SSR3_RAT
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 03-AUG-2022, entry version 154.
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}.
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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 GlyGen; P30936; 2 sites.
DR iPTMnet; P30936; -.
DR PhosphoSitePlus; P30936; -.
DR PaxDb; P30936; -.
DR PRIDE; P30936; -.
DR Ensembl; ENSRNOT00000009612; ENSRNOP00000009612; ENSRNOG00000007332.
DR GeneID; 171044; -.
DR KEGG; rno:171044; -.
DR UCSC; RGD:620308; rat.
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; VCSQEPT; -.
DR OrthoDB; 1011272at2759; -.
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 tissues.
DR Genevisible; P30936; RN.
DR GO; GO:0060170; C:ciliary membrane; ISO:RGD.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0042277; F:peptide 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 InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000586; Somatstn_rcpt.
DR InterPro; IPR001856; Somatstn_rcpt_3.
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 PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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
