ID   SSR5_HUMAN              Reviewed;         364 AA.
AC   P35346; P34988; Q541E0; Q9UJI5;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 3.
DT   17-JUN-2020, entry version 183.
DE   RecName: Full=Somatostatin receptor type 5;
DE            Short=SS-5-R;
DE            Short=SS5-R;
DE            Short=SS5R;
GN   Name=SSTR5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=8373420; DOI=10.1006/bbrc.1993.2122;
RA   Yamada Y., Kagimoto S., Kubota A., Yasuda K., Masuda K., Someya Y.,
RA   Ihara Y., Li Q., Imura H., Seino S., Seino Y.;
RT   "Cloning, functional expression and pharmacological characterization of a
RT   fourth (hSSTR4) and a fifth (hSSTR5) human somatostatin receptor subtype.";
RL   Biochem. Biophys. Res. Commun. 195:844-852(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=8078491;
RA   O'Carroll A.-M., Raynor K., Lolait S.J., Reisine T.;
RT   "Characterization of cloned human somatostatin receptor SSTR5.";
RL   Mol. Pharmacol. 46:291-298(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12072395; DOI=10.1210/endo.143.7.8883;
RA   Petersenn S., Rasch A.C., Bohnke C., Schulte H.M.;
RT   "Identification of an upstream pituitary-active promoter of human
RT   somatostatin receptor subtype 5.";
RL   Endocrinology 143:2626-2634(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-335.
RX   PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA   Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA   Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT   "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT   the short arm of human chromosome 16.";
RL   Hum. Mol. Genet. 10:339-352(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-335.
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   SUBUNIT.
RX   PubMed=18653781; DOI=10.1210/me.2007-0334;
RA   Grant M., Alturaihi H., Jaquet P., Collier B., Kumar U.;
RT   "Cell growth inhibition and functioning of human somatostatin receptor type
RT   2 are modulated by receptor heterodimerization.";
RL   Mol. Endocrinol. 22:2278-2292(2008).
RN   [9]
RP   PALMITOYLATION BY 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 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.
CC       {ECO:0000269|PubMed:12072395, ECO:0000269|PubMed:7908405,
CC       ECO:0000269|PubMed:8078491, ECO:0000269|PubMed:8373420}.
CC   -!- SUBUNIT: Heterodimer with SSTR2. Heterodimerization with SSTR2
CC       increases cell growth inhibition activity of SSTR2.
CC       {ECO:0000269|PubMed:18653781}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Adult pituitary gland, heart, small intestine,
CC       adrenal gland, cerebellum and fetal hypothalamus. No expression in
CC       fetal or adult kidney, liver, pancreas, uterus, spleen, lung, thyroid
CC       or ovary. {ECO:0000269|PubMed:12072395, ECO:0000269|PubMed:7908405,
CC       ECO:0000269|PubMed:8078491}.
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. {ECO:0000269|PubMed:21820437}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; L14865; AAA20828.1; -; Genomic_DNA.
DR   EMBL; D16827; BAA04107.1; -; Genomic_DNA.
DR   EMBL; AY081193; AAL88744.1; -; Genomic_DNA.
DR   EMBL; AE006466; AAK61266.1; -; Genomic_DNA.
DR   EMBL; AL031713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471112; EAW85687.1; -; Genomic_DNA.
DR   CCDS; CCDS10429.1; -.
DR   PIR; I57955; I57955.
DR   PIR; JN0763; JN0763.
DR   RefSeq; NP_001044.1; NM_001053.3.
DR   RefSeq; NP_001166031.1; NM_001172560.1.
DR   BioGRID; 112633; 10.
DR   CORUM; P35346; -.
DR   STRING; 9606.ENSP00000293897; -.
DR   BindingDB; P35346; -.
DR   ChEMBL; CHEMBL1792; -.
DR   DrugBank; DB15494; Edotreotide gallium Ga-68.
DR   DrugBank; DB06791; Lanreotide.
DR   DrugBank; DB13985; Lutetium Lu 177 dotatate.
DR   DrugBank; DB00104; Octreotide.
DR   DrugBank; DB06663; Pasireotide.
DR   DrugBank; DB09099; Somatostatin.
DR   DrugBank; DB04894; Vapreotide.
DR   DrugCentral; P35346; -.
DR   GuidetoPHARMACOLOGY; 359; -.
DR   iPTMnet; P35346; -.
DR   PhosphoSitePlus; P35346; -.
DR   BioMuta; SSTR5; -.
DR   DMDM; 12644225; -.
DR   jPOST; P35346; -.
DR   PaxDb; P35346; -.
DR   PeptideAtlas; P35346; -.
DR   PRIDE; P35346; -.
DR   ProteomicsDB; 55025; -.
DR   Antibodypedia; 3358; 304 antibodies.
DR   DNASU; 6755; -.
