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8ZYR

Cryo-EM structure of BTN2A1-BTN3A1-BTN3A3

Functional Information from GO Data
ChainGOidnamespacecontents
A0001817biological_processregulation of cytokine production
A0005102molecular_functionsignaling receptor binding
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0009897cellular_componentexternal side of plasma membrane
A0016020cellular_componentmembrane
A0050852biological_processT cell receptor signaling pathway
B0001817biological_processregulation of cytokine production
B0001819biological_processpositive regulation of cytokine production
B0002250biological_processadaptive immune response
B0002376biological_processimmune system process
B0005102molecular_functionsignaling receptor binding
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0009897cellular_componentexternal side of plasma membrane
B0032729biological_processpositive regulation of type II interferon production
B0050798biological_processactivated T cell proliferation
B0050852biological_processT cell receptor signaling pathway
C0001817biological_processregulation of cytokine production
C0002250biological_processadaptive immune response
C0002376biological_processimmune system process
C0002456biological_processT cell mediated immunity
C0005102molecular_functionsignaling receptor binding
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0009897cellular_componentexternal side of plasma membrane
C0016020cellular_componentmembrane
C0050852biological_processT cell receptor signaling pathway
D0001817biological_processregulation of cytokine production
D0005102molecular_functionsignaling receptor binding
D0005886cellular_componentplasma membrane
D0006629biological_processlipid metabolic process
D0009897cellular_componentexternal side of plasma membrane
D0016020cellular_componentmembrane
D0050852biological_processT cell receptor signaling pathway
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues880
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues76
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues224
DetailsDomain: {"description":"Ig-like V-type"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues583
DetailsDomain: {"description":"B30.2/SPRY","evidences":[{"source":"PROSITE-ProRule","id":"PRU00548","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues241
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues218
DetailsDomain: {"description":"Ig-like V-type 1"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues182
DetailsDomain: {"description":"Ig-like V-type 2"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22846996","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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