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 Q03175

Entry ID Method Resolution Chain Position Source
AF-Q03175-F1 Predicted AlphaFoldDB

7 variants for Q03175

Variant ID(s) Position Change Description Diseaes Association Provenance
s13-469390 29 V>A No SGRP
s13-469363 38 A>E No SGRP
s13-469319 53 L>F No SGRP
s13-469004 158 G>R No SGRP
s13-468991 162 R>T No SGRP
s13-468764 238 H>Y No SGRP
s13-468493 328 Y>C No SGRP

No associated diseases with Q03175

1 regional properties for Q03175

Type Name Position InterPro Accession
conserved_site Di-trans-poly-cis-decaprenylcistransferase-like, conserved site 243 - 260 IPR018520

Functions

Description
EC Number 2.5.1.87 Transferring alkyl or aryl groups, other than methyl groups
Subcellular Localization
  • Lipid droplet
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
dehydrodolichyl diphosphate synthase complex A protein complex which is capable of dehydrodolichyl diphosphate synthase activity.
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).
intrinsic component of membrane The component of a membrane consisting of the gene products having some covalently attached portion, for example part of a peptide sequence or some other covalently attached group such as a GPI anchor, which spans or is embedded in one or both leaflets of the membrane.
lipid droplet An intracellular non-membrane-bounded organelle comprising a matrix of coalesced lipids surrounded by a phospholipid monolayer. May include associated proteins.

3 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).
prenyltransferase activity Catalysis of the transfer of a prenyl group from one compound (donor) to another (acceptor).

3 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.
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.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P35196 RER2 Dehydrodolichyl diphosphate synthase complex subunit RER2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q86SQ9 DHDDS Dehydrodolichyl diphosphate synthase complex subunit DHDDS Homo sapiens (Human) PR
Q8LAR7 At5g60510 Dehydrodolichyl diphosphate synthase 8 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MKMPSIIQIQ FVALKRLLVE TKEQMCFAVK SIFQRVFAWV MSLSLFSWFY VNLQNILIKA
70 80 90 100 110 120
LRVGPVPEHV SFIMDGNRRY AKSRRLPVKK GHEAGGLTLL TLLYICKRLG VKCVSAYAFS
130 140 150 160 170 180
IENFNRPKEE VDTLMNLFTV KLDEFAKRAK DYKDPLYGSK IRIVGDQSLL SPEMRKKIKK
190 200 210 220 230 240
VEEITQDGDD FTLFICFPYT SRNDMLHTIR DSVEDHLENK SPRINIRKFT NKMYMGFHSN
250 260 270 280 290 300
KCELLIRTSG HRRLSDYMLW QVHENATIEF SDTLWPNFSF FAMYLMILKW SFFSTIQKYN
310 320 330 340
EKNHSLFEKI HESVPSIFKK KKTAMSLYNF PNPPISVSVT GDE