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 Q9DCI3

Entry ID Method Resolution Chain Position Source
AF-Q9DCI3-F1 Predicted AlphaFoldDB

8 variants for Q9DCI3

Variant ID(s) Position Change Description Diseaes Association Provenance
rs49524883 7 H>D No EVA
rs3389239605 22 L>Q No EVA
rs3389286866 29 N>S No EVA
rs3389282779 31 A>T No EVA
rs3389273918 45 K>N No EVA
rs3389202015 123 W>C No EVA
rs3389273807 169 W>* No EVA
rs3389256410 207 Q>* No EVA

No associated diseases with Q9DCI3

1 regional properties for Q9DCI3

Type Name Position InterPro Accession
domain MENTAL domain 48 - 218 IPR019498

Functions

Description
EC Number
Subcellular Localization
  • Late endosome membrane ; Multi-pass membrane protein
  • Localizes to contact sites between the endoplasmic reticulum and late endosomes: associates with the endoplasmic reticulum membrane via interaction with VAPA, VAPB or MOSPD2
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
endoplasmic reticulum-endosome membrane contact site A contact site between the endoplasmic reticulum membrane and the endosome membrane.
endosome A vacuole to which materials ingested by endocytosis are delivered.
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.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
late endosome membrane The lipid bilayer surrounding a late endosome.
organelle membrane contact site A zone of apposition between the membranes of an organelle with another membrane, either another membrane of the same organelle, a membrane of another organelle, or the plasma membrane. Membrane contact sites (MCSs) are structured by bridging complexes. They are specialized for communication, including the efficient traffic of small molecules such as Ca2+ ions and lipids, as well as enzyme-substrate interactions.

2 GO annotations of molecular function

Name Definition
cholesterol binding Binding to cholesterol (cholest-5-en-3-beta-ol); the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
protein homodimerization activity Binding to an identical protein to form a homodimer.

2 GO annotations of biological process

Name Definition
cholesterol transport The directed movement of cholesterol, cholest-5-en-3-beta-ol, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
vesicle tethering to endoplasmic reticulum The initial, indirect interaction between a transport vesicle membrane and the membrane of the endoplasmic reticulum. This interaction is mediated by tethering factors (or complexes), which interact with both membranes. Interaction can occur via direct binding to membrane phospholipids or membrane proteins, or via binding to vesicle coat proteins. This process is distinct from and prior fusion.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q14849 STARD3 StAR-related lipid transfer protein 3 Homo sapiens (Human) PR
O95772 STARD3NL STARD3 N-terminal-like protein Homo sapiens (Human) PR
Q61542 Stard3 StAR-related lipid transfer protein 3 Mus musculus (Mouse) PR
O17883 strl-1 Steroidogenic acute regulatory-like protein 1 Caenorhabditis elegans PR
10 20 30 40 50 60
MNHLPEHMEN TLTGSQSSHA SLRDIHSINP AQLMARIESY EGREKKGISD VRRTFCLFVT
70 80 90 100 110 120
FDLLFVTLLW IIELNVNGGI ENTLKKEVIH YDYYSSYFDI FLLAVFRFKV LILGYAVCRL
130 140 150 160 170 180
RHWWAIALTT AVTSAFLLAK VILSKLFSQG AFGYVLPIIS FILAWIETWF LDFKVLPQEA
190 200 210 220 230
EEENRLLLVQ DASERAALIP AGLSDGQFYS PPESEAGSEE EAEEKQESEK PLLEL