SSR2_BOVIN
ID SSR2_BOVIN Reviewed; 368 AA.
AC P34993;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Somatostatin receptor type 2;
DE Short=SS-2-R;
DE Short=SS2-R;
DE Short=SS2R;
DE AltName: Full=SRIF-1;
GN Name=SSTR2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Xin W.W., Wong M.-L., Rimland J., Nestler E.J., Duman R.S.;
RT "Characterization and functional expression of a somatostatin receptor
RT isolated from locus Coeruleus.";
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Cytoplasm {ECO:0000250}. Note=Located mainly at the cell surface under
CC basal conditions. Agonist stimulation results in internalization to the
CC cytoplasm (By similarity). {ECO:0000250}.
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; L06613; AAA30764.1; -; mRNA.
DR RefSeq; NP_776892.1; NM_174467.1.
DR AlphaFoldDB; P34993; -.
DR SMR; P34993; -.
DR STRING; 9913.ENSBTAP00000022785; -.
DR PaxDb; P34993; -.
DR GeneID; 282083; -.
DR KEGG; bta:282083; -.
DR CTD; 6752; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P34993; -.
DR OrthoDB; 1011272at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004994; F:somatostatin receptor activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..368
FT /note="Somatostatin receptor type 2"
FT /id="PRO_0000070119"
FT TOPO_DOM 1..42
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..180
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..302
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30680"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30680"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30680"
FT MOD_RES 352
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30680"
FT MOD_RES 353
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30680"
FT LIPID 327
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
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 114..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 368 AA; 41134 MW; B5852262A6BB080B CRC64;
MDLVSELNET QPWLTTPFDL NGSVGAANIS NQTEPYYDLA SNVVLTFIYF VVCIIGLCGN
TLVIYVILRY AKMKTITNIY ILNLAIADEL FMLGLPFLAM QVALVHWPFG KAICRVVMTV
DGINQFTSIF CLTVMSIDRY LAVVHPIKSA KWRRPRTAKM INVAVWGVSL LVILPIMIYA
GLRSNQWGRS SCTINWPGES GAWYTGFIIY AFILGFLVPL TIICLCYLFI IIKVKSSGIR
VGSSKRKKSE KKVTRMVSIV VAVFIFCWLP FYIFNVSSVS VAISPTPALK GMFDFVVVLT
YANSCANPIL YAFLSDNFKK SFQNVLCLVK VSGTDDGERS DSKQDKSRLN ETTETQRTLL
NGDLQTSI
