C3AR_PONAB
ID C3AR_PONAB Reviewed; 482 AA.
AC Q5REI5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=C3a anaphylatoxin chemotactic receptor;
DE Short=C3AR;
DE Short=C3a-R;
GN Name=C3AR1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for the chemotactic and inflammatory peptide
CC anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme
CC release and superoxide anion production (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with VGF-derived peptide TLQP-21 (By similarity).
CC {ECO:0000250|UniProtKB:O09047}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- PTM: Among the sulfation sites Tyr-174 is essential for binding of C3a
CC anaphylatoxin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; CR857543; CAH89822.1; -; mRNA.
DR RefSeq; NP_001124844.1; NM_001131372.1.
DR AlphaFoldDB; Q5REI5; -.
DR SMR; Q5REI5; -.
DR STRING; 9601.ENSPPYP00000004833; -.
DR GeneID; 100171704; -.
DR KEGG; pon:100171704; -.
DR CTD; 719; -.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR InParanoid; Q5REI5; -.
DR OrthoDB; 1003587at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004876; F:complement component C3a receptor activity; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR InterPro; IPR001644; Anaphtx_C3AR1.
DR InterPro; IPR002234; Anphylx_rcpt.
DR InterPro; IPR000826; Formyl_rcpt-rel.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24225; PTHR24225; 1.
DR PANTHER; PTHR24225:SF28; PTHR24225:SF28; 1.
DR Pfam; PF00001; 7tm_1; 2.
DR PRINTS; PR01104; ANPHYLATOXNR.
DR PRINTS; PR01060; C3ANPHYLTXNR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Sulfation; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..482
FT /note="C3a anaphylatoxin chemotactic receptor"
FT /id="PRO_0000269719"
FT TOPO_DOM 1..23
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..360
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..400
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 174
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 184
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 318
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09047"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O09047"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 482 AA; 54013 MW; FA92F753594A00A5 CRC64;
MASFSAETNS TDLLSQPWNE PPVILSMVIL SLTFLLGLPG NGLVLWVAGL KMQRTVNTVW
FLHLTLADLL CCLSLPFSLA HLALQGQWPY GRFLCELIPS IIVLNMFASV FLLTAISLDR
CLVVFKPIWC QNHRNVGTAC SICGCIWVVA FVMCIPVFVY REIFTADNHN RCGYKFGLSS
SLDYPDFYGD PLENRSLENI VQLPGEMNDR LDPSSFQTND HPWTVPTVFQ PQTFQRPSAD
SLHRDSARLT SQNLYSNVFK PADVVSPKIP SGFPIKDQET SPLDNSDAFL STHLKLFPSA
SSNSFYESEL PQDFQDYYNL GQFEDDNQVP TPLVAITITR LVVGFLLPSV IMIACYSFIV
FRMQRGRFAK SQSKTFRVAV VVVAVFLVCW TPYHIFGVLS LLIDPESPLG KTLMSWDHVS
IALASANSCF NPFLYALLGK DFRKKARQSI QGILEAAFSE ELTRSTHCNS NNVFSERNST
TV
