SSR1_CANLF
ID SSR1_CANLF Reviewed; 391 AA.
AC Q49LX5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Somatostatin receptor type 1;
DE Short=SS-1-R;
DE Short=SS1-R;
DE Short=SS1R;
GN Name=SSTR1;
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 with higher affinity for
CC somatostatin-14 than -28. This receptor is coupled via pertussis toxin
CC sensitive G proteins to inhibition of adenylyl cyclase. In addition it
CC stimulates phosphotyrosine phosphatase and Na(+)/H(+) exchanger via
CC pertussis toxin insensitive G proteins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SKB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {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; AY702069; AAW31435.1; -; Genomic_DNA.
DR RefSeq; NP_001026986.1; NM_001031816.1.
DR AlphaFoldDB; Q49LX5; -.
DR SMR; Q49LX5; -.
DR STRING; 9612.ENSCAFP00000020273; -.
DR PaxDb; Q49LX5; -.
DR Ensembl; ENSCAFT00000021824; ENSCAFP00000020273; ENSCAFG00000013755.
DR Ensembl; ENSCAFT00040000280; ENSCAFP00040000215; ENSCAFG00040000183.
DR GeneID; 403455; -.
DR KEGG; cfa:403455; -.
DR CTD; 6751; -.
DR VGNC; VGNC:46843; SSTR1.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; Q49LX5; -.
DR OMA; PDNMESD; -.
DR OrthoDB; 1011272at2759; -.
DR TreeFam; TF315737; -.
DR Reactome; R-CFA-375276; Peptide ligand-binding receptors.
DR Reactome; R-CFA-418594; G alpha (i) signalling events.
DR Proteomes; UP000002254; Unplaced.
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:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; IEA:Ensembl.
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; IPR001116; Somatstn_rcpt_1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00246; SOMATOSTATNR.
DR PRINTS; PR00587; SOMATOSTTN1R.
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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..391
FT /note="Somatostatin receptor type 1"
FT /id="PRO_0000289598"
FT TOPO_DOM 1..55
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..83
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..119
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..152
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..295
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..302
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..326
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 338
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 129..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 391 AA; 42670 MW; 131F8E0152EE1725 CRC64;
MFPNGTASSP SSPSPSPGSC GEGGGSRGPG AGAADGMEEP GRNASQNGTL SEGQGSAILI
SFIYSVVCLV GLCGNSMVIY VILRYAKMKT ATNIYILNLA IADELLMLSV PFLVTSTLLR
HWPFGALLCR LVLSVDAVNM FTSIYCLTVL SVDRYVAVVH PIKAARYRRP TVAKVVNLGV
WVLSLLVILP IVVFSRTAAN SDGTVACNML MPEPAQRWLV GFVLYTFLMG FLLPVGAICL
CYVLIIAKMR MVALKAGWQQ RKRSERKITL MVMMVVMVFV ICWMPFYVVQ LVNVFAEQDD
ATVSQLSVIL GYANSCANPI LYGFLSDNFK RSFQRILCLS WMDNAAEEPV DYYATALKSR
AYSVEDFQPE NLESGGAVFR NGTCTSRITT L
