PKR2_BOVIN
ID PKR2_BOVIN Reviewed; 384 AA.
AC Q8SPN1;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Prokineticin receptor 2;
DE Short=PK-R2;
DE AltName: Full=G-protein coupled receptor 73-like 1;
DE AltName: Full=G-protein coupled receptor I5E;
GN Name=PROKR2; Synonyms=GPR73L1, PKR2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12054613; DOI=10.1016/s0006-291x(02)00239-5;
RA Masuda Y., Takatsu Y., Terao Y., Kumano S., Ishibashi Y., Suenaga M.,
RA Abe M., Fukusumi S., Watanabe T., Shintani Y., Yamada T., Hinuma S.,
RA Inatomi N., Ohtaki T., Onda H., Fujino M.;
RT "Isolation and identification of EG-VEGF/prokineticins as cognate ligands
RT for two orphan G-protein-coupled receptors.";
RL Biochem. Biophys. Res. Commun. 293:396-402(2002).
CC -!- FUNCTION: Receptor for prokineticin 2. Exclusively coupled to the G(q)
CC subclass of heteromeric G proteins. Activation leads to mobilization of
CC calcium, stimulation of phosphoinositide turnover and activation of
CC p44/p42 mitogen-activated protein kinase (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NFJ6};
CC 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; AY089973; AAM11889.1; -; mRNA.
DR RefSeq; NP_777065.1; NM_174640.1.
DR RefSeq; XP_005214494.1; XM_005214437.3.
DR AlphaFoldDB; Q8SPN1; -.
DR SMR; Q8SPN1; -.
DR STRING; 9913.ENSBTAP00000021097; -.
DR PaxDb; Q8SPN1; -.
DR Ensembl; ENSBTAT00000021097; ENSBTAP00000021097; ENSBTAG00000015872.
DR GeneID; 282431; -.
DR KEGG; bta:282431; -.
DR CTD; 128674; -.
DR VEuPathDB; HostDB:ENSBTAG00000015872; -.
DR VGNC; VGNC:33363; PROKR2.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000154544; -.
DR HOGENOM; CLU_009579_6_0_1; -.
DR InParanoid; Q8SPN1; -.
DR OMA; KTHTFFA; -.
DR OrthoDB; 664455at2759; -.
DR TreeFam; TF315303; -.
DR Reactome; R-BTA-375276; Peptide ligand-binding receptors.
DR Reactome; R-BTA-416476; G alpha (q) signalling events.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000015872; Expressed in semen and 17 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR GO; GO:0007623; P:circadian rhythm; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000611; NPY_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01012; NRPEPTIDEYR.
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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..384
FT /note="Prokineticin receptor 2"
FT /id="PRO_0000070082"
FT TOPO_DOM 1..53
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..313
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 128..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 384 AA; 44138 MW; 997895960EEB2DD4 CRC64;
MAAQNGNASF PANFSIPQEH ASSLPFNFSY DDYDLPLDED EDMTKTQTFF AAKIVIGVAL
VGIMLTCGIG NFVFITALTR YKKLRNLTNL LIANLAISDF LVAIICCPFE MDYYVVHQLS
WEHGHVLCAC INYLRTVSLY VSTNALLAIA IDRYLAIVHP LKPRMNYQTA SFLIALVWMV
SILISIPSAY FTKETVLFIV KNQKKIFCGQ VWPVDQQLYY KSYFLFVFGI EFLGPVFTMT
LCYARISREL WFKAVPGFQT EQIRKRLRCR RKTVLVLMCI LTAYVLCWAP FYGFTIVRDF
FPTVFVKEKH YLTAFYVVEC IAMSNSMINT VCFVTVKNST MKYFKKMLLL HWRPSHHGSK
SSADLDLKTS RLPATEEVDC IRLK
