ID   SSR2_HUMAN              Reviewed;         369 AA.
AC   P30874; A8K3Y0; B2R9P7; Q4VBP0; Q96GE0; Q96TF2; Q9BWH1;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Somatostatin receptor type 2;
DE            Short=SS-2-R;
DE            Short=SS2-R;
DE            Short=SS2R;
DE            Short=SST2;
DE   AltName: Full=SRIF-1;
GN   Name=SSTR2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B).
RX   PubMed=10619399; DOI=10.1016/s0303-7207(99)00161-6;
RA   Petersenn S., Rasch A.C., Presch S., Beil F.U., Schulte H.M.;
RT   "Genomic structure and transcriptional regulation of the human somatostatin
RT   receptor type 2.";
RL   Mol. Cell. Endocrinol. 157:75-85(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT   "Isolation of complete coding sequence for somatostatin receptor 2
RT   (SSTR2).";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA   Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT   "Genome-wide discovery and analysis of human seven transmembrane helix
RT   receptor genes.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   TISSUE=Eye;
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).
RN   [8]
RP   ALTERNATIVE SPLICING (ISOFORMS A AND B).
RX   PubMed=8386508; DOI=10.1006/bbrc.1993.1412;
RA   Patel Y.C., Greenwood M., Kent G., Panetta R., Srikant C.B.;
RT   "Multiple gene transcripts of the somatostatin receptor SSTR2: tissue
RT   selective distribution and cAMP regulation.";
RL   Biochem. Biophys. Res. Commun. 192:288-294(1993).
RN   [9]
RP   INTERACTION WITH SHANK1.
RX   PubMed=10551867; DOI=10.1074/jbc.274.46.32997;
RA   Zitzer H., Hoenck H.-H., Baechner D., Richter D., Kreienkamp H.-J.;
RT   "Somatostatin receptor interacting protein defines a novel family of
RT   multidomain proteins present in human and rodent brain.";
RL   J. Biol. Chem. 274:32997-33001(1999).
RN   [10]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=15231824; DOI=10.1074/jbc.m407310200;
RA   Grant M., Collier B., Kumar U.;
RT   "Agonist-dependent dissociation of human somatostatin receptor 2 dimers: a
RT   role in receptor trafficking.";
RL   J. Biol. Chem. 279:36179-36183(2004).
RN   [11]
RP   FUNCTION, SUBUNIT, INTERACTION WITH BETA-ARRESTIN, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=18653781; DOI=10.1210/me.2007-0334;
RA   Grant M., Alturaihi H., Jaquet P., Collier B., Kumar U.;
RT   "Cell growth inhibition and functioning of human somatostatin receptor type
RT   2 are modulated by receptor heterodimerization.";
RL   Mol. Endocrinol. 22:2278-2292(2008).
RN   [12]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=19434240; DOI=10.1371/journal.pone.0005509;
RA   Le Verche V., Kaindl A.M., Verney C., Csaba Z., Peineau S., Olivier P.,
RA   Adle-Biassette H., Leterrier C., Vitalis T., Renaud J., Dargent B.,
RA   Gressens P., Dournaud P.;
RT   "The somatostatin 2A receptor is enriched in migrating neurons during rat
RT   and human brain development and stimulates migration and axonal
RT   outgrowth.";
RL   PLoS ONE 4:E5509-E5509(2009).
RN   [13]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=22932785; DOI=10.1152/ajpendo.00207.2012;
RA   Kailey B., van de Bunt M., Cheley S., Johnson P.R., MacDonald P.E.,
RA   Gloyn A.L., Rorsman P., Braun M.;
RT   "SSTR2 is the functionally dominant somatostatin receptor in human
RT   pancreatic beta- and alpha-cells.";
RL   Am. J. Physiol. 303:E1107-E1116(2012).
RN   [14]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-89; ASP-139 AND
RP   ARG-140.
RX   PubMed=22495673; DOI=10.1210/en.2011-1662;
RA   Parry J.J., Chen R., Andrews R., Lears K.A., Rogers B.E.;
RT   "Identification of critical residues involved in ligand binding and G
RT   protein signaling in human somatostatin receptor subtype 2.";
RL   Endocrinology 153:2747-2755(2012).
