ID   SSR3_MOUSE              Reviewed;         428 AA.
AC   P30935; Q0VB04; Q3UVV5;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 164.
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; Synonyms=Smstr3;
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], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=1328199; DOI=10.1016/s0021-9258(19)88719-7;
RA   Yasuda K., Rens-Domiano S., Breder C.D., Law S.F., Saper C.B., Reisine T.,
RA   Bell G.I.;
RT   "Cloning of a novel somatostatin receptor, SSTR3, coupled to
RT   adenylylcyclase.";
RL   J. Biol. Chem. 267:20422-20428(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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 and -28. This receptor is
CC       coupled via pertussis toxin sensitive G proteins to inhibition of
CC       adenylyl cyclase. {ECO:0000269|PubMed:1328199}.
CC   -!- SUBUNIT: Homodimer and heterodimer with SSTR2. Heterodimerization with
CC       SSTR2 inactivates SSTR3 receptor function (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Note=Internalized into endoplasmic vesicles upon
CC       somatostatin-stimulation. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: In the brain, primarily observed in the forebrain.
CC       Moderate levels found throughout laminae 2-6 of the neocortex and
CC       allocortex, and high levels in lamina 2 of the piriform and entorhinal
CC       cortices. High levels also present in the cornu ammonis fields of the
CC       hippocampus. In the amygdala, highly expressed in the nucleus of the
CC       lateral olfactory tract with expression also detected in the rostral
CC       portions of the basal magnocellular and lateral nuclei. In the
CC       diencephalon, moderate levels observed in the ventromedial and arcuate
CC       nuclei of the hypothalamus. In the midbrain, moderate levels found in
CC       the lateral portion of the substantia nigra pars reticulata.
CC       {ECO:0000269|PubMed:1328199}.
CC   -!- PTM: Phosphorylated. Phosphorylation increases upon somatostatin
CC       binding (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; M91000; AAA40144.1; -; Genomic_DNA.
DR   EMBL; AK136904; BAE23164.1; -; mRNA.
DR   EMBL; AL590144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC120843; AAI20844.1; -; mRNA.
DR   EMBL; BC137670; AAI37671.1; -; mRNA.
DR   CCDS; CCDS27617.1; -.
DR   PIR; A44021; A44021.
DR   RefSeq; NP_033244.2; NM_009218.3.
DR   RefSeq; XP_006520732.1; XM_006520669.3.
DR   RefSeq; XP_006520733.1; XM_006520670.3.
DR   RefSeq; XP_011243833.1; XM_011245531.1.
DR   AlphaFoldDB; P30935; -.
DR   SMR; P30935; -.
DR   IntAct; P30935; 9.
DR   STRING; 10090.ENSMUSP00000058040; -.
DR   BindingDB; P30935; -.
DR   ChEMBL; CHEMBL2238; -.
DR   DrugCentral; P30935; -.
DR   GuidetoPHARMACOLOGY; 357; -.
DR   GlyCosmos; P30935; 2 sites, No reported glycans.
DR   GlyGen; P30935; 2 sites.
DR   iPTMnet; P30935; -.
DR   PhosphoSitePlus; P30935; -.
DR   MaxQB; P30935; -.
DR   PaxDb; 10090-ENSMUSP00000058040; -.
DR   ProteomicsDB; 257078; -.
DR   Antibodypedia; 74216; 221 antibodies from 32 providers.
DR   DNASU; 20607; -.
DR   Ensembl; ENSMUST00000053239.4; ENSMUSP00000058040.3; ENSMUSG00000044933.4.
DR   GeneID; 20607; -.
DR   KEGG; mmu:20607; -.
DR   UCSC; uc007wpo.1; mouse.
DR   AGR; MGI:98329; -.
DR   CTD; 6753; -.
DR   MGI; MGI:98329; Sstr3.
DR   VEuPathDB; HostDB:ENSMUSG00000044933; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000162038; -.
DR   HOGENOM; CLU_009579_8_1_1; -.
DR   InParanoid; P30935; -.
DR   OMA; NTSSAWP; -.
DR   OrthoDB; 5393360at2759; -.
DR   PhylomeDB; P30935; -.
DR   TreeFam; TF315737; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
DR   BioGRID-ORCS; 20607; 1 hit in 80 CRISPR screens.
DR   PRO; PR:P30935; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; P30935; Protein.
DR   Bgee; ENSMUSG00000044933; Expressed in islet of Langerhans and 70 other cell types or tissues.
DR   ExpressionAtlas; P30935; baseline and differential.
DR   GO; GO:0060170; C:ciliary membrane; IDA:MGI.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0097730; C:non-motile cilium; IDA:BHF-UCL.
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:0005102; F:signaling receptor binding; IPI:MGI.
DR   GO; GO:0004994; F:somatostatin receptor activity; IEA:InterPro.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
DR   GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
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; IPR001856; Somatstn_rcpt_3.
DR   PANTHER; PTHR24229; NEUROPEPTIDES RECEPTOR; 1.
DR   PANTHER; PTHR24229:SF42; SOMATOSTATIN RECEPTOR TYPE 3; 1.
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   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; P30935; MM.
PE   2: Evidence at transcript 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_0000070125"
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          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..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:0000250|UniProtKB:P30936"
FT   MOD_RES         346
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30936"
FT   MOD_RES         351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30936"
FT   MOD_RES         357
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P30936"
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   CONFLICT        12
FT                   /note="T -> M (in Ref. 1; AAA40144 and 4;
FT                   AAI20844/AAI37671)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        19
FT                   /note="A -> T (in Ref. 1; AAA40144 and 4;
FT                   AAI20844/AAI37671)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        166
FT                   /note="A -> R (in Ref. 1; AAA40144)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        211
FT                   /note="T -> M (in Ref. 1; AAA40144)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   428 AA;  47216 MW;  5B1010167AD8780F CRC64;
     MATVTYPSSE PTTLDPGNAS STWPLDTTLG NTSAGASLTG LAVSGILISL VYLVVCVVGL
     LGNSLVIYVV LRHTSSPSVT SVYILNLALA DELFMLGLPF LAAQNALSYW PFGSLMCRLV
     MAVDGINQFT SIFCLTVMSV DRYLAVVHPT RSARWRTAPV ARTVSAAVWV ASAVVVLPVV
     VFSGVPRGMS TCHMQWPEPA AAWRTAFIIY TAALGFFGPL LVICLCYLLI VVKVRSTTRR
     VRAPSCQWVQ APACQRRRRS ERRVTRMVVA VVALFVLCWM PFYLLNIVNV VCPLPEEPAF
     FGLYFLVVAL PYANSCANPI LYGFLSYRFK QGFRRILLRP SRRIRSQEPG SGPPEKTEEE
     EDEEEEERRE EEERRMQRGQ EMNGRLSQIA QAGTSGQQPR PCTGTAKEQQ LLPQEATAGD
     KASTLSHL
//