SSR2_HUMAN
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 03-AUG-2022, entry version 192.
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}.
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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 PDBsum; 7T10; -.
DR PDBsum; 7T11; -.
DR AlphaFoldDB; P30874; -.
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 GlyGen; P30874; 4 sites.
DR iPTMnet; P30874; -.
DR PhosphoSitePlus; P30874; -.
DR BioMuta; SSTR2; -.
DR DMDM; 401126; -.
DR jPOST; P30874; -.
DR MassIVE; P30874; -.
DR PaxDb; P30874; -.
DR PeptideAtlas; P30874; -.
DR PRIDE; P30874; -.
DR ProteomicsDB; 54743; -. [P30874-1]
DR ProteomicsDB; 54744; -. [P30874-2]
DR ABCD; P30874; 9 sequenced antibodies.
DR Antibodypedia; 1548; 389 antibodies from 36 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 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; NGCFCTI; -.
DR OrthoDB; 1011272at2759; -.
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 1071 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 130 other tissues.
DR Genevisible; P30874; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
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:0006937; P:regulation of muscle contraction; IEA:Ensembl.
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; IPR002074; Somatstn_rcpt_2.
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 PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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"
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