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. In addition it stimulates phosphotyrosine phosphatase
CC       and PLC via pertussis toxin insensitive as well as sensitive G
CC       proteins. Inhibits calcium entry by suppressing voltage-dependent
CC       calcium channels. Acts as the functionally dominant somatostatin
CC       receptor in pancreatic alpha- and beta-cells where it mediates the
CC       inhibitory effect of somatostatin-14 on hormone secretion. Inhibits
CC       cell growth through enhancement of MAPK1 and MAPK2 phosphorylation and
CC       subsequent up-regulation of CDKN1B. Stimulates neuronal migration and
CC       axon outgrowth and may participate in neuron development and maturation
CC       during brain development. Mediates negative regulation of insulin
CC       receptor signaling through PTPN6. Inactivates SSTR3 receptor function
CC       following heterodimerization. {ECO:0000269|PubMed:15231824,
CC       ECO:0000269|PubMed:18653781, ECO:0000269|PubMed:19434240,
CC       ECO:0000269|PubMed:22495673, ECO:0000269|PubMed:22932785}.
CC   -!- SUBUNIT: Homodimer and heterodimer with SSTR3 and SSTR5.
CC       Heterodimerization with SSTR3 inactivates SSTR3 receptor function.
CC       Heterodimerization with SSTR5 is enhanced by agonist stimulation of
CC       SSTR2 and increases SSTR2 cell growth inhibition activity. Following
CC       agonist stimulation, homodimers dissociate into monomers which is
CC       required for receptor internalization. Interacts with beta-arrestin;
CC       this interaction is necessary for receptor internalization and is
CC       destabilized by heterodimerization with SSTR5 which results in
CC       increased recycling of SSTR2 to the cell surface. Interacts (via C-
CC       terminus) with SHANK1 (via PDZ domain). {ECO:0000269|PubMed:10551867,
CC       ECO:0000269|PubMed:15231824, ECO:0000269|PubMed:18653781}.
CC   -!- INTERACTION:
CC       P30874; P27986: PIK3R1; NbExp=5; IntAct=EBI-6266898, EBI-79464;
CC       P30874; P32745: SSTR3; NbExp=3; IntAct=EBI-6266898, EBI-6266935;
CC       P30874; P35346: SSTR5; NbExp=4; IntAct=EBI-6266898, EBI-27053622;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cytoplasm. Note=Located mainly at the cell surface under basal
CC       conditions. Agonist stimulation results in internalization to the
CC       cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A; Synonyms=SSTR2A;
CC         IsoId=P30874-1; Sequence=Displayed;
CC       Name=B; Synonyms=SSTR2B;
CC         IsoId=P30874-2; Sequence=VSP_001922;
CC   -!- TISSUE SPECIFICITY: Expressed in both pancreatic alpha- and beta-cells
CC       (at protein level). Expressed at higher levels in the pancreas than
CC       other somatostatin receptors. Also expressed in the cerebrum and kidney
CC       and, in lesser amounts, in the jejunum, colon and liver. In the
CC       developing nervous system, expressed in the cortex where it is located
CC       in the preplate at early stages and is enriched in the outer part of
CC       the germinal zone at later stages. In the cerebellum, expressed in the
CC       deep part of the external granular layer at gestational week 19. This
CC       pattern persists until birth but disappears at adulthood.
CC       {ECO:0000269|PubMed:19434240, ECO:0000269|PubMed:22932785}.
CC   -!- PTM: Phosphorylated on serine and threonine residues in response to
CC       agonist stimulation, leading to receptor desensitization and rapid
CC       internalization. Phosphorylated to a greater extent on serine than
CC       threonine residues. Threonine phosphorylation is required for arrestin
CC       binding and receptor endocytosis but is not necessary for
CC       desensitization (By similarity). {ECO:0000250}.
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; M81830; AAA58248.1; -; Genomic_DNA.
DR   EMBL; AY236542; AAO92064.1; -; Genomic_DNA.
DR   EMBL; AF184174; AAF42809.1; -; Genomic_DNA.
DR   EMBL; AF184174; AAF42810.1; -; Genomic_DNA.
DR   EMBL; AB065911; BAC06126.1; -; Genomic_DNA.
