ID SSR4_MOUSE Reviewed; 385 AA. AC P49660; Q8BQ97; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 28-JAN-2026, sequence version 3. DT 02-SEP-2026, entry version 162. DE RecName: Full=Somatostatin receptor type 4; DE Short=SS-4-R; DE Short=SS4-R; DE Short=SS4R; GN Name=Sstr4; Synonyms=Smstr4; 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]. RC STRAIN=129/SvJ; TISSUE=Liver; RX PubMed=8654950; DOI=10.1016/0378-1119(95)00748-2; RA Schwabe W., Brennan M.B., Hochgeschwender U.; RT "Isolation and characterization of the mouse (Mus musculus) somatostatin RT receptor type-4-encoding gene (mSSTR4)."; RL Gene 168:233-235(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CAST/EiJ; TISSUE=Brain; RX PubMed=16670015; DOI=10.1186/1471-2164-7-102; RA Farber C.R., Corva P.M., Medrano J.F.; RT "Genome-wide isolation of growth and obesity QTL using mouse speed congenic RT strains."; RL BMC Genomics 7:102-102(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Receptor for somatostatin-14. The activity of this receptor CC is mediated by G proteins which inhibits adenylyl cyclase. It is CC functionally coupled not only to inhibition of adenylate cyclase, but CC also to activation of both arachidonate release and mitogen-activated CC protein (MAP) kinase cascade. CC -!- INTERACTION: CC P49660; Q62108: Dlg4; NbExp=3; IntAct=EBI-7665342, EBI-300895; CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. 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; U26176; AAA67561.1; -; Genomic_DNA. DR EMBL; AY902332; AAX90617.1; -; Genomic_DNA. DR EMBL; AK051189; BAC34552.1; -; mRNA. DR EMBL; AL935149; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC138487; AAI38488.1; -; mRNA. DR EMBL; BC138488; AAI38489.1; -; mRNA. DR CCDS; CCDS38260.1; -. DR PIR; JC4629; JC4629. DR RefSeq; NP_033245.2; NM_009219.3. DR AlphaFoldDB; P49660; -. DR SMR; P49660; -. DR FunCoup; P49660; 568. DR IntAct; P49660; 2. DR MINT; P49660; -. DR STRING; 10090.ENSMUSP00000105588; -. DR BindingDB; P49660; -. DR ChEMBL; CHEMBL4397; -. DR DrugCentral; P49660; -. DR GuidetoPHARMACOLOGY; 358; -. DR GlyCosmos; P49660; 1 site, No reported glycans. DR GlyGen; P49660; 1 site. DR PhosphoSitePlus; P49660; -. DR SwissPalm; P49660; -. DR PaxDb; 10090-ENSMUSP00000105588; -. DR ABCD; P49660; 21 sequenced antibodies. DR DNASU; 20608; -. DR Ensembl; ENSMUST00000109962.4; ENSMUSP00000105588.3; ENSMUSG00000037014.5. DR GeneID; 20608; -. DR KEGG; mmu:20608; -. DR UCSC; uc008mtc.1; mouse. DR AGR; MGI:105372; -. DR CTD; 6754; -. DR MGI; MGI:105372; Sstr4. DR eggNOG; KOG3656; Eukaryota. DR InParanoid; P49660; -. DR OrthoDB; 6076970at2759; -. DR Reactome; R-MMU-375276; Peptide ligand-binding receptors. DR Reactome; R-MMU-418594; G alpha (i) signalling events. DR BioGRID-ORCS; 20608; 1 hit in 77 CRISPR screens. DR PRO; PR:P49660; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P49660; protein. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central. DR GO; GO:0004994; F:somatostatin receptor activity; ISO:GO_Central. DR GO; GO:0016477; P:cell migration; ISO:GO_Central. DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IBA:GO_Central. DR GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:GO_Central. DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central. DR GO; GO:0090238; P:positive regulation of arachidonate secretion; ISO:GO_Central. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:GO_Central. DR CDD; cd15973; 7tmA_SSTR4; 1. DR FunFam; 1.20.1070.10:FF:000060; Somatostatin receptor type 1; 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; IPR001512; Somatstn_rcpt_4. DR PANTHER; PTHR24229; NEUROPEPTIDES RECEPTOR; 1. DR PANTHER; PTHR24229:SF35; SOMATOSTATIN RECEPTOR TYPE 4; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00246; SOMATOSTATNR. DR PRINTS; PR00590; SOMATOSTTN4R. 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. 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..385 FT /note="Somatostatin receptor type 4" FT /id="PRO_0000070128" FT TOPO_DOM 1..42 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 43..70 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 71..80 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 81..106 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 107..117 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 118..139 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 140..161 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 162..182 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 183..204 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 205..229 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 230..255 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 256..281 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 282..288 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 289..312 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 313..385 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 1..37 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT LIPID 324 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000255" FT CARBOHYD 21 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 116..195 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT CONFLICT 8..9 FT /note="PP -> LR (in Ref. 1; AAA67561)" FT /evidence="ECO:0000305" FT CONFLICT 27..29 FT /note="DEE -> EQ (in Ref. 1; AAA67561)" FT /evidence="ECO:0000305" FT CONFLICT 101 FT /note="A -> R (in Ref. 1; AAA67561)" FT /evidence="ECO:0000305" FT CONFLICT 151 FT /note="A -> T (in Ref. 1; AAA67561)" FT /evidence="ECO:0000305" FT CONFLICT 219 FT /note="L -> P (in Ref. 1; AAA67561)" FT /evidence="ECO:0000305" FT CONFLICT 242 FT /note="A -> G (in Ref. 1; AAA67561)" FT /evidence="ECO:0000305" SQ SEQUENCE 385 AA; 42046 MW; 41E31230BCBE9ACB CRC64; MNAPATLPPG VEDTTWTPGI NASWAPDEEE EDAMGSDGTG TAGMVTIQCI YALVCLVGLV GNALVIFVIL RYAKMKTATN IYLLNLAVAD ELFMLSVPFV ASAAALRHWP FGAVLCRAVL SVDGLNMFTS VFCLTVLSVD RYVAVVHPLR AATYRRPSVA KLINLGVWLA SLLVTLPIAV FADTRPARGG EAVACNLHWP HPAWSAVFVI YTFLLGFLLP VLAIGLCYLL IVGKMRAVAL RAGWQQRRRS EKKITRLVLM VVTVFVLCWM PFYVVQLLNL FVTSLDATVN HVSLILSYAN SCANPILYGF LSDNFRRSFQ RVLCLRCCLL ETTGGAEEEP LDYYATALKS RGGAGCICPP LPCQQEPVQA EPGCKQVPFT KTTTF //