ID SSR3_RAT Reviewed; 428 AA. AC P30936; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 24-JAN-2024, entry version 162. DE RecName: Full=Somatostatin receptor type 3; DE Short=SS-3-R; DE Short=SS3-R; DE Short=SS3R; DE AltName: Full=SSR-28; GN Name=Sstr3; 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], FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Wistar; TISSUE=Brain; RX PubMed=1279674; DOI=10.1073/pnas.89.21.10267; RA Meyerhof W., Wulfsen I., Schoenrock C., Fehr S., Richter D.; RT "Molecular cloning of a somatostatin-28 receptor and comparison of its RT expression pattern with that of a somatostatin-14 receptor in rat brain."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10267-10271(1992). RN [2] RP SUBCELLULAR LOCATION, MUTAGENESIS OF SER-341; SER-346; SER-351 AND THR-357, RP AND PHOSPHORYLATION AT SER-341; SER-346; SER-351 AND THR-357. RX PubMed=9295322; DOI=10.1074/jbc.272.38.23769; RA Roth A., Kreienkamp H.-J., Meyerhof W., Richter D.; RT "Phosphorylation of four amino acid residues in the carboxyl terminus of RT the rat somatostatin receptor subtype 3 is crucial for its desensitization RT and internalization."; RL J. Biol. Chem. 272:23769-23774(1997). RN [3] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=11134004; DOI=10.1074/jbc.m006084200; RA Pfeiffer M., Koch T., Schroder H., Klutzny M., Kirscht S., Kreienkamp H.J., RA Hollt V., Schulz S.; RT "Homo- and heterodimerization of somatostatin receptor subtypes. RT Inactivation of sst(3) receptor function by heterodimerization with RT sst(2A)."; RL J. Biol. Chem. 276:14027-14036(2001). CC -!- FUNCTION: Receptor for somatostatin-14 and -28. This receptor is CC coupled via pertussis toxin sensitive G proteins to inhibition of CC adenylyl cyclase. {ECO:0000269|PubMed:11134004, CC ECO:0000269|PubMed:1279674}. CC -!- SUBUNIT: Homodimer and heterodimer with SSTR2. Heterodimerization with CC SSTR2 inactivates SSTR3 receptor function. CC {ECO:0000269|PubMed:11134004}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11134004, CC ECO:0000269|PubMed:9295322}; Multi-pass membrane protein CC {ECO:0000269|PubMed:11134004, ECO:0000269|PubMed:9295322}. CC Note=Internalized into endoplasmic vesicles upon somatostatin- CC stimulation. CC -!- TISSUE SPECIFICITY: Densely expressed in cerebellum and at moderate CC levels in the amygdala, cortex, striatum, spleen, liver and pituitary. CC {ECO:0000269|PubMed:1279674}. CC -!- PTM: Phosphorylated. Phosphorylation increases upon somatostatin CC binding. {ECO:0000269|PubMed:9295322}. 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; X63574; CAA45130.1; -; mRNA. DR PIR; S30508; S30508. DR RefSeq; NP_598206.1; NM_133522.1. DR RefSeq; XP_006242028.1; XM_006241966.2. DR AlphaFoldDB; P30936; -. DR SMR; P30936; -. DR BioGRID; 251061; 1. DR STRING; 10116.ENSRNOP00000009612; -. DR BindingDB; P30936; -. DR ChEMBL; CHEMBL3340; -. DR DrugCentral; P30936; -. DR GuidetoPHARMACOLOGY; 357; -. DR GlyCosmos; P30936; 2 sites, No reported glycans. DR GlyGen; P30936; 2 sites. DR iPTMnet; P30936; -. DR PhosphoSitePlus; P30936; -. DR PaxDb; 10116-ENSRNOP00000009612; -. DR Ensembl; ENSRNOT00000009612.4; ENSRNOP00000009612.2; ENSRNOG00000007332.4. DR Ensembl; ENSRNOT00055055509; ENSRNOP00055045798; ENSRNOG00055032113. DR Ensembl; ENSRNOT00060053042; ENSRNOP00060044095; ENSRNOG00060030539. DR Ensembl; ENSRNOT00065056180; ENSRNOP00065046278; ENSRNOG00065032663. DR GeneID; 171044; -. DR KEGG; rno:171044; -. DR UCSC; RGD:620308; rat. DR AGR; RGD:620308; -. DR CTD; 6753; -. DR RGD; 620308; Sstr3. