PK1R_DROME
ID PK1R_DROME Reviewed; 430 AA.
AC Q8ITC9; Q0IGX8; Q71RH8;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Pyrokinin-1 receptor {ECO:0000303|PubMed:16054112};
GN Name=PK1-R {ECO:0000312|FlyBase:FBgn0038201};
GN ORFNames=CG9918 {ECO:0000312|FlyBase:FBgn0038201};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAN10044.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Canton-S {ECO:0000312|EMBL:AAN10044.1};
RX PubMed=12177421; DOI=10.1073/pnas.162276199;
RA Park Y., Kim Y.-J., Adams M.E.;
RT "Identification of G protein-coupled receptors for Drosophila PRXamide
RT peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor
RT coevolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11423-11428(2002).
RN [2] {ECO:0000312|EMBL:AAQ15197.2}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16054112; DOI=10.1016/j.bbrc.2005.07.038;
RA Cazzamali G., Torp M., Hauser F., Williamson M., Grimmelikhuijzen C.J.;
RT "The Drosophila gene CG9918 codes for a pyrokinin-1 receptor.";
RL Biochem. Biophys. Res. Commun. 33:14-19(2005).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000312|EMBL:ABI34173.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABI34173.1};
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Celniker S.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for the neuropeptide CAP-3/pyrokinin-1
CC (TGPSASSGLWFGPRL-amide) (PubMed:16054112). Also activated weakly by
CC other neuropeptides terminating in the sequence PRL-amide including
CC pyrokinin-2, Hug-gamma, and ecdysis-triggering-hormone-1
CC (PubMed:12177421, PubMed:16054112). The activity of this receptor is
CC mediated by G proteins which activate a phosphatidyl-inositol-calcium
CC second messenger system (PubMed:16054112).
CC {ECO:0000269|PubMed:12177421, ECO:0000269|PubMed:16054112}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12177421,
CC ECO:0000269|PubMed:16054112}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|RuleBase:RU000688, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI34173.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF522191; AAN10044.1; -; mRNA.
DR EMBL; AF368273; AAQ15197.2; -; mRNA.
DR EMBL; AE014297; AAX52950.1; -; Genomic_DNA.
DR EMBL; AE014297; AFH06407.1; -; Genomic_DNA.
DR EMBL; BT028792; ABI34173.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001014620.1; NM_001014620.2.
DR RefSeq; NP_001247089.1; NM_001260160.1.
DR AlphaFoldDB; Q8ITC9; -.
DR SMR; Q8ITC9; -.
DR IntAct; Q8ITC9; 1.
DR STRING; 7227.FBpp0296961; -.
DR GlyGen; Q8ITC9; 1 site.
DR PaxDb; Q8ITC9; -.
DR EnsemblMetazoa; FBtr0100131; FBpp0099477; FBgn0038201.
DR EnsemblMetazoa; FBtr0305681; FBpp0296961; FBgn0038201.
DR GeneID; 41713; -.
DR KEGG; dme:Dmel_CG9918; -.
DR UCSC; CG9918-RD; d. melanogaster.
DR CTD; 41713; -.
DR FlyBase; FBgn0038201; PK1-R.
DR VEuPathDB; VectorBase:FBgn0038201; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01040000240430; -.
DR HOGENOM; CLU_009579_6_5_1; -.
DR InParanoid; Q8ITC9; -.
DR OMA; YTVMTYV; -.
DR OrthoDB; 890529at2759; -.
DR PhylomeDB; Q8ITC9; -.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 41713; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41713; -.
DR PRO; PR:Q8ITC9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038201; Expressed in adult integumentary system and 5 other tissues.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:FlyBase.
DR GO; GO:0008188; F:neuropeptide receptor activity; ISM:FlyBase.
DR GO; GO:0036401; F:pyrokinin receptor activity; IPI:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:FlyBase.
DR GO; GO:0090278; P:negative regulation of peptide hormone secretion; IMP:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:FlyBase.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
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..430
FT /note="Pyrokinin-1 receptor"
FT /id="PRO_0000439215"
FT TOPO_DOM 1..16
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 54..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..96
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 97..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 141..161
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..185
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 186..206
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 282..302
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..321
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 322..342
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 388..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 94..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 430 AA; 47317 MW; FB28DD7E482E425F CRC64;
MSAGNMSHDL GPPRDPLAIV IPVTVVYSLI FITGVVGNIS TCIVIKKNRS MHTATNYYLF
SLAISDFLLL LSGVPQEVSY IWSKYPYVFG EYICIGRGLL AETSANATVL TITAFTVERY
IAICHPFLGQ AMSKLSRAIR IIVLVWIMAI VTAIPQAAQF GIEHYSGVEQ CGIVRVIVKH
SFQLSTFIFF LAPMSIILVL YLLIGVHLYR STLVEGPASV ARRQQLKSVP SDTILYRYGG
SGTAMSFNGG GSGAGTAGLM GGSGAQLSSV RGRLNHYGTR RVLRMLVAVV VCFFLCWAPF
HAQRLIAIYA PARGAKLRDQ HEFVYTVMTY VSGVLYYLST CINPLLYNIM SHKFREAFKA
VLFGKKVSKG SLNSRNNIES RRLRRALTNS SQTQRFSIES AEQPKPSIMQ NPTNKPPVAA
QYAMIGVQVN
