Q8IWJ2: GRIP and coiled-coil domain-containing protein 2 (GCC2)

GRIP and coiled-coil domain-containing protein 2 (GCC2) is a 1684-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8IWJ2.

Gene
GCC2
Organism
Homo sapiens
Length
1684 residues
Mean pLDDT
71.7
Model
AF-Q8IWJ2-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 71.7 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate0%
70 to 90Confident: backbone generally right74%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Golgin which probably tethers transport vesicles to the trans-Golgi network (TGN) and regulates vesicular transport between the endosomes and the Golgi. As a RAB9A effector it is involved in recycling of the mannose 6-phosphate receptor from the late endosomes to the TGN. May also play a role in transport between the recycling endosomes and the Golgi. Required for maintenance of the Golgi structure, it is involved in the biogenesis of noncentrosomal, Golgi-associated microtubules through recruitment of CLASP1 and CLASP2

Subunit structure

Homodimer. Interacts (via GRIP domain) with RAB6A (preferentially in its GTP-bound form). May interact (RAB6A-dependent) with ARL1; according to PubMed:19703403, RAB6A and ARL1 are not involved in GCC2 Golgi localization as proposed by PubMed:18243103. Interacts (probably via GRIP domain) with RAB9A (preferentially in its GTP-bound form). Interacts with CLASP1 and CLASP2; recruits both proteins…

Subcellular location

Cytoplasm, Golgi apparatus, trans-Golgi network membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3BBPX-ray3.0 ÅD/E/F=1547-1612

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