ID   GPR33_RATRT             Reviewed;         339 AA.
AC   Q49SP8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Probable G-protein coupled receptor 33;
GN   Name=Gpr33;
OS   Rattus rattus (Black rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10117;
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 Rattus norvegicus, Gpr33 is disrupted by a 14 bp
CC       deletion. GPR33 has undergone independent pseudogenization in human,
CC       chimpanzee, orangutan, siamang and rat. This selective inactivation may
CC       be due to its interaction with a putative pathogen that could use GPR33
CC       as a receptor for cell invasion. {ECO:0000305|PubMed:15987686}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY494004; AAR98757.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q49SP8; -.
DR   SMR; Q49SP8; -.
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:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
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; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..339
FT                   /note="Probable G-protein coupled receptor 33"
FT                   /id="PRO_0000069557"
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..339
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        101..179
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   339 AA;  38374 MW;  6AC8FF6567E88B79 CRC64;
     MDRVNSSGHV ISVSPSLTNS TGVPTPAPKA IIAAALFMSF IVGTISNGLY LWMLKFKMQR
     TVNTLLFFHL ILSYFISTLI LPFMATSFLQ DNHWAFGSVL CKVFNSTLSV SMFASVFFLS
     AISVDRYHLT LHPVWSQQHR TPRWASRIAL RIWILATILS IPYLVFRETH DDHKGRIKCQ
     NNYIVGTNWE SSEHQTLGQW IHAACFGRRF LLGFLLPFLV IVFCYKRVAT KMKDKGLFKS
     SKPFKVMLTA VVSFFVCWMP YHVHSGLVLT KSQPLPSQLT LGLAVVTISF NTVVSPILYL
     FTGENFEVFK KSILALFKST FSDSSATERT QTLNSETEI