GPR15_CHLAE
ID GPR15_CHLAE Reviewed; 360 AA.
AC O18982;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=G-protein coupled receptor 15;
DE AltName: Full=Brother of Bonzo;
DE Short=BoB;
GN Name=GPR15;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9230441; DOI=10.1038/40894;
RA Deng H.K., Unutmaz D., Kewalramani V.N., Littman D.R.;
RT "Expression cloning of new receptors used by simian and human
RT immunodeficiency viruses.";
RL Nature 388:296-300(1997).
CC -!- FUNCTION: Probable chemokine receptor. SIV-1 coreceptor.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF007856; AAB64222.1; -; Genomic_DNA.
DR AlphaFoldDB; O18982; -.
DR SMR; O18982; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; G-protein coupled receptor; Membrane; Receptor; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..360
FT /note="G-protein coupled receptor 15"
FT /id="PRO_0000069530"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 360 AA; 40774 MW; 9C8EF239AE004E83 CRC64;
MDPEETSVYL DYYYATSPNP DIRETHSHVP YTSVFLPVFY IAVFLTGVLG NLVLMGALHF
KPGSRRLIDI FIINLAASDF IFLVTLPLWV DKEASLGLWR TGSFLCKGSS YMISVNMHCS
VFLLTCMSVD RYLAIVCPVV SRKFRRTDCA YVVCASIWFI SCLLGLPTLL SRELTLIDDK
PYCAEKKATP LKLIWSLVAL IFTFFVPLLS IVTCYCRIAR KLCAHYQQSG KHNKKLKKSI
KIIFIVVAAF LVSWLPFNTS KLLAIVSGLQ QERYFPSAIL QLGMEVSGPL AFANSCVNPF
IYYIFDSYIR RAIVHCLCPC LKNYDFGSST ETSDSHLTKA LSTFIHAEDF TRRRKRSVSL