DR   EMBL; AK290745; BAF83434.1; -; mRNA.
DR   EMBL; AK313866; BAG36594.1; -; mRNA.
DR   EMBL; BT019926; AAV38729.1; -; mRNA.
DR   EMBL; BC000256; AAH00256.1; -; mRNA.
DR   EMBL; BC009522; AAH09522.1; -; mRNA.
DR   EMBL; BC019610; AAH19610.1; -; mRNA.
DR   EMBL; BC095495; AAH95495.1; -; mRNA.
DR   CCDS; CCDS11691.1; -. [P30874-1]
DR   PIR; B41795; B41795.
DR   RefSeq; NP_001041.1; NM_001050.2. [P30874-1]
DR   PDB; 7T10; EM; 2.50 A; R=1-237, R=253-369.
DR   PDB; 7T11; EM; 2.70 A; R=1-237, R=253-369.
DR   PDB; 7UL5; EM; 3.10 A; A=1-237, A=254-369.
DR   PDB; 7WIC; EM; 2.80 A; R=1-369.
DR   PDB; 7WIG; EM; 2.70 A; R=1-369.
DR   PDB; 7WJ5; EM; 3.72 A; R=1-369.
DR   PDB; 7XAT; EM; 2.85 A; A=1-361.
DR   PDB; 7XAU; EM; 2.97 A; A=1-361.
DR   PDB; 7XAV; EM; 2.87 A; A=1-361.
DR   PDB; 7XMR; EM; 3.10 A; R=2-359.
DR   PDB; 7Y24; EM; 3.25 A; E=1-327.
DR   PDB; 7Y26; EM; 3.30 A; E=1-337.
DR   PDB; 7Y27; EM; 3.48 A; E=1-337.
DR   PDB; 7YAC; EM; 3.24 A; E=31-338.
DR   PDB; 7YAE; EM; 3.37 A; E=1-369.
DR   PDBsum; 7T10; -.
DR   PDBsum; 7T11; -.
DR   PDBsum; 7UL5; -.
DR   PDBsum; 7WIC; -.
DR   PDBsum; 7WIG; -.
DR   PDBsum; 7WJ5; -.
DR   PDBsum; 7XAT; -.
DR   PDBsum; 7XAU; -.
DR   PDBsum; 7XAV; -.
DR   PDBsum; 7XMR; -.
DR   PDBsum; 7Y24; -.
DR   PDBsum; 7Y26; -.
DR   PDBsum; 7Y27; -.
DR   PDBsum; 7YAC; -.
DR   PDBsum; 7YAE; -.
DR   AlphaFoldDB; P30874; -.
DR   EMDB; EMD-26592; -.
DR   EMDB; EMD-32528; -.
DR   EMDB; EMD-32529; -.
DR   EMDB; EMD-33098; -.
DR   EMDB; EMD-33099; -.
DR   EMDB; EMD-33100; -.
DR   EMDB; EMD-33302; -.
DR   EMDB; EMD-33585; -.
DR   EMDB; EMD-33586; -.
DR   EMDB; EMD-33587; -.
DR   EMDB; EMD-33708; -.
DR   SMR; P30874; -.
DR   BioGRID; 112630; 62.
DR   CORUM; P30874; -.
DR   IntAct; P30874; 4.
DR   MINT; P30874; -.
DR   STRING; 9606.ENSP00000350198; -.
DR   BindingDB; P30874; -.
DR   ChEMBL; CHEMBL1804; -.
DR   DrugBank; DB15873; Copper oxodotreotide Cu-64.
DR   DrugBank; DB13925; Dotatate gallium Ga-68.
DR   DrugBank; DB15494; Edotreotide gallium Ga-68.
DR   DrugBank; DB06791; Lanreotide.
DR   DrugBank; DB13985; Lutetium Lu 177 dotatate.
DR   DrugBank; DB06663; Pasireotide.
DR   DrugBank; DB09099; Somatostatin.
DR   DrugBank; DB04894; Vapreotide.
DR   DrugCentral; P30874; -.
DR   GuidetoPHARMACOLOGY; 356; -.
DR   GlyCosmos; P30874; 4 sites, No reported glycans.
DR   GlyGen; P30874; 4 sites.
DR   iPTMnet; P30874; -.