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT00940000162038; -. DR HOGENOM; CLU_009579_8_1_1; -. DR InParanoid; P30936; -. DR OMA; NTSSAWP; -. DR OrthoDB; 5393360at2759; -. DR PhylomeDB; P30936; -. DR TreeFam; TF315737; -. DR Reactome; R-RNO-375276; Peptide ligand-binding receptors. DR Reactome; R-RNO-418594; G alpha (i) signalling events. DR Reactome; R-RNO-5620922; BBSome-mediated cargo-targeting to cilium. DR PRO; PR:P30936; -. DR Proteomes; UP000002494; Chromosome 7. DR Bgee; ENSRNOG00000007332; Expressed in thymus and 13 other cell types or tissues. DR GO; GO:0060170; C:ciliary membrane; ISO:RGD. DR GO; GO:0005929; C:cilium; ISO:RGD. DR GO; GO:0043005; C:neuron projection; ISO:RGD. DR GO; GO:0097730; C:non-motile cilium; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central. DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central. DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD. DR GO; GO:0004994; F:somatostatin receptor activity; IEA:InterPro. DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD. DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEP:RGD. DR GO; GO:0021549; P:cerebellum development; IEP:RGD. DR GO; GO:0030900; P:forebrain development; IEP:RGD. DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central. DR GO; GO:0042594; P:response to starvation; IEP:RGD. DR GO; GO:0007283; P:spermatogenesis; IEP:RGD. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR InterPro; IPR000586; Somatstn_rcpt. DR InterPro; IPR001856; Somatstn_rcpt_3. DR PANTHER; PTHR24229; NEUROPEPTIDES RECEPTOR; 1. DR PANTHER; PTHR24229:SF42; SOMATOSTATIN RECEPTOR TYPE 3; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00246; SOMATOSTATNR. DR PRINTS; PR00589; SOMATOSTTN3R. DR SMART; SM01381; 7TM_GPCR_Srsx; 1. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR Genevisible; P30936; RN. PE 1: Evidence at protein level; KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..428 FT /note="Somatostatin receptor type 3" FT /id="PRO_0000070126" FT TOPO_DOM 1..45 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 46..71 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 72..81 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 82..103 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 104..118 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 119..140 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 141..162 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 163..182 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 183..206 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 207..232 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 233..266 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 267..288 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 289..302 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 303..325 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 326..428 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 343..428 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 355..369 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 381..428 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 341 FT /note="Phosphoserine" FT /evidence="ECO:0000305|PubMed:9295322" FT MOD_RES 346 FT /note="Phosphoserine" FT /evidence="ECO:0000305|PubMed:9295322" FT MOD_RES 351 FT /note="Phosphoserine" FT /evidence="ECO:0000305|PubMed:9295322" FT MOD_RES 357 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:9295322" FT CARBOHYD 18 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 31 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 117..192 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT MUTAGEN 341 FT /note="S->A: Impaired internalization after somatostatin FT binding." FT /evidence="ECO:0000269|PubMed:9295322" FT MUTAGEN 346 FT /note="S->A: Impaired internalization after somatostatin FT binding." FT /evidence="ECO:0000269|PubMed:9295322" FT MUTAGEN 351 FT /note="S->A: Impaired internalization after somatostatin FT binding." FT /evidence="ECO:0000269|PubMed:9295322" FT MUTAGEN 357 FT /note="T->A: Reduced basal and somatostatin-induced FT phosphorylation. Impaired internalization after FT somatostatin binding." FT /evidence="ECO:0000269|PubMed:9295322" SQ SEQUENCE 428 AA; 47151 MW; BE0AA948840A9E9D CRC64; MAAVTYPSSV PTTLDPGNAS SAWPLDTSLG NASAGTSLAG LAVSGILISL VYLVVCVVGL LGNSLVIYVV LRHTSSPSVT SVYILNLALA DELFMLGLPF LAAQNALSYW PFGSLMCRLV MAVDGINQFT SIFCLTVMSV DRYLAVVHPT RSARWRTAPV ARMVSAAVWV ASAVVVLPVV VFSGVPRGMS TCHMQWPEPA AAWRTAFIIY TAALGFFGPL LVICLCYLLI VVKVRSTTRR VRAPSCQWVQ APACQRRRRS ERRVTRMVVA VVALFVLCWM PFYLLNIVNV VCPLPEEPAF FGLYFLVVAL PYANSCANPI LYGFLSYRFK QGFRRILLRP SRRVRSQEPG SGPPEKTEEE EDEEEEERRE EEERRMQRGQ EMNGRLSQIA QPGPSGQQQR PCTGTAKEQQ LLPQEATAGD KASTLSHL //