SSR3_MOUSE
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 03-AUG-2022, entry version 156.
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 GlyGen; P30935; 2 sites.
DR iPTMnet; P30935; -.
DR PhosphoSitePlus; P30935; -.
DR MaxQB; P30935; -.
DR PaxDb; P30935; -.
DR PRIDE; P30935; -.
DR ProteomicsDB; 257078; -.
DR Antibodypedia; 74216; 182 antibodies from 32 providers.
DR DNASU; 20607; -.
DR Ensembl; ENSMUST00000053239; ENSMUSP00000058040; ENSMUSG00000044933.
DR GeneID; 20607; -.
DR KEGG; mmu:20607; -.
DR UCSC; uc007wpo.1; mouse.
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; VCSQEPT; -.
DR OrthoDB; 1011272at2759; -.
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 75 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 tissues.
DR ExpressionAtlas; P30935; baseline and differential.
DR Genevisible; P30935; MM.
DR GO; GO:0060170; C:ciliary membrane; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0042277; F:peptide 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 InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000586; Somatstn_rcpt.
DR InterPro; IPR001856; Somatstn_rcpt_3.
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 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 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; AAI20844/
FT AAI37671)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="A -> T (in Ref. 1; AAA40144 and 4; AAI20844/
FT 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
