SSR1_RAT
ID SSR1_RAT Reviewed; 391 AA.
AC P28646;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Somatostatin receptor type 1;
DE Short=SS-1-R;
DE Short=SS1-R;
DE Short=SS1R;
DE AltName: Full=SRIF-2;
GN Name=Sstr1;
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].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=1661599; DOI=10.1089/dna.1991.10.689;
RA Meyerhof W., Paust H.J., Schoenrock C., Richter D.;
RT "Cloning of a cDNA encoding a novel putative G-protein-coupled receptor
RT expressed in specific rat brain regions.";
RL DNA Cell Biol. 10:689-694(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1400442; DOI=10.1016/s0021-9258(19)36609-8;
RA Li X.-J., Forte M.A., North R.A., Ross C.A., Snyder S.H.;
RT "Cloning and expression of a rat somatostatin receptor enriched in brain.";
RL J. Biol. Chem. 267:21307-21312(1992).
CC -!- FUNCTION: Receptor for somatostatin with higher affinity for
CC somatostatin-14 than -28. This receptor is coupled to phosphotyrosine
CC phosphatase and Na(+)/H(+) exchanger via pertussis toxin insensitive G
CC proteins.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Brain, pituitary, islet, jejunum, stomach, heart,
CC spleen.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X62314; CAA44193.1; -; mRNA.
DR EMBL; M97656; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A39297; A39297.
DR RefSeq; NP_036851.1; NM_012719.2.
DR RefSeq; XP_006240177.1; XM_006240115.2.
DR AlphaFoldDB; P28646; -.
DR SMR; P28646; -.
DR BioGRID; 247112; 1.
DR STRING; 10116.ENSRNOP00000067355; -.
DR BindingDB; P28646; -.
DR ChEMBL; CHEMBL4652; -.
DR DrugCentral; P28646; -.
DR GuidetoPHARMACOLOGY; 355; -.
DR GlyGen; P28646; 3 sites.
DR PhosphoSitePlus; P28646; -.
DR PaxDb; P28646; -.
DR PRIDE; P28646; -.
DR Ensembl; ENSRNOT00000073970; ENSRNOP00000067355; ENSRNOG00000048145.
DR GeneID; 25033; -.
DR KEGG; rno:25033; -.
DR UCSC; RGD:3762; rat.
DR CTD; 6751; -.
DR RGD; 3762; Sstr1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000161442; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; P28646; -.
DR OMA; PDNMESD; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; P28646; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P28646; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000048145; Expressed in frontal cortex and 8 other tissues.
DR Genevisible; P28646; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
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:0004994; F:somatostatin receptor activity; IMP:RGD.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0030900; P:forebrain development; IEP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; ISO:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISO:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0030217; P:T cell differentiation; NAS:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000586; Somatstn_rcpt.
DR InterPro; IPR001116; Somatstn_rcpt_1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00246; SOMATOSTATNR.
DR PRINTS; PR00587; SOMATOSTTN1R.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..391
FT /note="Somatostatin receptor type 1"
FT /id="PRO_0000070118"
FT TOPO_DOM 1..56
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..84
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..120
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..131
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..244
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..296
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..327
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 339
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 130..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 391 AA; 42746 MW; 28ED6E894B72FBB7 CRC64;
MFPNGTAPSP TSSPSSSPGG CGEGVCSRGP GSGAADGMEE PGRNSSQNGT LSEGQGSAIL
ISFIYSVVCL VGLCGNSMVI YVILRYAKMK TATNIYILNL AIADELLMLS VPFLVTSTLL
RHWPFGALLC RLVLSVDAVN MFTSIYCLTV LSVDRYVAVV HPIKAARYRR PTVAKVVNLG
VWVLSLLVIL PIVVFSRTAA NSDGTVACNM LMPEPAQRWL VGFVLYTFLM GFLLPVGAIC
LCYVLIIAKM RMVALKAGWQ QRKRSERKIT LMVMMVVMVF VICWMPFYVV QLVNVFAEQD
DATVSQLSVI LGYANSCANP ILYGFLSDNF KRSFQRILCL SWMDNAAEEP VDYYATALKS
RAYSVEDFQP ENLESGGVFR NGTCASRIST L
