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22CR

C5a-desArg bound C5aR2 in complex with beta-arrestin1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000822molecular_functioninositol hexakisphosphate binding
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
A0005102molecular_functionsignaling receptor binding
A0005515molecular_functionprotein binding
A0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005905cellular_componentclathrin-coated pit
A0006511biological_processubiquitin-dependent protein catabolic process
A0006898biological_processreceptor-mediated endocytosis
A0007600biological_processsensory perception
A0008277biological_processregulation of G protein-coupled receptor signaling pathway
A0009968biological_processnegative regulation of signal transduction
A0030132cellular_componentclathrin coat of coated pit
A0030276molecular_functionclathrin binding
A0031143cellular_componentpseudopodium
A0031410cellular_componentcytoplasmic vesicle
A0031623biological_processreceptor internalization
A0032050molecular_functionclathrin heavy chain binding
A0033130molecular_functionacetylcholine receptor binding
A0035612molecular_functionAP-2 adaptor complex binding
A0036094molecular_functionsmall molecule binding
A0045746biological_processnegative regulation of Notch signaling pathway
A0045880biological_processpositive regulation of smoothened signaling pathway
A0060090molecular_functionmolecular adaptor activity
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A0072583biological_processclathrin-dependent endocytosis
A0097499biological_processprotein localization to non-motile cilium
R0002430biological_processcomplement receptor mediated signaling pathway
R0004878molecular_functioncomplement component C5a receptor activity
R0004930molecular_functionG protein-coupled receptor activity
R0005515molecular_functionprotein binding
R0005886cellular_componentplasma membrane
R0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
R0007204biological_processpositive regulation of cytosolic calcium ion concentration
R0009925cellular_componentbasal plasma membrane
R0016323cellular_componentbasolateral plasma membrane
R0032677biological_processregulation of interleukin-8 production
R0032715biological_processnegative regulation of interleukin-6 production
R0032720biological_processnegative regulation of tumor necrosis factor production
R0038178biological_processcomplement component C5a signaling pathway
R0045177cellular_componentapical part of cell
R0090024biological_processnegative regulation of neutrophil chemotaxis
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
LTYR193-HIS199
HTYR204-HIS210

site_idPS00295
Number of Residues19
DetailsARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL
ChainResidueDetails
APHE61-LEU79

site_idPS01177
Number of Residues35
DetailsANAPHYLATOXIN_1 Anaphylatoxin domain signature. CCydGarvnnde.TCEqraarisl.GprCikafte.CC
ChainResidueDetails
CCYS21-CYS55

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsDomain: {"description":"Anaphylatoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00022","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues29
DetailsRegion: {"description":"Involved in C5AR1 binding","evidences":[{"source":"PubMed","id":"9553099","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18536718","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CU7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KLS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KM9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues32
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues60
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q695P6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues41
DetailsRegion: {"description":"Interaction with CHRM2"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BWG8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

259987

PDB entries from 2026-09-23

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