NPR22_CAEEL
ID NPR22_CAEEL Reviewed; 434 AA.
AC Q59E83; Q9N324;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Neuropeptide receptor 22 {ECO:0000305};
GN Name=npr-22 {ECO:0000312|WormBase:Y59H11AL.1b};
GN ORFNames=Y59H11AL.1 {ECO:0000312|WormBase:Y59H11AL.1b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=16377032; DOI=10.1016/j.peptides.2005.11.017;
RA Mertens I., Clinckspoor I., Janssen T., Nachman R., Schoofs L.;
RT "FMRFamide related peptide ligands activate the Caenorhabditis elegans
RT orphan GPCR Y59H11AL.1.";
RL Peptides 27:1291-1296(2006).
RN [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28847365; DOI=10.7554/elife.28877;
RA Ohno H., Yoshida M., Sato T., Kato J., Miyazato M., Kojima M., Ida T.,
RA Iino Y.;
RT "Luqin-like RYamide peptides regulate food-evoked responses in C.
RT elegans.";
RL Elife 6:0-0(2017).
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28128367; DOI=10.1038/ncomms14237;
RA Palamiuc L., Noble T., Witham E., Ratanpal H., Vaughan M., Srinivasan S.;
RT "A tachykinin-like neuroendocrine signalling axis couples central serotonin
RT action and nutrient sensing with peripheral lipid metabolism.";
RL Nat. Commun. 8:14237-14237(2017).
CC -!- FUNCTION: Receptor for the LURY-1-1 and LURY-1-2 peptides which control
CC food-related processes including feeding, lifespan, egg-laying and
CC roaming behavior (PubMed:28847365). Receptor for flp-7 which stimulates
CC serotonin-induced fat loss (PubMed:28128367). Serotonin induces
CC secretion of flp-7 from neurons and binding to npr-22 which leads to
CC induction of the atgp-1 lipase and subsequent fat loss
CC (PubMed:28128367). Acts in vitro as a receptor for the flp-7 FMRFamide-
CC like neuropeptides TPMQRSSMVRF-amide, SPMQRSSMVRF-amide, SPMERSAMVRF-
CC amide and SPMDRSKMVRF-amide (PubMed:16377032). Also acts in vitro as a
CC receptor for a number of other FMRFamide-like neuropeptides including
CC the flp-1 neuropeptide PNFMRY-amide, the flp-9 neuropeptide KPSFVRF-
CC amide, the flp-11 neuropeptides AMRNALVRF-amide, ASGGMRNALVRF-amide and
CC NGAPQPFVRF-amide, the flp-13 neuropeptides AADGAPLIRF-amide,
CC ASPSAPLIRF-amide, SPSAVPLIRF-amide, SAAAPLIRF-amide and ASSAPLIRF-
CC amide, and the flp-22 neuropeptide SPSAKWMRF-amide (PubMed:16377032).
CC The SPMERSAMVRF-amide neuropeptide from flp-7 acts as the strongest in
CC vitro activator of npr-22 (PubMed:16377032).
CC {ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:28128367,
CC ECO:0000269|PubMed:28847365}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:Y59H11AL.1b};
CC IsoId=Q59E83-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:Y59H11AL.1a};
CC IsoId=Q59E83-2; Sequence=VSP_059252;
CC -!- TISSUE SPECIFICITY: Expressed in many cells, mainly in the head region,
CC with expression detected in the head muscles, I2 neurons, MC neurons,
CC RIH neuron, AIA neurons, AUA neurons, ASK neurons, ASI neurons, a few
CC B-type motorneurons in the posterior ventral nerve cord, pharyngeal
CC muscles, body wall muscles, the intestine and a few classes of
CC unidentified cells anterior to the nerve ring (PubMed:28847365).
CC Expression in the MC neurons is important to mediate suppression of
CC feeding while expression in the RIH neuron is important for the
CC facilitation of egg-laying (PubMed:28847365). No expression detected in
CC other tissues including hypodermis (PubMed:28128367).
CC {ECO:0000269|PubMed:28128367, ECO:0000269|PubMed:28847365}.
