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Protein

Somatostatin receptor type 5

Gene

SSTR5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for somatostatin 28 and to a lesser extent for somatostatin-14. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Increases cell growth inhibition activity of SSTR2 following heterodimerization.4 Publications

GO - Molecular functioni

  1. neuropeptide binding Source: GO_Central
  2. somatostatin receptor activity Source: ProtInc

GO - Biological processi

  1. cellular response to estradiol stimulus Source: GO_Central
  2. cellular response to glucocorticoid stimulus Source: GO_Central
  3. glucose homeostasis Source: Ensembl
  4. G-protein coupled receptor signaling pathway Source: ProtInc
  5. G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: ProtInc
  6. negative regulation of cell proliferation Source: ProtInc
  7. neuropeptide signaling pathway Source: GO_Central
  8. positive regulation of cytokinesis Source: UniProtKB
  9. regulation of insulin secretion Source: GO_Central
  10. somatostatin signaling pathway Source: GOC
  11. synaptic transmission Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_14819. Peptide ligand-binding receptors.
REACT_19231. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Somatostatin receptor type 5
Short name:
SS-5-R
Short name:
SS5-R
Short name:
SS5R
Gene namesi
Name:SSTR5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:11334. SSTR5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3838ExtracellularSequence AnalysisAdd
BLAST
Transmembranei39 – 6628Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini67 – 7610CytoplasmicSequence Analysis
Transmembranei77 – 10125Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini102 – 11312ExtracellularSequence AnalysisAdd
BLAST
Transmembranei114 – 13522Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini136 – 15722CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei158 – 17821Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini179 – 19719ExtracellularSequence AnalysisAdd
BLAST
Transmembranei198 – 22225Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini223 – 24725CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei248 – 27326Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini274 – 28310ExtracellularSequence Analysis
Transmembranei284 – 30825Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini309 – 36456CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of plasma membrane Source: ProtInc
  2. neuron projection Source: GO_Central
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36158.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 364364Somatostatin receptor type 5PRO_0000070130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi13 – 131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi26 – 261N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi112 ↔ 186PROSITE-ProRule annotation
Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
Lipidationi320 – 3201S-palmitoyl cysteine; by ZDHHC5By similarity
Modified residuei325 – 3251Phosphoserine; by PKASequence Analysis

Post-translational modificationi

Palmitoylated by ZDHHC5, but not ZDHHC3, nor ZDHHC8. Palmitoylation creates an additional intracellular loop which is thought to be important for efficient coupling to G-proteins and may target the protein to lipid rafts.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP35346.
PRIDEiP35346.

PTM databases

PhosphoSiteiP35346.

Expressioni

Tissue specificityi

Adult pituitary gland, heart, small intestine, adrenal gland, cerebellum and fetal hypothalamus. No expression in fetal or adult kidney, liver, pancreas, uterus, spleen, lung, thyroid or ovary.3 Publications

Gene expression databases

BgeeiP35346.
CleanExiHS_SSTR5.
GenevestigatoriP35346.

Interactioni

Subunit structurei

Heterodimer with SSTR2. Heterodimerization with SSTR2 increases cell growth inhibition activity of SSTR2.1 Publication

Protein-protein interaction databases

BioGridi112633. 3 interactions.
STRINGi9606.ENSP00000293897.

