SSR5_MOUSE
ID SSR5_MOUSE Reviewed; 362 AA.
AC O08858; A6H6N8; O08998; Q3UZM7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Somatostatin receptor type 5;
DE Short=SS-5-R;
DE Short=SS5-R;
DE Short=SS5R;
GN Name=Sstr5; Synonyms=Smstr5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=9300821; DOI=10.1016/s0378-1119(97)00156-x;
RA Lublin A.L., Diehl N.L., Hochgeschwender U.;
RT "Isolation and characterization of the gene encoding the type 5 mouse (Mus
RT musculus) somatostatin receptor (msst5).";
RL Gene 195:63-66(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Moldovan S., DeMayo F., Brunicardi F.C.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Gordon D.F., Woodmansee W.W., Wood W.M., Knauf H., James R.A.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Baumeister H., Roosterman D., Schafer J., Kreuzer O., Meyerhof W.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP TOPOLOGY, SUBCELLULAR LOCATION, AND PALMITOYLATION AT CYS-319.
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 -!- 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:0000269|PubMed:21820437};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21820437}.
CC -!- TISSUE SPECIFICITY: Expressed in adult brain but not in liver, heart,
CC spleen, or kidney. {ECO:0000269|PubMed:9300821}.
CC -!- PTM: Palmitoylated at Cys-319 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. {ECO:0000269|PubMed:21820437}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB88302.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U82697; AAC53353.1; -; Genomic_DNA.
DR EMBL; AF004740; AAB61418.1; -; Genomic_DNA.
DR EMBL; AF030441; AAB86492.1; -; Genomic_DNA.
DR EMBL; AF035777; AAB88302.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK133609; BAE21747.1; -; mRNA.
DR EMBL; AK133767; BAE21829.1; -; mRNA.
DR EMBL; AC131323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC145943; AAI45944.1; -; mRNA.
DR EMBL; BC150805; AAI50806.1; -; mRNA.
DR CCDS; CCDS28520.1; -.
DR RefSeq; NP_001177937.1; NM_001191008.1.
DR RefSeq; NP_035555.1; NM_011425.3.
DR AlphaFoldDB; O08858; -.
DR SMR; O08858; -.
DR IntAct; O08858; 1.
DR MINT; O08858; -.
DR STRING; 10090.ENSMUSP00000051085; -.
DR BindingDB; O08858; -.
DR ChEMBL; CHEMBL2733; -.
DR DrugCentral; O08858; -.
DR GuidetoPHARMACOLOGY; 359; -.
DR GlyGen; O08858; 3 sites.
DR PhosphoSitePlus; O08858; -.
DR SwissPalm; O08858; -.
DR PaxDb; O08858; -.
DR PRIDE; O08858; -.
DR Antibodypedia; 3358; 320 antibodies from 36 providers.
DR DNASU; 20609; -.
DR Ensembl; ENSMUST00000051864; ENSMUSP00000051085; ENSMUSG00000050824.
DR Ensembl; ENSMUST00000165183; ENSMUSP00000128787; ENSMUSG00000050824.
DR GeneID; 20609; -.
DR KEGG; mmu:20609; -.
DR UCSC; uc008bax.2; mouse.
DR CTD; 6755; -.
DR MGI; MGI:894282; Sstr5.
DR VEuPathDB; HostDB:ENSMUSG00000050824; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160265; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; O08858; -.
DR OMA; ICYLLVC; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; O08858; -.
DR TreeFam; TF315737; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 20609; 1 hit in 74 CRISPR screens.
DR PRO; PR:O08858; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O08858; protein.
DR Bgee; ENSMUSG00000050824; Expressed in choroid plexus of fourth ventricle and 12 other tissues.
DR Genevisible; O08858; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:MGI.
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; ISO:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:MGI.
DR GO; GO:0050796; P:regulation of insulin secretion; IMP:MGI.
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..362
FT /note="Somatostatin receptor type 5"
FT /id="PRO_0000070131"
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..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..220
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..272
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 319
FT /note="S-palmitoyl cysteine; by ZDHHC5"
FT /evidence="ECO:0000269|PubMed:21820437"
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 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 7
FT /note="T -> A (in Ref. 1; AAC53353, 2; AAB61418, 3;
FT AAB86492, 4; AAB88302 and 7; AAI45944/AAI50806)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="S -> G (in Ref. 1; AAC53353, 2; AAB61418, 3;
FT AAB86492, 4; AAB88302 and 7; AAI45944/AAI50806)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="V -> VV (in Ref. 1; AAC53353)"
FT /evidence="ECO:0000305"
FT CONFLICT 303..305
FT /note="YGF -> LWL (in Ref. 2; AAB61418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 40008 MW; C069149B8A8141C4 CRC64;
MEPLSLTSTP SWNASAASSS SHNWSLVDPV SPMGARAVLV PVLYLLVCTV GLGGNTLVIY
VVLRYAKMKT VTNVYILNLA VADVLFMLGL PFLATQNAVS YWPFGSFLCR LVMTLDGINQ
FTSIFCLMVM SVDRYLAVVH PLRSARWRRP RVAKLASAAV WVFSLLMSLP LLVFADVQEG
WGTCNLSWPE PVGLWGAAFI TYTSVLGFFG PLLVICLCYL LIVVKVKAAG MRVGSSRRRR
SERKVTRMVV VVVLVFVGCW LPFFIVNIVN LAFTLPEEPT SAGLYFFVVV LSYANSCANP
LLYGFLSDNF RQSFRKALCL RRGYGVEDAD AIEPRPDKSG RPQTTLPTRS CEANGLMQTS
RL
