ID   SPRR2_CAEEL             Reviewed;         451 AA.
AC   Q93704;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Sex peptide receptor-related protein 2 {ECO:0000312|WormBase:F42D1.3};
DE   AltName: Full=Myoinhibitory-like protein receptor homolog {ECO:0000303|PubMed:30779740};
GN   Name=sprr-2 {ECO:0000312|WormBase:F42D1.3};
GN   Synonyms=mipr-1 {ECO:0000303|PubMed:30779740};
GN   ORFNames=F42D1.3 {ECO:0000312|WormBase:F42D1.3};
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, AND TISSUE SPECIFICITY.
RX   PubMed=30779740; DOI=10.1371/journal.pgen.1007945;
RA   Peymen K., Watteyne J., Borghgraef C., Van Sinay E., Beets I., Schoofs L.;
RT   "Myoinhibitory peptide signaling modulates aversive gustatory learning in
RT   Caenorhabditis elegans.";
RL   PLoS Genet. 15:E1007945-E1007945(2019).
CC   -!- FUNCTION: G-protein coupled receptor for the neuropeptide like protein
CC       nlp-38 (PubMed:30779740). Plays a role in several types of aversive
CC       gustatory associative learning including gustatory plasticity and salt
CC       avoidance learning (PubMed:30779740). Its role in salt avoidance
CC       learning may be through activation of the transcription factor crh-
CC       1/CREB and de novo transcription and translation, which in turn
CC       promotes the formation of long-term memory (PubMed:30779740).
CC       {ECO:0000269|PubMed:30779740}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in head neurons including the ASE sensory
CC       neurons and the ASI and AWB chemosensory neurons, the midbody neurons
CC       SDQ, and motor neurons in the tail. {ECO:0000269|PubMed:30779740}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX284606; CAB03091.2; -; Genomic_DNA.
DR   PIR; T22088; T22088.
DR   RefSeq; NP_510455.2; NM_078054.5.
DR   AlphaFoldDB; Q93704; -.
DR   SMR; Q93704; -.
DR   STRING; 6239.F42D1.3; -.
DR   PaxDb; Q93704; -.
DR   EnsemblMetazoa; F42D1.3.1; F42D1.3.1; WBGene00009629.
DR   EnsemblMetazoa; F42D1.3.2; F42D1.3.2; WBGene00009629.
DR   EnsemblMetazoa; F42D1.3.3; F42D1.3.3; WBGene00009629.
DR   GeneID; 181575; -.
DR   KEGG; cel:CELE_F42D1.3; -.
DR   UCSC; F42D1.3; c. elegans.
DR   CTD; 181575; -.
DR   WormBase; F42D1.3; CE31511; WBGene00009629; sprr-2.
DR   eggNOG; ENOG502QVMK; Eukaryota.
DR   HOGENOM; CLU_009579_24_5_1; -.
DR   InParanoid; Q93704; -.
DR   OMA; HMITPTN; -.
DR   OrthoDB; 994073at2759; -.
DR   PhylomeDB; Q93704; -.
DR   PRO; PR:Q93704; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00009629; Expressed in larva and 3 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IEA:InterPro.
DR   GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Behavior; Cell membrane; Chemotaxis; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..451
FT                   /note="Sex peptide receptor-related protein 2"
FT                   /id="PRO_0000448956"
FT   TOPO_DOM        1..63
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        64..84
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..97
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        98..118
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        119..140
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        141..161
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..183
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        184..204
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        205..251
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        252..272
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..301
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        302..322
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        323..334
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        335..355
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        356..451
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        15
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        134..225
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   451 AA;  51217 MW;  6730888413750212 CRC64;
     MNYEVYCGNA HAEPNSSAVQ QLAEACVEQD ASYFDGCSRT CVKDKYLLPL TQFDNLEIVV
     YGQIFPILVL FAVFANAAVA LVLSKKHMIT PTNVVLKYMA IAELLVGLVP LPWTLFFFSM
     GNIKETHRLE LWWCYLQKYS MDAFPPVFHM IAMWLTVLLA AQRYVSISHP LHSRSACNVK
     NVRLATMIIT VTSFLCGLPK SFDYEYETVH GWIYSHGNWT YASSCVMMPT AILTNMGQTV
     YFNIYFWTRA LGFIILPSFL LVLLNGLLIK GIRRAQRRKL RLLREKRSEE AARQRDSNST
     SLMLVAIVSI FLIVNLPQAI FMGLLCVCET FTIKIPILEG TFPAVFLIAS NMIVIATYPI
     NFGIYCFMSS SFRQTFKLLF CPGASQLQCE RRIEAASAVH SSRRRSDICS HLVNVCTNSE
     GFMQVSHHCL HVDYLVSDRQ STQFTTMDRS D