SSR1_MOUSE
ID SSR1_MOUSE Reviewed; 391 AA.
AC P30873;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 161.
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; Synonyms=Smstr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1346068; DOI=10.1073/pnas.89.1.251;
RA Yamada Y., Post S.R., Wang K., Tager H.S., Bell G.I., Seino S.;
RT "Cloning and functional characterization of a family of human and mouse
RT somatostatin receptors expressed in brain, gastrointestinal tract, and
RT kidney.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:251-255(1992).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Receptor for somatostatin with higher affinity for
CC somatostatin-14 than -28. This receptor is coupled via pertussis toxin
CC sensitive G proteins to inhibition of adenylyl cyclase. In addition it
CC stimulates phosphotyrosine phosphatase and Na(+)/H(+) exchanger via
CC pertussis toxin insensitive G proteins.
CC -!- INTERACTION:
CC P30873; Q62108: Dlg4; NbExp=3; IntAct=EBI-7665262, EBI-300895;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Jejunum and stomach.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M81831; AAA58255.1; -; Genomic_DNA.
DR CCDS; CCDS36456.1; -.
DR PIR; C41795; C41795.
DR RefSeq; NP_033242.1; NM_009216.3.
DR RefSeq; XP_006515697.1; XM_006515634.3.
DR AlphaFoldDB; P30873; -.
DR SMR; P30873; -.
DR IntAct; P30873; 2.
DR MINT; P30873; -.
DR STRING; 10090.ENSMUSP00000106299; -.
DR BindingDB; P30873; -.
DR ChEMBL; CHEMBL4242; -.
DR DrugCentral; P30873; -.
DR GuidetoPHARMACOLOGY; 355; -.
DR GlyGen; P30873; 3 sites.
DR iPTMnet; P30873; -.
DR PhosphoSitePlus; P30873; -.
DR SwissPalm; P30873; -.
DR PaxDb; P30873; -.
DR PRIDE; P30873; -.
DR ProteomicsDB; 257077; -.
DR Antibodypedia; 4061; 433 antibodies from 39 providers.
DR DNASU; 20605; -.
DR Ensembl; ENSMUST00000044299; ENSMUSP00000037045; ENSMUSG00000035431.
DR Ensembl; ENSMUST00000110671; ENSMUSP00000106299; ENSMUSG00000035431.
DR GeneID; 20605; -.
DR KEGG; mmu:20605; -.
DR UCSC; uc007npu.1; mouse.
DR CTD; 6751; -.
DR MGI; MGI:98327; Sstr1.
DR VEuPathDB; HostDB:ENSMUSG00000035431; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000161442; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; P30873; -.
DR OMA; PDNMESD; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; P30873; -.
DR TreeFam; TF315737; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 20605; 3 hits in 72 CRISPR screens.
DR PRO; PR:P30873; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P30873; protein.
DR Bgee; ENSMUSG00000035431; Expressed in dentate gyrus of hippocampal formation granule cell and 48 other tissues.
DR ExpressionAtlas; P30873; baseline and differential.
DR Genevisible; P30873; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:MGI.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; IDA:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:MGI.
DR GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
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 1: Evidence at protein 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_0000070117"
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; 42718 MW; 4461673956F2BD22 CRC64;
MFPNGTASSP SSSPSPSPGS CGEGACSRGP GSGAADGMEE PGRNASQNGT 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