DR   PhosphoSitePlus; P30874; -.
DR   BioMuta; SSTR2; -.
DR   DMDM; 401126; -.
DR   jPOST; P30874; -.
DR   MassIVE; P30874; -.
DR   PaxDb; 9606-ENSP00000350198; -.
DR   PeptideAtlas; P30874; -.
DR   ProteomicsDB; 54743; -. [P30874-1]
DR   ProteomicsDB; 54744; -. [P30874-2]
DR   ABCD; P30874; 9 sequenced antibodies.
DR   Antibodypedia; 1548; 455 antibodies from 37 providers.
DR   DNASU; 6752; -.
DR   Ensembl; ENST00000357585.4; ENSP00000350198.2; ENSG00000180616.9. [P30874-1]
DR   GeneID; 6752; -.
DR   KEGG; hsa:6752; -.
DR   MANE-Select; ENST00000357585.4; ENSP00000350198.2; NM_001050.3; NP_001041.1.
DR   UCSC; uc002jje.4; human. [P30874-1]
DR   AGR; HGNC:11331; -.
DR   CTD; 6752; -.
DR   DisGeNET; 6752; -.
DR   GeneCards; SSTR2; -.
DR   HGNC; HGNC:11331; SSTR2.
DR   HPA; ENSG00000180616; Tissue enhanced (brain).
DR   MIM; 182452; gene.
DR   neXtProt; NX_P30874; -.
DR   OpenTargets; ENSG00000180616; -.
DR   PharmGKB; PA36155; -.
DR   VEuPathDB; HostDB:ENSG00000180616; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000156544; -.
DR   HOGENOM; CLU_009579_8_1_1; -.
DR   InParanoid; P30874; -.
DR   OMA; SSSCTMI; -.
DR   OrthoDB; 5393360at2759; -.
DR   PhylomeDB; P30874; -.
DR   TreeFam; TF315737; -.
DR   PathwayCommons; P30874; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; P30874; -.
DR   SIGNOR; P30874; -.
DR   BioGRID-ORCS; 6752; 9 hits in 1155 CRISPR screens.
DR   ChiTaRS; SSTR2; human.
DR   GeneWiki; Somatostatin_receptor_2; -.
DR   GenomeRNAi; 6752; -.
DR   Pharos; P30874; Tclin.
DR   PRO; PR:P30874; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P30874; Protein.
DR   Bgee; ENSG00000180616; Expressed in buccal mucosa cell and 131 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR   GO; GO:0004994; F:somatostatin receptor activity; IBA:GO_Central.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; IBA:GO_Central.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IBA:GO_Central.
DR   GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0030432; P:peristalsis; IEA:Ensembl.
DR   GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   CDD; cd15971; 7tmA_SSTR2; 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; IPR002074; Somatstn_rcpt_2.
DR   PANTHER; PTHR24229; NEUROPEPTIDES RECEPTOR; 1.
DR   PANTHER; PTHR24229:SF6; SOMATOSTATIN RECEPTOR TYPE 2; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00246; SOMATOSTATNR.
DR   PRINTS; PR00588; SOMATOSTTN2R.
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; P30874; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW   Disulfide bond; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..369
FT                   /note="Somatostatin receptor type 2"
FT                   /id="PRO_0000070120"
FT   TOPO_DOM        1..43
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..67
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..78
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..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..138
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..181
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        182..207
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..229
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..253
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..278
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        279..288
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..303
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..369
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   SITE            89
FT                   /note="Important for ligand binding"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30680"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30680"
FT   MOD_RES         348
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30680"
FT   MOD_RES         353
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P30680"
FT   MOD_RES         354
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P30680"
FT   LIPID           328
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        9
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        115..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VAR_SEQ         332..369
FT                   /note="VSGTDDGERSDSKQDKSRLNETTETQRTLLNGDLQTSI -> VDNSKSGEEG
FT                   SCLDMIFRNNKNRKK (in isoform B)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001922"
FT   MUTAGEN         89
FT                   /note="D->A: Expression levels reduced by 60%."
FT                   /evidence="ECO:0000269|PubMed:22495673"
FT   MUTAGEN         89
FT                   /note="D->L: Expression levels reduced by 80%."
