SSR5_HUMAN
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 03-AUG-2022, entry version 192.
DE RecName: Full=Somatostatin receptor type 5;
DE Short=SS-5-R;
DE Short=SS5-R;
DE Short=SS5R;
DE Short=SST5;
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 -!- INTERACTION:
CC P35346; P30872: SSTR1; NbExp=3; IntAct=EBI-27053622, EBI-21273948;
CC P35346; P30874: SSTR2; NbExp=4; IntAct=EBI-27053622, EBI-6266898;
CC P35346; P31391: SSTR4; NbExp=3; IntAct=EBI-27053622, EBI-21274002;
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 AlphaFoldDB; P35346; -.
DR SMR; P35346; -.
DR BioGRID; 112633; 15.
DR CORUM; P35346; -.
DR IntAct; P35346; 4.
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; DB06663; Pasireotide.
DR DrugBank; DB09099; Somatostatin.
DR DrugBank; DB04894; Vapreotide.
DR DrugCentral; P35346; -.
DR GuidetoPHARMACOLOGY; 359; -.
DR GlyGen; P35346; 3 sites.
DR iPTMnet; P35346; -.
DR PhosphoSitePlus; P35346; -.
DR BioMuta; SSTR5; -.
DR DMDM; 12644225; -.
DR jPOST; P35346; -.
DR MassIVE; P35346; -.
DR PaxDb; P35346; -.
DR PeptideAtlas; P35346; -.
DR PRIDE; P35346; -.
DR ProteomicsDB; 55025; -.
DR Antibodypedia; 3358; 320 antibodies from 36 providers.
DR DNASU; 6755; -.
DR Ensembl; ENST00000293897.6; ENSP00000293897.4; ENSG00000162009.9.
DR Ensembl; ENST00000689027.1; ENSP00000508487.1; ENSG00000162009.9.
DR GeneID; 6755; -.
DR KEGG; hsa:6755; -.
DR MANE-Select; ENST00000689027.1; ENSP00000508487.1; NM_001172560.3; NP_001166031.1.
DR UCSC; uc002ckq.4; human.
DR CTD; 6755; -.
DR DisGeNET; 6755; -.
DR GeneCards; SSTR5; -.
DR HGNC; HGNC:11334; SSTR5.
DR HPA; ENSG00000162009; Group enriched (adrenal gland, heart muscle, pituitary gland).
DR MIM; 182455; gene.
DR neXtProt; NX_P35346; -.
DR OpenTargets; ENSG00000162009; -.
DR PharmGKB; PA36158; -.
DR VEuPathDB; HostDB:ENSG00000162009; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160265; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; P35346; -.
DR OMA; ICYLLVC; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; P35346; -.
DR TreeFam; TF315737; -.
DR PathwayCommons; P35346; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P35346; -.
DR SIGNOR; P35346; -.
DR BioGRID-ORCS; 6755; 13 hits in 1076 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 56 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:ProtInc.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
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; 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 REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
