SSR4_RAT
ID SSR4_RAT Reviewed; 384 AA.
AC P30937;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Somatostatin receptor type 4;
DE Short=SS-4-R;
DE Short=SS4-R;
DE Short=SS4R;
GN Name=Sstr4;
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 [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=1360663; DOI=10.1073/pnas.89.23.11151;
RA Bruno J.F., Xu Y., Song J., Berelowitz M.;
RT "Molecular cloning and functional expression of a brain-specific
RT somatostatin receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11151-11155(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RX PubMed=8175684; DOI=10.1016/s0021-9258(18)99936-9;
RA Bito H., Mori M., Sakanaka C., Takano T., Honda Z., Gotoh Y., Nishida E.,
RA Shimizu T.;
RT "Functional coupling of SSTR4, a major hippocampal somatostatin receptor,
RT to adenylate cyclase inhibition, arachidonate release and activation of the
RT mitogen-activated protein kinase cascade.";
RL J. Biol. Chem. 269:12722-12730(1994).
CC -!- FUNCTION: Receptor for somatostatin-14. The activity of this receptor
CC is mediated by G proteins which inhibits adenylyl cyclase. It is
CC functionally coupled not only to inhibition of adenylate cyclase, but
CC also to activation of both arachidonate release and mitogen-activated
CC protein (MAP) kinase cascade.
CC -!- INTERACTION:
CC P30937; P31016: Dlg4; NbExp=3; IntAct=EBI-7665959, EBI-375655;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Brain, lung, heart and islets. Moderate levels in
CC the hippocampus, cortex and olfactory bulb.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M96544; AAA42180.1; -; Genomic_DNA.
DR EMBL; U04738; AAA17519.1; -; mRNA.
DR PIR; A47249; A47249.
DR RefSeq; NP_037168.1; NM_013036.2.
DR AlphaFoldDB; P30937; -.
DR SMR; P30937; -.
DR BioGRID; 247586; 1.
DR IntAct; P30937; 1.
DR MINT; P30937; -.
DR STRING; 10116.ENSRNOP00000066231; -.
DR BindingDB; P30937; -.
DR ChEMBL; CHEMBL2096977; -.
DR DrugCentral; P30937; -.
DR GuidetoPHARMACOLOGY; 358; -.
DR GlyGen; P30937; 1 site.
DR PhosphoSitePlus; P30937; -.
DR PaxDb; P30937; -.
DR Ensembl; ENSRNOT00000006181; ENSRNOP00000066231; ENSRNOG00000004641.
DR GeneID; 25555; -.
DR KEGG; rno:25555; -.
DR UCSC; RGD:3764; rat.
DR CTD; 6754; -.
DR RGD; 3764; Sstr4.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000156819; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; P30937; -.
DR OMA; WPHPAWS; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; P30937; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P30937; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000004641; Expressed in lung and 5 other tissues.
DR Genevisible; P30937; RN.
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:0016477; P:cell migration; IDA:RGD.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEP:RGD.
DR GO; GO:0030900; P:forebrain development; IEP:RGD.
DR GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0090238; P:positive regulation of arachidonic acid secretion; IDA:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000586; Somatstn_rcpt.
DR InterPro; IPR001512; Somatstn_rcpt_4.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00246; SOMATOSTATNR.
DR PRINTS; PR00590; SOMATOSTTN4R.
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..384
FT /note="Somatostatin receptor type 4"
FT /id="PRO_0000070129"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..105
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..280
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..311
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 323
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 384 AA; 42088 MW; 044542B4922411E5 CRC64;
MNTPATLPLG GEDTTWTPGI NASWAPDEEE DAVRSDGTGT AGMVTIQCIY ALVCLVGLVG
NALVIFVILR YAKMKTATNI YLLNLAVADE LFMLSVPFVA SAAALRHWPF GAVLCRAVLS
VDGLNMFTSV FCLTVLSVDR YVAVVHPLRA ATYRRPSVAK LINLGVWLAS LLVTLPIAVF
ADTRPARGGE AVACNLHWPH PAWSAVFVIY TFLLGFLLPV LAIGLCYLLI VGKMRAVALR
AGWQQRRRSE KKITRLVLMV VTVFVLCWMP FYVVQLLNLF VTSLDATVNH VSLILSYANS
CANPILYGFL SDNFRRSFQR VLCLRCCLLE TTGGAEEEPL DYYATALKSR GGPGCICPPL
PCQQEPMQAE PACKRVPFTK TTTF
