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9UYL

Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 1 (Conformation 4)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000785cellular_componentchromatin
A0001664molecular_functionG protein-coupled receptor binding
A0001678biological_processintracellular glucose homeostasis
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
A0006351biological_processDNA-templated transcription
A0006357biological_processregulation of transcription by RNA polymerase II
A0006511biological_processubiquitin-dependent protein catabolic process
A0007166biological_processcell surface receptor signaling pathway
A0007600biological_processsensory perception
A0009968biological_processnegative regulation of signal transduction
A0010613biological_processpositive regulation of cardiac muscle hypertrophy
A0015031biological_processprotein transport
A0016567biological_processprotein ubiquitination
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
A0032715biological_processnegative regulation of interleukin-6 production
A0032717biological_processnegative regulation of interleukin-8 production
A0035025biological_processpositive regulation of Rho protein signal transduction
A0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
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
R0005515molecular_functionprotein binding
R0005886cellular_componentplasma membrane
R0007154biological_processcell communication
R0007165biological_processsignal transduction
R0007186biological_processG protein-coupled receptor signaling pathway
R0007218biological_processneuropeptide signaling pathway
R0023052biological_processsignaling
R0042593biological_processglucose homeostasis
R0042923molecular_functionneuropeptide binding
R0043005cellular_componentneuron projection
R0050727biological_processregulation of inflammatory response
R0097003molecular_functionadipokinetic hormone receptor activity
R0097004molecular_functionadipokinetic hormone binding
Functional Information from PROSITE/UniProt
site_idPS00295
Number of Residues19
DetailsARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL
ChainResidueDetails
APHE61-LEU79

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues41
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues53
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues34
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues11
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BWG8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247035

PDB entries from 2026-01-07

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