DMSR1_CAEEL
ID DMSR1_CAEEL Reviewed; 510 AA.
AC Q20929; Q8MQ19;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=G-protein coupled receptor dmsr-1 {ECO:0000305};
DE AltName: Full=Dromyosuppressin receptor related 1 {ECO:0000303|PubMed:28094002};
GN Name=dmsr-1 {ECO:0000303|PubMed:28094002, ECO:0000312|WormBase:F57B7.1a};
GN ORFNames=F57B7.1 {ECO:0000312|WormBase:F57B7.1a};
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 (ISOFORM A), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF 107-TRP--ILE-510; ALA-207; 246-ARG--ILE-510;
RP 322-GLN--ILE-510; 337-ARG--ILE-510 AND 345-GLY--ILE-510.
RX PubMed=28094002; DOI=10.7554/elife.19837;
RA Iannacone M.J., Beets I., Lopes L.E., Churgin M.A., Fang-Yen C.,
RA Nelson M.D., Schoofs L., Raizen D.M.;
RT "The RFamide receptor DMSR-1 regulates stress-induced sleep in C.
RT elegans.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: G-protein coupled receptor. {ECO:0000305|PubMed:28094002}.
CC -!- FUNCTION: [Isoform a]: G-protein coupled receptor for flp-13 RFamide
CC neuropeptides in vitro (PubMed:28094002). Upon activation by flp-13
CC RFamide neuropeptides, promotes sleep in response to cellular stress
CC also known as stress-induced sleep (SIS), probably by inhibiting the
CC activity of wake-promoting neurons (PubMed:28094002).
CC {ECO:0000269|PubMed:28094002}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28094002};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F57B7.1a};
CC IsoId=Q20929-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F57B7.1b};
CC IsoId=Q20929-2; Sequence=VSP_060778, VSP_060779;
CC -!- TISSUE SPECIFICITY: Expressed in head neurons including the RID neuron
CC and the paired AIY neurons, and in tail neurons including the paired
CC PHA and PHB neurons (PubMed:28094002). Not expressed in AVE and AVA
CC neurons (PubMed:28094002). {ECO:0000269|PubMed:28094002}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; BX284605; CAA98492.1; -; Genomic_DNA.
DR EMBL; BX284605; CAD36492.1; -; Genomic_DNA.
DR PIR; T22835; T22835.
DR RefSeq; NP_741629.1; NM_171541.4. [Q20929-1]
DR RefSeq; NP_741630.1; NM_171542.4. [Q20929-2]
DR AlphaFoldDB; Q20929; -.
DR SMR; Q20929; -.
DR STRING; 6239.F57B7.1a; -.
DR PaxDb; Q20929; -.
DR EnsemblMetazoa; F57B7.1a.1; F57B7.1a.1; WBGene00010191. [Q20929-1]
DR EnsemblMetazoa; F57B7.1b.1; F57B7.1b.1; WBGene00010191. [Q20929-2]
DR GeneID; 186437; -.
DR KEGG; cel:CELE_F57B7.1; -.
DR UCSC; F57B7.1a; c. elegans.
DR CTD; 186437; -.
DR WormBase; F57B7.1a; CE05989; WBGene00010191; dmsr-1. [Q20929-1]
DR WormBase; F57B7.1b; CE31009; WBGene00010191; dmsr-1. [Q20929-2]
DR eggNOG; ENOG502RECK; Eukaryota.
DR GeneTree; ENSGT00940000166133; -.
DR HOGENOM; CLU_009579_24_4_1; -.
DR InParanoid; Q20929; -.
DR OMA; KLSYGWA; -.
DR OrthoDB; 790152at2759; -.
DR PhylomeDB; Q20929; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010191; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q20929; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
DR GO; GO:0008188; F:neuropeptide receptor activity; IDA:UniProtKB.
DR GO; GO:1900034; P:regulation of cellular response to heat; IGI:UniProtKB.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:UniProtKB.
DR InterPro; IPR019427; 7TM_GPCR_serpentine_rcpt_Srw.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF10324; 7TM_GPCR_Srw; 2.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..510
FT /note="G-protein coupled receptor dmsr-1"
FT /id="PRO_0000451414"
FT TOPO_DOM 1..35
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 36..56
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 65..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..107
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 108..128
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 156..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..223
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 224..244
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 308..328
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..343
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 344..364
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 451..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 430..441
FT /note="SASVKMVGIQVR -> WSESRYEETVRK (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060778"
FT VAR_SEQ 442..510
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060779"
FT MUTAGEN 107..510
FT /note="Missing: In qn53; defective sleep induction
FT following heat stress in a flp-13 overexpressing mutant
FT background."
FT /evidence="ECO:0000269|PubMed:28094002"
FT MUTAGEN 207
FT /note="A->V: In qn52; defective sleep induction following
FT heat stress in a flp-13 overexpressing mutant background."
FT /evidence="ECO:0000269|PubMed:28094002"
FT MUTAGEN 246..510
FT /note="Missing: In qn40; defective sleep induction
FT following heat stress in a flp-13 overexpressing mutant
FT background."
FT /evidence="ECO:0000269|PubMed:28094002"
FT MUTAGEN 322..510
FT /note="Missing: In qn51; defective sleep induction
FT following heat stress in a flp-13 overexpressing mutant
FT background."
FT /evidence="ECO:0000269|PubMed:28094002"
FT MUTAGEN 337..510
FT /note="Missing: In qn44; defective sleep induction
FT following heat stress in a flp-13 overexpressing mutant
FT background."
FT /evidence="ECO:0000269|PubMed:28094002"
FT MUTAGEN 345..510
FT /note="Missing: In qn49; defective sleep induction
FT following heat stress in a flp-13 overexpressing mutant
FT background."
FT /evidence="ECO:0000269|PubMed:28094002"
SQ SEQUENCE 510 AA; 57249 MW; BB42DDEB661718FF CRC64;
MEFTECKTTF IHLPDKSFLY DVFVSVYNFY HPIHAYLSIF LCVLGTIANF CNIVVLTRRT
MRTPVNMILT AMASCDTVVL FSNLIYTTHY SFVAFKFCHP KHWSYSWALF LIAHAHLSLV
AHSSSVWLSV MLALVRYVTL RSRGNMGGMQ VTLRHSYYAV AVTVSLVAVL NAPNFLNYKI
NEQPLNETCT DLDPMFWNSP AYLPGIADIA KANSCLVFRL SYWISGMVFK VLPCALLSLF
VWLLLRILRE VRENRQRLLK NSQHRPPNQT TTRNGQRLSI SVAGNEKLGR NGSLRGRGER
VDRTTHMLLA IVAVMLVTEL PQGIMAVLSG MCSEEFRIYI YNNLGDILDL FSLCGSCCSF
IIYCSMSGQF RNEFHRVFVP AKVRCLRMSS PSIRRPSDAY STTKMTFLKP NEKNGNGMNG
NGTYSEDTRS ASVKMVGIQV RRNSTEITRM TGCDSITPCS PMPTSFPSSP LPPIRSGEDE
STDETSHLLN SSGPNSTASA DGIRGHFQNI
