SSR2_CANLF
ID SSR2_CANLF Reviewed; 369 AA.
AC Q49LX6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Somatostatin receptor type 2;
DE Short=SS-2-R;
DE Short=SS2-R;
DE Short=SS2R;
GN Name=SSTR2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Liew C.W., Richter D., Kreienkamp H.-J.;
RT "Cloning of somatostatin receptors from Canis familiaris.";
RL Submitted (JUL-2004) 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 {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Located mainly at
CC the cell surface under basal conditions. Agonist stimulation results in
CC internalization to the 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; AY702068; AAW31434.1; -; Genomic_DNA.
DR RefSeq; NP_001026987.1; NM_001031817.1.
DR AlphaFoldDB; Q49LX6; -.
DR SMR; Q49LX6; -.
DR STRING; 9612.ENSCAFP00000006717; -.
DR PaxDb; Q49LX6; -.
DR GeneID; 403472; -.
DR KEGG; cfa:403472; -.
DR CTD; 6752; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q49LX6; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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:0004994; F:somatostatin receptor activity; IBA:GO_Central.
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:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
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 3: Inferred from homology;
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..369
FT /note="Somatostatin receptor type 2"
FT /id="PRO_0000289599"
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 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 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"
SQ SEQUENCE 369 AA; 41293 MW; 5A9393F272BE02A7 CRC64;
MDMEYELLNE SHTWVSPPFD LDGSVVAANS SNQTEPYYDL TSNAVLTFIY FVVCIIGLCG
NTLVIYVILR YAKMKTITNI YILNLAIAGE LFMLGLPFLA MQVALVHWPF GKAICRVVMT
VDGINQFTSI FCLTVMSIDR YLAVVHPIKS AKWRRPRTAK MVNVAVWGVS LLVVLPIMIY
AGLRSNQWGR SSCTINWPGE SGTWYTGFII YTFILGFLVP LTIICLCYLF IIIKVKSSGI
RVGSSKRKKS EKKVTRMVSI VVAVFIFCWL PFYIFNVSSV SVAISPTPAL KGMFDLVVVL
TYANSCANPI LYAFLSDNFK KSFQNVLCLV KVSGPDDGER SDSKQDKSRL NETTETQRTL
LNGDLQTSI