Structurei

3D structure databases

ProteinModelPortaliP35346.
SMRiP35346. Positions 46-317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG274661.
GeneTreeiENSGT00760000118797.
HOGENOMiHOG000230485.
HOVERGENiHBG106919.
InParanoidiP35346.
KOiK04221.
OMAiNAVSYWP.
PhylomeDBiP35346.
TreeFamiTF315737.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000586. Somatstn_rcpt.
IPR001184. Somatstn_rcpt_5.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00246. SOMATOSTATNR.
PR00591. SOMATOSTTN5R.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35346-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEPLFPASTP SWNASSPGAA SGGGDNRTLV GPAPSAGARA VLVPVLYLLV
60 70 80 90 100
CAAGLGGNTL VIYVVLRFAK MKTVTNIYIL NLAVADVLYM LGLPFLATQN
110 120 130 140 150
AASFWPFGPV LCRLVMTLDG VNQFTSVFCL TVMSVDRYLA VVHPLSSARW
160 170 180 190 200
RRPRVAKLAS AAAWVLSLCM SLPLLVFADV QEGGTCNASW PEPVGLWGAV
210 220 230 240 250
FIIYTAVLGF FAPLLVICLC YLLIVVKVRA AGVRVGCVRR RSERKVTRMV
260 270 280 290 300
LVVVLVFAGC WLPFFTVNIV NLAVALPQEP ASAGLYFFVV ILSYANSCAN
310 320 330 340 350
PVLYGFLSDN FRQSFQKVLC LRKGSGAKDA DATEPRPDRI RQQQEATPPA
360
HRAAANGLMQ TSKL
Length:364
Mass (Da):39,202
Last modified:December 1, 2000 - v3
Checksum:i905744715F31121C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti348 – 3525PPAHR → RPRT in AAA20828. (PubMed:7908405)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371G → R.
Corresponds to variant rs4988482 [ dbSNP | Ensembl ].
VAR_029222
Natural varianti48 – 481L → M.
Corresponds to variant rs4988483 [ dbSNP | Ensembl ].
VAR_029223
Natural varianti52 – 521A → V.
Corresponds to variant rs4988484 [ dbSNP | Ensembl ].
VAR_029224
Natural varianti105 – 1051W → R.
Corresponds to variant rs34803074 [ dbSNP | Ensembl ].
VAR_033484
Natural varianti109 – 1091P → S.
Corresponds to variant rs4988487 [ dbSNP | Ensembl ].
VAR_029225
Natural varianti234 – 2341R → C.
Corresponds to variant rs34070276 [ dbSNP | Ensembl ].
VAR_049442
Natural varianti251 – 2511L → S.
Corresponds to variant rs34474910 [ dbSNP | Ensembl ].
VAR_033485
Natural varianti267 – 2671V → I.
Corresponds to variant rs35125411 [ dbSNP | Ensembl ].
VAR_049443
Natural varianti333 – 3331T → M.
Corresponds to variant rs12596873 [ dbSNP | Ensembl ].
VAR_029226
Natural varianti335 – 3351P → L.2 Publications
Corresponds to variant rs169068 [ dbSNP | Ensembl ].
VAR_020073
Natural varianti339 – 3391R → K.
Corresponds to variant rs35072648 [ dbSNP | Ensembl ].
VAR_033486
Natural varianti357 – 3571G → R.
Corresponds to variant rs34947461 [ dbSNP | Ensembl ].
VAR_049444

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14865 Genomic DNA. Translation: AAA20828.1.
D16827 Genomic DNA. Translation: BAA04107.1.
AY081193 Genomic DNA. Translation: AAL88744.1.
AE006466 Genomic DNA. Translation: AAK61266.1.
AL031713 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85687.1.
CCDSiCCDS10429.1.
PIRiI57955.
JN0763.
RefSeqiNP_001044.1. NM_001053.3.
NP_001166031.1. NM_001172560.1.
XP_006720999.1. XM_006720936.1.
UniGeneiHs.449840.

Genome annotation databases

EnsembliENST00000293897; ENSP00000293897; ENSG00000162009.
GeneIDi6755.
KEGGihsa:6755.
UCSCiuc002ckq.3. human.

Polymorphism databases

DMDMi12644225.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14865 Genomic DNA. Translation: AAA20828.1.
D16827 Genomic DNA. Translation: BAA04107.1.
AY081193 Genomic DNA. Translation: AAL88744.1.
AE006466 Genomic DNA. Translation: AAK61266.1.
AL031713 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85687.1.
CCDSiCCDS10429.1.
PIRiI57955.
JN0763.
RefSeqiNP_001044.1. NM_001053.3.
NP_001166031.1. NM_001172560.1.
XP_006720999.1. XM_006720936.1.
UniGeneiHs.449840.

