cress) PR
Q8RX73 At5g58780 Dehydrodolichyl diphosphate synthase 3 Arabidopsis thaliana (Mouse-ear cress) PR
Q56Y11 At5g58770 Dehydrodolichyl diphosphate synthase 2 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MLSLLSSDSS LLSLLFLFLI PCLFITSYIG FPVFLLKLIG LIKIKAARDN EKRDEGTYVV
70 80 90 100 110 120
REDGLQRELM PRHVAFILDG NRRWAKRAGL TTSQGHEAGA KRLIDIAELC FELGVHTVSA
130 140 150 160 170 180
FAFSTENWGR DKIEIDNLMS LIQHYRNKSN IKFFHRSEVR VSVIGNKTKI PESLLKEIHE
190 200 210 220 230 240
IEEATKGYKN KHLIMAVDYS GKFDIMHACK SLVKKSEKGL IREEDVDEAL IERELLTNCS
250 260 270 280 290 300
DFPSPDLMIR TSGEQRISNF FLWQLAYSEL FFSPVFWPDF DKDKLLEALA SYQRRERRFG
CRV