SSR5_RAT
ID SSR5_RAT Reviewed; 363 AA.
AC P30938;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Somatostatin receptor type 5;
DE Short=SS-5-R;
DE Short=SS5-R;
DE Short=SS5R;
GN Name=Sstr5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Pituitary;
RX PubMed=1362243;
RA O'Carroll A.-M., Lolait S.J., Konig M., Mahan L.C.;
RT "Molecular cloning and expression of a pituitary somatostatin receptor with
RT preferential affinity for somatostatin-28.";
RL Mol. Pharmacol. 42:939-946(1992).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Pituitary;
RX PubMed=7908405;
RA Panetta R., Greenwood M.T., Warszynska A., Demchyshyn L.L., Day R.,
RA Niznik H.B., Srikant C.B., Patel Y.C.;
RT "Molecular cloning, functional characterization, and chromosomal
RT localization of a human somatostatin receptor (somatostatin receptor type
RT 5) with preferential affinity for somatostatin-28.";
RL Mol. Pharmacol. 45:417-427(1994).
RN [3]
RP INTERACTION WITH ZDHHC5.
RX PubMed=21820437; DOI=10.1016/j.febslet.2011.07.028;
RA Kokkola T., Kruse C., Roy-Pogodzik E.M., Pekkinen J., Bauch C., Honck H.H.,
RA Hennemann H., Kreienkamp H.J.;
RT "Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5
RT palmitoyltransferase.";
RL FEBS Lett. 585:2665-2670(2011).
CC -!- FUNCTION: Receptor for somatostatin-28. The activity of this receptor
CC is mediated by G proteins which inhibit adenylyl cyclase. Increases
CC cell growth inhibition activity of SSTR2 following heterodimerization.
CC {ECO:0000269|PubMed:1362243, ECO:0000269|PubMed:7908405}.
CC -!- SUBUNIT: Heterodimer with SSTR2. Heterodimerization with SSTR2
CC increases cell growth inhibition activity of SSTR2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Prominent in the pituitary and small intestine. Low
CC levels in islets and spleen. Not detected in kidney, pancreas,
CC cerebellum, or cortex. {ECO:0000269|PubMed:1362243,
CC ECO:0000269|PubMed:7908405}.
CC -!- PTM: Palmitoylated at Cys-320 by ZDHHC5, but not ZDHHC8. Palmitoylation
CC creates an additional intracellular loop which is thought to be
CC important for efficient coupling to G-proteins and may target the
CC protein to lipid rafts (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; L04535; AAA17029.1; -; mRNA.
DR EMBL; U01152; AAC09011.1; -; mRNA.
DR EMBL; X74828; CAA52825.1; -; mRNA.
DR PIR; I57940; I57940.
DR AlphaFoldDB; P30938; -.
DR SMR; P30938; -.
DR IntAct; P30938; 1.
DR MINT; P30938; -.
DR STRING; 10116.ENSRNOP00000025451; -.
DR BindingDB; P30938; -.
DR ChEMBL; CHEMBL4318; -.
DR DrugCentral; P30938; -.
DR GuidetoPHARMACOLOGY; 359; -.
DR GlyGen; P30938; 3 sites.
DR PhosphoSitePlus; P30938; -.
DR PaxDb; P30938; -.
DR UCSC; RGD:3765; rat.
DR RGD; 3765; Sstr5.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P30938; -.
DR PhylomeDB; P30938; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P30938; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
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; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEP:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:RGD.
DR GO; GO:0050796; P:regulation of insulin secretion; ISO:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000586; Somatstn_rcpt.
DR InterPro; IPR001184; Somatstn_rcpt_5.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00246; SOMATOSTATNR.
DR PRINTS; PR00591; SOMATOSTTN5R.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..363
FT /note="Somatostatin receptor type 5"
FT /id="PRO_0000070132"
FT TOPO_DOM 1..35
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..196
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..221
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..273
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 331..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 320
FT /note="S-palmitoyl cysteine; by ZDHHC5"
FT /evidence="ECO:0000250"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 363 AA; 39971 MW; 4BD4512960613B4A CRC64;
MEPLSLASTP SWNASAASSG NHNWSLVGSA SPMGARAVLV PVLYLLVCTV GLSGNTLVIY
VVLRHAKMKT VTNVYILNLA VADVLFMLGL PFLATQNAVV SYWPFGSFLC RLVMTLDGIN
QFTSIFCLMV MSVDRYLAVV HPLRSARWRR PRVAKMASAA VWVFSLLMSL PLLVFADVQE
GWGTCNLSWP EPVGLWGAAF ITYTSVLGFF GPLLVICLCY LLIVVKVKAA GMRVGSSRRR
RSEPKVTRMV VVVVLVFVGC WLPFFIVNIV NLAFTLPEEP TSAGLYFFVV VLSYANSCAN
PLLYGFLSDN FRQSFRKVLC LRRGYGMEDA DAIEPRPDKS GRPQATLPTR SCEANGLMQT
SRI
