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   24-JAN-2024, entry version 169.
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.ENSMUSP00000037045; -.
DR   BindingDB; P30873; -.
DR   ChEMBL; CHEMBL4242; -.
DR   DrugCentral; P30873; -.
DR   GuidetoPHARMACOLOGY; 355; -.
DR   GlyCosmos; P30873; 3 sites, No reported glycans.
DR   GlyGen; P30873; 3 sites.
DR   iPTMnet; P30873; -.
DR   PhosphoSitePlus; P30873; -.
DR   SwissPalm; P30873; -.
DR   PaxDb; 10090-ENSMUSP00000106299; -.
DR   ProteomicsDB; 257077; -.
DR   Antibodypedia; 4061; 456 antibodies from 39 providers.
DR   DNASU; 20605; -.
DR   Ensembl; ENSMUST00000044299.3; ENSMUSP00000037045.3; ENSMUSG00000035431.5.
DR   Ensembl; ENSMUST00000110671.3; ENSMUSP00000106299.3; ENSMUSG00000035431.5.
DR   GeneID; 20605; -.
DR   KEGG; mmu:20605; -.
DR   UCSC; uc007npu.1; mouse.
DR   AGR; MGI:98327; -.
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; YFRDMRT; -.
DR   OrthoDB; 5393360at2759; -.
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 77 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 49 other cell types or tissues.
DR   ExpressionAtlas; P30873; baseline and differential.
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:0042923; F:neuropeptide 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   CDD; cd15970; 7tmA_SSTR1; 1.
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; IPR001116; Somatstn_rcpt_1.
DR   PANTHER; PTHR24229; NEUROPEPTIDES RECEPTOR; 1.
DR   PANTHER; PTHR24229:SF38; SOMATOSTATIN RECEPTOR TYPE 1; 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   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; P30873; MM.
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
//