GPR33_PANTR
ID GPR33_PANTR Reviewed; 333 AA.
AC Q49SQ3; Q49SQ4; Q49SQ5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable G-protein coupled receptor 33;
GN Name=GPR33;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15987686; DOI=10.1074/jbc.m503586200;
RA Roempler H., Schulz A., Pitra C., Coop G., Przeworski M., Paeaebo S.,
RA Schoeneberg T.;
RT "The rise and fall of the chemoattractant receptor GPR33.";
RL J. Biol. Chem. 280:31068-31075(2005).
CC -!- FUNCTION: Orphan receptor; could be a chemoattractant receptor.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- POLYMORPHISM: In some individuals a nonsense mutation transforms either
CC Ser-39 or Arg-140 into a premature stop codon. GPR33 has undergone
CC independent pseudogenization in human, chimpanzee, orangutan and rat.
CC This selective inactivation may be due to its interaction with a
CC putative pathogen that could use GPR33 as a receptor for cell invasion.
CC {ECO:0000305|PubMed:15987686}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY493991; AAR98750.1; -; Genomic_DNA.
DR EMBL; AY493993; AAR98751.1; -; Genomic_DNA.
DR EMBL; AY493995; AAR98752.1; -; Genomic_DNA.
DR RefSeq; NP_001074257.2; NM_001080788.2.
DR RefSeq; XP_009425731.1; XM_009427456.1.
DR AlphaFoldDB; Q49SQ3; -.
DR SMR; Q49SQ3; -.
DR STRING; 9598.ENSPTRP00000054852; -.
DR PaxDb; Q49SQ3; -.
DR Ensembl; ENSPTRT00000062296; ENSPTRP00000054852; ENSPTRG00000032557.
DR GeneID; 746838; -.
DR KEGG; ptr:746838; -.
DR CTD; 2856; -.
DR VGNC; VGNC:7442; GPR33.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; Q49SQ3; -.
DR OMA; STNWESK; -.
DR OrthoDB; 1025058at2759; -.
DR TreeFam; TF330976; -.
DR Proteomes; UP000002277; Chromosome 14.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR InterPro; IPR000826; Formyl_rcpt-rel.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24225; PTHR24225; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..333
FT /note="Probable G-protein coupled receptor 33"
FT /id="PRO_0000069556"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..103
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..303
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 101..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 333 AA; 38257 MW; DFE4B85D99B73C83 CRC64;
MDLINSTDYL INASTLVRNS TQFLAPASKM IIALSLYISS IIGTITNGLY LWVLRFKMKQ
TVNTLLFFHL ILSYFISTMI LPFMATSQLQ DNHWNFGTAL CKVFNGTLSL GMFTSVFFLS
AIGLDRYLLT LHPVWSQQHR TPRWASSIVL GVWISAAALS IPYLIFRQTH HDRKGKVTCQ
NNYAVSTNWE SKEMQALRQW IHVACFISRF LLGFLLPFFI IIFCYERVAS KVKERSLFKS
SKPFKVMMTA IISFFVCWMP YHIHQGLLLT TNQSLLLELT LILTVLTTSF NTIFSPTLYL
FVGENFKKVF KKSILALFES TFSEDSSVER TQT
