SSR5_BOVIN
ID SSR5_BOVIN Reviewed; 368 AA.
AC F1MV99;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Somatostatin receptor type 5;
DE Short=SS-5-R;
DE Short=SS5-R;
DE Short=SS5R;
GN Name=SSTR5;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Receptor for somatostatin 28 and to a lesser extent for
CC somatostatin-14. The activity of this receptor is mediated by G
CC proteins which inhibit adenylyl cyclase. Increases cell growth
CC inhibition activity of SSTR2 following heterodimerization (By
CC similarity). {ECO:0000250}.
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 {ECO:0000250}; Multi-pass membrane
CC protein.
CC -!- PTM: Palmitoylated by ZDHHC5, but not ZDHHC3, nor ZDHHC8.
CC Palmitoylation creates an additional intracellular loop which is
CC thought to be important for efficient coupling to G-proteins and may
CC target the 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}.
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DR EMBL; DAAA02057287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005196928.1; XM_005196871.3.
DR RefSeq; XP_005224651.1; XM_005224594.3.
DR AlphaFoldDB; F1MV99; -.
DR SMR; F1MV99; -.
DR STRING; 9913.ENSBTAP00000047847; -.
DR PaxDb; F1MV99; -.
DR Ensembl; ENSBTAT00000052225; ENSBTAP00000047847; ENSBTAG00000039974.
DR VEuPathDB; HostDB:ENSBTAG00000039974; -.
DR VGNC; VGNC:35328; SSTR5.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160265; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; F1MV99; -.
DR OMA; ICYLLVC; -.
DR OrthoDB; 1011272at2759; -.
DR TreeFam; TF315737; -.
DR Reactome; R-BTA-375276; Peptide ligand-binding receptors.
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000039974; Expressed in prostate gland and 20 other tissues.
DR ExpressionAtlas; F1MV99; baseline.
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:0071385; P:cellular response to glucocorticoid stimulus; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0050796; P:regulation of insulin secretion; IBA:GO_Central.
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 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..368
FT /note="Somatostatin receptor type 5"
FT /id="PRO_0000418365"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 322
FT /note="S-palmitoyl cysteine; by ZDHHC5"
FT /evidence="ECO:0000250"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 113..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 368 AA; 39961 MW; 3F21C39B939F3BF8 CRC64;
MEPLFPASPL TTWNTSSVVP SGSGDENGTL AGLGPSPGAR AVVVPVLYLL VCAVGLGGNT
LVIYVVLRHA KMKTVTNIYI LNLAVADVLL MLGLPFVATQ NAISYWPFGP VLCRLVMTLD
GINQFTSIFC LTVMSVDRYL AVVHPIRSAR WRRPRVAKLA SAAVWAFSLV MSLPLVVFAD
IQEGWNTCNL SWPEPVGLWG AVFIIYTSVL GFFGPLLVIC LCYLLIVVKL KASGVRVGST
RRRSERKVTR MVVVVVLVFA GCWLPFFIVN IVNLAFALPE EPASAGAYFF VVVLSYANSC
ANPLLYGFLS DNFRQSFRKV LCLRKGYGAG AEDADATEPQ PGPSSRLQEA MMPVRSCKAN
GLMQTSKL
