PKR2_RAT
ID PKR2_RAT Reviewed; 383 AA.
AC Q8R415;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 2.
DT 25-MAY-2022, entry version 127.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
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 -!- TISSUE SPECIFICITY: Abundantly expressed in the CNS and reproductive
CC organs with the highest levels in the cerebrum, cerebellum, testis and
CC ovary.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM11891.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY089975; AAM11891.1; ALT_INIT; mRNA.
DR RefSeq; NP_620434.1; NM_138978.1.
DR AlphaFoldDB; Q8R415; -.
DR SMR; Q8R415; -.
DR STRING; 10116.ENSRNOP00000028889; -.
DR GlyGen; Q8R415; 2 sites.
DR PhosphoSitePlus; Q8R415; -.
DR PaxDb; Q8R415; -.
DR GeneID; 192649; -.
DR KEGG; rno:192649; -.
DR UCSC; RGD:708445; rat.
DR CTD; 128674; -.
DR RGD; 708445; Prokr2.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q8R415; -.
DR PhylomeDB; Q8R415; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:Q8R415; -.
DR Proteomes; UP000002494; Unplaced.
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; IMP:RGD.
DR GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
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..383
FT /note="Prokineticin receptor 2"
FT /id="PRO_0000070085"
FT TOPO_DOM 1..54
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..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..136
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..222
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 7
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..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 383 AA; 43603 MW; 477C501099535B93 CRC64;
MGDQNGNTSF APDLNPPQDH VSLLPLNYSY GDYDIPLDDD EDVTKTQTFF AAKIVIGVAL
AGIMLVCGVG NFVFIAALAR YKKLRNLTNL LIANLAISDF LVAIVCCPFE MDYYVVRQLS
WEHGHVLCAS VNYLRTVSLY VSTNALLAIA IDRYLAIVHP LKRMNYQTAS FLIALVWMVS
ILIAIPSAYF TTETILVIVK NQEKLFCGQI WPVDQQLYYK SYFLFVFGLE FVGPVVTMTL
CYARISQELW FKAVPGFQTE QIRKRLRCRR KTVLLLMGIL TAYVLCWAPF YGFTIVRDFF
PTLVVKEKHY LTAFYVVECI AMSNSMINTI CFVTVKNNTM KYFKKMLLLH WRPSHYGSKS
SADLDLKTSG VPATEEVDCI RLK
