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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8WRZ

Cry-EM structure of cannabinoid receptor-beta-arrestin-1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000785cellular_componentchromatin
A0001664molecular_functionG protein-coupled receptor binding
A0001934biological_processpositive regulation of protein phosphorylation
A0002029biological_processdesensitization of G protein-coupled receptor signaling pathway
A0002031biological_processG protein-coupled receptor internalization
A0002092biological_processpositive regulation of receptor internalization
A0003713molecular_functiontranscription coactivator activity
A0004402molecular_functionhistone acetyltransferase activity
A0004857molecular_functionenzyme inhibitor activity
A0005096molecular_functionGTPase activator activity
A0005159molecular_functioninsulin-like growth factor receptor binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005905cellular_componentclathrin-coated pit
A0006357biological_processregulation of transcription by RNA polymerase II
A0006511biological_processubiquitin-dependent protein catabolic process
A0007165biological_processsignal transduction
A0007600biological_processsensory perception
A0009968biological_processnegative regulation of signal transduction
A0010613biological_processpositive regulation of cardiac muscle hypertrophy
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0016567biological_processprotein ubiquitination
A0016604cellular_componentnuclear body
A0019899molecular_functionenzyme binding
A0030659cellular_componentcytoplasmic vesicle membrane
A0030666cellular_componentendocytic vesicle membrane
A0031143cellular_componentpseudopodium
A0031397biological_processnegative regulation of protein ubiquitination
A0031410cellular_componentcytoplasmic vesicle
A0031625molecular_functionubiquitin protein ligase binding
A0031701molecular_functionangiotensin receptor binding
A0032088biological_processnegative regulation of NF-kappaB transcription factor activity
A0032715biological_processnegative regulation of interleukin-6 production
A0032717biological_processnegative regulation of interleukin-8 production
A0035025biological_processpositive regulation of Rho protein signal transduction
A0042995cellular_componentcell projection
A0043149biological_processstress fiber assembly
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0045746biological_processnegative regulation of Notch signaling pathway
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0060090molecular_functionmolecular adaptor activity
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A1902533biological_processpositive regulation of intracellular signal transduction
A1990763molecular_functionarrestin family protein binding
R0004930molecular_functionG protein-coupled receptor activity
R0004949molecular_functioncannabinoid receptor activity
R0005506molecular_functioniron ion binding
R0007186biological_processG protein-coupled receptor signaling pathway
R0009055molecular_functionelectron transfer activity
R0016020cellular_componentmembrane
R0020037molecular_functionheme binding
R0022900biological_processelectron transport chain
R0042597cellular_componentperiplasmic space
R0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASVgSLFLIAIDRYIsI
ChainResidueDetails
RALA202-ILE218
site_idPS00295
Number of Residues19
DetailsARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL
ChainResidueDetails
APHE61-LEU79
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues41
DetailsRegion: {"description":"Interaction with CHRM2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BWG8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"27768894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27851727","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues30
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"27768894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27851727","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"27768894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27851727","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues39
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"27768894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27851727","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"27768894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27851727","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"27768894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27851727","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"27768894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27851727","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"27768894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27851727","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"27768894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27851727","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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