FT                   /evidence="ECO:0000269|PubMed:22495673"
FT   MUTAGEN         89
FT                   /note="D->R: Slightly reduced expression levels. Remains
FT                   localized in membrane. Abolishes ligand binding and G
FT                   protein-mediated calcium release."
FT                   /evidence="ECO:0000269|PubMed:22495673"
FT   MUTAGEN         139
FT                   /note="D->A: Expression levels reduced by 50%.
FT                   Significantly reduced ligand binding capacity but increased
FT                   affinity. Reduced G protein-mediated cAMP release but no
FT                   effect on G-protein mediated calcium release."
FT                   /evidence="ECO:0000269|PubMed:22495673"
FT   MUTAGEN         139
FT                   /note="D->N: Expression levels reduced by 40%. No
FT                   significant change in ligand binding capacity or affinity.
FT                   Reduced G protein-mediated cAMP signaling but no effect on
FT                   G protein-mediated calcium release."
FT                   /evidence="ECO:0000269|PubMed:22495673"
FT   MUTAGEN         140
FT                   /note="R->A: Slightly reduced expression levels. No
FT                   significant change in ligand binding capacity or affinity.
FT                   No significant change in G protein-mediated cAMP or calcium
FT                   release."
FT                   /evidence="ECO:0000269|PubMed:22495673"
FT   MUTAGEN         140
FT                   /note="R->E: Almost abolishes expression. Abolishes
FT                   membrane localization."
FT                   /evidence="ECO:0000269|PubMed:22495673"
FT   MUTAGEN         140
FT                   /note="R->L: Slightly reduced expression levels.
FT                   Significantly reduced ligand binding capacity but increased
FT                   affinity. Reduced G protein-mediated cAMP release but no
FT                   effect on G protein-mediated calcium release."
FT                   /evidence="ECO:0000269|PubMed:22495673"
FT   CONFLICT        77
FT                   /note="I -> T (in Ref. 5; BAG36594)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="D -> N (in Ref. 5; BAG36594)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="T -> A (in Ref. 5; BAG36594)"
FT                   /evidence="ECO:0000305"
FT   HELIX           41..69
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:7XAU"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:7WIC"
FT   HELIX           77..92
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:7Y26"
FT   HELIX           96..104
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   HELIX           112..145
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   HELIX           156..173
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   HELIX           175..179
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   STRAND          187..189
FT                   /evidence="ECO:0007829|PDB:7XAT"
FT   STRAND          191..195
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   HELIX           198..200
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   HELIX           204..216
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   HELIX           218..237
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   TURN            239..242
FT                   /evidence="ECO:0007829|PDB:7XAT"
FT   HELIX           247..250
FT                   /evidence="ECO:0007829|PDB:7XAV"
FT   HELIX           253..281
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   HELIX           288..300
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   HELIX           303..312
FT                   /evidence="ECO:0007829|PDB:7T10"
FT   TURN            313..315
FT                   /evidence="ECO:0007829|PDB:7T11"
FT   HELIX           317..319
FT                   /evidence="ECO:0007829|PDB:7Y26"
FT   HELIX           320..326
FT                   /evidence="ECO:0007829|PDB:7T10"
SQ   SEQUENCE   369 AA;  41333 MW;  3B5D7D8A9AC246C6 CRC64;
     MDMADEPLNG SHTWLSIPFD LNGSVVSTNT SNQTEPYYDL TSNAVLTFIY FVVCIIGLCG
     NTLVIYVILR YAKMKTITNI YILNLAIADE LFMLGLPFLA MQVALVHWPF GKAICRVVMT
     VDGINQFTSI FCLTVMSIDR YLAVVHPIKS AKWRRPRTAK MITMAVWGVS LLVILPIMIY
     AGLRSNQWGR SSCTINWPGE SGAWYTGFII YTFILGFLVP LTIICLCYLF IIIKVKSSGI
     RVGSSKRKKS EKKVTRMVSI VVAVFIFCWL PFYIFNVSSV SMAISPTPAL KGMFDFVVVL
     TYANSCANPI LYAFLSDNFK KSFQNVLCLV KVSGTDDGER SDSKQDKSRL NETTETQRTL
     LNGDLQTSI
//