DR   Ensembl; ENST00000293897; ENSP00000293897; ENSG00000162009.
DR   GeneID; 6755; -.
DR   KEGG; hsa:6755; -.
DR   UCSC; uc002ckq.4; human.
DR   CTD; 6755; -.
DR   DisGeNET; 6755; -.
DR   EuPathDB; HostDB:ENSG00000162009.8; -.
DR   GeneCards; SSTR5; -.
DR   HGNC; HGNC:11334; SSTR5.
DR   HPA; ENSG00000162009; Tissue enhanced (gallbladder, lymphoid tissue, pituitary gland).
DR   MIM; 182455; gene.
DR   neXtProt; NX_P35346; -.
DR   OpenTargets; ENSG00000162009; -.
DR   PharmGKB; PA36158; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   eggNOG; ENOG410XRW9; LUCA.
DR   GeneTree; ENSGT00940000160265; -.
DR   HOGENOM; CLU_009579_8_1_1; -.
DR   InParanoid; P35346; -.
DR   KO; K04221; -.
DR   OMA; AGLYFFV; -.
DR   OrthoDB; 1011272at2759; -.
DR   PhylomeDB; P35346; -.
DR   TreeFam; TF315737; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SIGNOR; P35346; -.
DR   BioGRID-ORCS; 6755; 2 hits in 787 CRISPR screens.
DR   ChiTaRS; SSTR5; human.
DR   GeneWiki; Somatostatin_receptor_5; -.
DR   GenomeRNAi; 6755; -.
DR   Pharos; P35346; Tclin.
DR   PRO; PR:P35346; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P35346; protein.
DR   Bgee; ENSG00000162009; Expressed in right atrium auricular region and 62 other tissues.
DR   Genevisible; P35346; HS.
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:HPA.
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:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
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   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..364
FT                   /note="Somatostatin receptor type 5"
FT                   /id="PRO_0000070130"
FT   TOPO_DOM        1..38
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..66
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        67..76
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..101
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..113
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..135
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..197
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..222
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..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..364
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         325
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
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        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        112..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         37
FT                   /note="G -> R (in dbSNP:rs4988482)"
FT                   /id="VAR_029222"
FT   VARIANT         48
FT                   /note="L -> M (in dbSNP:rs4988483)"
FT                   /id="VAR_029223"
FT   VARIANT         52
FT                   /note="A -> V (in dbSNP:rs4988484)"
FT                   /id="VAR_029224"
FT   VARIANT         105
FT                   /note="W -> R (in dbSNP:rs34803074)"
FT                   /id="VAR_033484"
FT   VARIANT         109
FT                   /note="P -> S (in dbSNP:rs4988487)"
FT                   /id="VAR_029225"
FT   VARIANT         234
FT                   /note="R -> C (in dbSNP:rs34070276)"
FT                   /id="VAR_049442"
FT   VARIANT         251
FT                   /note="L -> S (in dbSNP:rs34474910)"
FT                   /id="VAR_033485"
FT   VARIANT         267
FT                   /note="V -> I (in dbSNP:rs35125411)"
FT                   /id="VAR_049443"
FT   VARIANT         333
FT                   /note="T -> M (in dbSNP:rs12596873)"
FT                   /id="VAR_029226"
FT   VARIANT         335
FT                   /note="P -> L (in dbSNP:rs169068)"
FT                   /evidence="ECO:0000269|PubMed:11157797,
FT                   ECO:0000269|PubMed:15616553"
FT                   /id="VAR_020073"
FT   VARIANT         339
FT                   /note="R -> K (in dbSNP:rs35072648)"
FT                   /id="VAR_033486"
FT   VARIANT         357
FT                   /note="G -> R (in dbSNP:rs34947461)"
FT                   /id="VAR_049444"
FT   CONFLICT        348..352
FT                   /note="PPAHR -> RPRT (in Ref. 1; AAA20828)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   364 AA;  39202 MW;  905744715F31121C CRC64;
     MEPLFPASTP SWNASSPGAA SGGGDNRTLV GPAPSAGARA VLVPVLYLLV CAAGLGGNTL
     VIYVVLRFAK MKTVTNIYIL NLAVADVLYM LGLPFLATQN AASFWPFGPV LCRLVMTLDG
     VNQFTSVFCL TVMSVDRYLA VVHPLSSARW RRPRVAKLAS AAAWVLSLCM SLPLLVFADV
     QEGGTCNASW PEPVGLWGAV FIIYTAVLGF FAPLLVICLC YLLIVVKVRA AGVRVGCVRR
     RSERKVTRMV LVVVLVFAGC WLPFFTVNIV NLAVALPQEP ASAGLYFFVV ILSYANSCAN
     PVLYGFLSDN FRQSFQKVLC LRKGSGAKDA DATEPRPDRI RQQQEATPPA HRAAANGLMQ
     TSKL
//