O60667: Immunoglobulin mu Fc receptor (FCMR)

Immunoglobulin mu Fc receptor (FCMR) is a 390-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O60667.

Gene
FCMR
Organism
Homo sapiens
Length
390 residues
Mean pLDDT
64.9
Model
AF-O60667-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 64.9 (low 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 accurate31%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution19%
Below 50Very low: often disordered regions42%

What pLDDT means and how to read it

Function

High-affinity Fc receptor for immunoglobulin M (IgM), both secreted and membrane-bound IgM (PubMed:19858324, PubMed:22675200, PubMed:36949194, PubMed:37095205). Primarily regulates IgM transport and homeostasis. In lymphoid cells, enables exocytosis of membrane-bound IgM on the plasma membrane as well as endocytosis of IgM-antigen complexes toward lysosomes for degradation. In mucosal epithelium, mediates retrotranscytosis of antigen-IgM complexes across mucosal M cells toward antigen-presenting cells in mucosal lymphoid tissues (PubMed:21908732, PubMed:28230186). Triggers costimulatory signaling and mediates most of IgM effector functions involved in B cell development and primary immune…

Subunit structure

Interacts (via Ig-like domain) with IGHM (via CH4/Cmu4 domain), both secreted and membrane-bound IgM; the interaction is glycan-independent and multivalent theoretically involving up to eight binding sites for the IgM pentamer

Subcellular location

Cell membrane, Early endosome membrane, Golgi apparatus, trans-Golgi network membrane, Lysosome membrane, Secreted

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7YTEX-ray3.0 ÅC/D=18-124
8BPGEM3.1 ÅA/B=18-251
7YSGEM3.18 ÅR/S/U/V=18-124
7YTCEM3.39 ÅR=18-124
8BPFEM3.5 ÅI=18-251
8BPEEM3.63 ÅI/M/N/O/P/Q/R/S=18-251
7YTDEM3.71 ÅR/S/U/V=18-124

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