CC -!- DISRUPTION PHENOTYPE: Eggs are retained in the body as normal during
CC starvation but the number of eggs laid during the initial refeeding
CC period is reduced and satiety-induced suppression of pharyngeal pumping
CC is slower than wild-type (PubMed:28847365). Suppression of serotonin-
CC induced body fat loss (PubMed:28128367). {ECO:0000269|PubMed:28128367,
CC ECO:0000269|PubMed:28847365}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|RuleBase:RU000688}.
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DR EMBL; BX284604; CCD64002.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD64003.1; -; Genomic_DNA.
DR RefSeq; NP_001023540.1; NM_001028369.3. [Q59E83-2]
DR RefSeq; NP_001023541.1; NM_001028370.3. [Q59E83-1]
DR AlphaFoldDB; Q59E83; -.
DR SMR; Q59E83; -.
DR STRING; 6239.Y59H11AL.1b; -.
DR PaxDb; Q59E83; -.
DR EnsemblMetazoa; Y59H11AL.1a.1; Y59H11AL.1a.1; WBGene00022004. [Q59E83-2]
DR EnsemblMetazoa; Y59H11AL.1b.1; Y59H11AL.1b.1; WBGene00022004. [Q59E83-1]
DR GeneID; 190424; -.
DR KEGG; cel:CELE_Y59H11AL.1; -.
DR UCSC; Y59H11AL.1a; c. elegans.
DR CTD; 190424; -.
DR WormBase; Y59H11AL.1a; CE31260; WBGene00022004; npr-22. [Q59E83-2]
DR WormBase; Y59H11AL.1b; CE38456; WBGene00022004; npr-22. [Q59E83-1]
DR eggNOG; KOG4219; Eukaryota.
DR GeneTree; ENSGT00940000165559; -.
DR InParanoid; Q59E83; -.
DR OMA; CICFYNI; -.
DR OrthoDB; 715197at2759; -.
DR PhylomeDB; Q59E83; -.
DR PRO; PR:Q59E83; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00022004; Expressed in larva and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; IDA:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IDA:UniProtKB.
DR GO; GO:2000252; P:negative regulation of feeding behavior; IDA:UniProtKB.
DR GO; GO:0040013; P:negative regulation of locomotion; IDA:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:WormBase.
DR GO; GO:1901046; P:positive regulation of oviposition; IDA:UniProtKB.
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 Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..434
FT /note="Neuropeptide receptor 22"
FT /id="PRO_0000442514"
FT TOPO_DOM 1..55
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 56..76
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 87..107
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..128
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 129..149
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 170..190
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..226
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 227..247
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 278..298
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..310
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 311..331
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 126..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 373..434
FT /note="SFRNRSRFSGVINPTSSDEKPATSLTRYSRSGVLDRQTCRSARFFEARPLVV
FT VRNNSANSLA -> RHRLRDIHEVESLTGKHVVRHVSSKPDHSSSSETTLPILSRSFSR
FT IIKKIDLPCT (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_059252"
SQ SEQUENCE 434 AA; 49751 MW; BB3D8C356B822CDB CRC64;
MDEGGGIGSS LLSRITTTAS EIMMRNEPTT TENPAVQEMN HIYHLTPSMK MLCILFYSIL
CVCCVYGNVL VILVIVYFKR LRTATNILIL NLAVADLLIS VFCIPFSYWQ VLIYDDQRWL
FGSMMCSLLA FLQAMAVFLS AWTLVVISFD RWMAIMFLLT PNIRITRRRA LYLVAATWIF
SILMALPLLF TTRFFEDQDG LPNCGENWTY FGDSGEQVRK VYSSMVLILQ YVVPQAVLII
TYTHIGIKMW NSRVPGMQNG ATKKMIVDRH ESVKKLVPMV ILISALFALC WLPLLILINV
IPEFYPDINS WGYILYLWWF AHGLAMSHSM VNPIIYFIRN ARFREGFCFF SSKLLPCISF
KELRLLTDNT SRSFRNRSRF SGVINPTSSD EKPATSLTRY SRSGVLDRQT CRSARFFEAR
PLVVVRNNSA NSLA