3D structure databases

ProteinModelPortaliP35346.
SMRiP35346. Positions 46-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112633. 3 interactions.
STRINGi9606.ENSP00000293897.

Chemistry

BindingDBiP35346.
ChEMBLiCHEMBL2111436.
DrugBankiDB00104. Octreotide.
DB06663. Pasireotide.
DB04894. Vapreotide.
GuidetoPHARMACOLOGYi359.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP35346.

Polymorphism databases

DMDMi12644225.

Proteomic databases

PaxDbiP35346.
PRIDEiP35346.

Protocols and materials databases

DNASUi6755.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000293897; ENSP00000293897; ENSG00000162009.
GeneIDi6755.
KEGGihsa:6755.
UCSCiuc002ckq.3. human.

Organism-specific databases

CTDi6755.
GeneCardsiGC16P001122.
HGNCiHGNC:11334. SSTR5.
MIMi182455. gene.
neXtProtiNX_P35346.
PharmGKBiPA36158.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG274661.
GeneTreeiENSGT00760000118797.
HOGENOMiHOG000230485.
HOVERGENiHBG106919.
InParanoidiP35346.
KOiK04221.
OMAiNAVSYWP.
PhylomeDBiP35346.
TreeFamiTF315737.

Enzyme and pathway databases

ReactomeiREACT_14819. Peptide ligand-binding receptors.
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

GeneWikiiSomatostatin_receptor_5.
GenomeRNAii6755.
NextBioi26352.
PROiP35346.
SOURCEiSearch...

Gene expression databases

BgeeiP35346.
CleanExiHS_SSTR5.
GenevestigatoriP35346.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000586. Somatstn_rcpt.
IPR001184. Somatstn_rcpt_5.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00246. SOMATOSTATNR.
PR00591. SOMATOSTTN5R.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, functional characterization, and chromosomal localization of a human somatostatin receptor (somatostatin receptor type 5) with preferential affinity for somatostatin-28."
    Panetta R., Greenwood M.T., Warszynska A., Demchyshyn L.L., Day R., Niznik H.B., Srikant C.B., Patel Y.C.
    Mol. Pharmacol. 45:417-427(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
  2. "Cloning, functional expression and pharmacological characterization of a fourth (hSSTR4) and a fifth (hSSTR5) human somatostatin receptor subtype."
    Yamada Y., Kagimoto S., Kubota A., Yasuda K., Masuda K., Someya Y., Ihara Y., Li Q., Imura H., Seino S., Seino Y.
    Biochem. Biophys. Res. Commun. 195:844-852(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  3. "Characterization of cloned human somatostatin receptor SSTR5."
    O'Carroll A.-M., Raynor K., Lolait S.J., Reisine T.
    Mol. Pharmacol. 46:291-298(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
  4. "Identification of an upstream pituitary-active promoter of human somatostatin receptor subtype 5."
    Petersenn S., Rasch A.C., Bohnke C., Schulte H.M.
    Endocrinology 143:2626-2634(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
  5. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
    Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
    Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-335.
  6. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-335.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "Cell growth inhibition and functioning of human somatostatin receptor type 2 are modulated by receptor heterodimerization."
    Grant M., Alturaihi H., Jaquet P., Collier B., Kumar U.
    Mol. Endocrinol. 22:2278-2292(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  9. "Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5 palmitoyltransferase."
    Kokkola T., Kruse C., Roy-Pogodzik E.M., Pekkinen J., Bauch C., Honck H.H., Hennemann H., Kreienkamp H.J.
    FEBS Lett. 585:2665-2670(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION BY ZDHHC5.

Entry informationi

Entry nameiSSR5_HUMAN
AccessioniPrimary (citable) accession number: P35346
Secondary accession number(s): P34988, Q541E0, Q9UJI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 1, 2000
Last modified: February 4, 2015
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.