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P30936 (SSR3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Somatostatin receptor type 3

Short name=SS-3-R
Short name=SS3-R
Short name=SS3R
Alternative name(s):
SSR-28
Gene names
Name:Sstr3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. Ref.1 Ref.3

Subunit structure

Homodimer and heterodimer with SSTR2. Heterodimerization with SSTR2 inactivates SSTR3 receptor function. Ref.3

Subcellular location

Cell membrane; Multi-pass membrane protein. Note: Internalized into endoplasmic vesicles upon somatostatin-stimulation. Ref.2 Ref.3

Tissue specificity

Densely expressed in cerebellum and at moderate levels in the amygdala, cortex, striatum, spleen, liver and pituitary. Ref.1

Post-translational modification

Phosphorylated. Phosphorylation increases upon somatostatin binding. Ref.2

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Somatostatin receptor type 3
PRO_0000070126

Regions

Topological domain1 – 4545Extracellular Potential
Transmembrane46 – 7126Helical; Name=1; Potential
Topological domain72 – 8110Cytoplasmic Potential
Transmembrane82 – 10322Helical; Name=2; Potential
Topological domain104 – 11815Extracellular Potential
Transmembrane119 – 14022Helical; Name=3; Potential
Topological domain141 – 16222Cytoplasmic Potential
Transmembrane163 – 18220Helical; Name=4; Potential
Topological domain183 – 20624Extracellular Potential
Transmembrane207 – 23226Helical; Name=5; Potential
Topological domain233 – 26634Cytoplasmic Potential
Transmembrane267 – 28822Helical; Name=6; Potential
Topological domain289 – 30214Extracellular Potential
Transmembrane303 – 32523Helical; Name=7; Potential
Topological domain326 – 428103Cytoplasmic Potential
Compositional bias358 – 37316Poly-Glu

Amino acid modifications

Modified residue3411Phosphoserine Probable
Modified residue3461Phosphoserine Probable
Modified residue3511Phosphoserine Probable
Modified residue3571Phosphothreonine Ref.2
Glycosylation181N-linked (GlcNAc...) Potential
Glycosylation311N-linked (GlcNAc...) Potential
Disulfide bond117 ↔ 192 By similarity

Experimental info

Mutagenesis3411S → A: Impaired internalization after somatostatin binding. Ref.2
Mutagenesis3461S → A: Impaired internalization after somatostatin binding. Ref.2
Mutagenesis3511S → A: Impaired internalization after somatostatin binding. Ref.2
Mutagenesis3571T → A: Reduced basal and somatostatin-induced phosphorylation. Impaired internalization after somatostatin binding. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P30936 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: BE0AA948840A9E9D

FASTA42847,151
        10         20         30         40         50         60 
MAAVTYPSSV PTTLDPGNAS SAWPLDTSLG NASAGTSLAG LAVSGILISL VYLVVCVVGL 

        70         80         90        100        110        120 
LGNSLVIYVV LRHTSSPSVT SVYILNLALA DELFMLGLPF LAAQNALSYW PFGSLMCRLV 

       130        140        150        160        170        180 
MAVDGINQFT SIFCLTVMSV DRYLAVVHPT RSARWRTAPV ARMVSAAVWV ASAVVVLPVV 

       190        200        210        220        230        240 
VFSGVPRGMS TCHMQWPEPA AAWRTAFIIY TAALGFFGPL LVICLCYLLI VVKVRSTTRR 

       250        260        270        280        290        300 
VRAPSCQWVQ APACQRRRRS ERRVTRMVVA VVALFVLCWM PFYLLNIVNV VCPLPEEPAF 

       310        320        330        340        350        360 
FGLYFLVVAL PYANSCANPI LYGFLSYRFK QGFRRILLRP SRRVRSQEPG SGPPEKTEEE 

       370        380        390        400        410        420 
EDEEEEERRE EEERRMQRGQ EMNGRLSQIA QPGPSGQQQR PCTGTAKEQQ LLPQEATAGD 


KASTLSHL 

« Hide

References

[1]"Molecular cloning of a somatostatin-28 receptor and comparison of its expression pattern with that of a somatostatin-14 receptor in rat brain."
Meyerhof W., Wulfsen I., Schoenrock C., Fehr S., Richter D.
Proc. Natl. Acad. Sci. U.S.A. 89:10267-10271(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Strain: Wistar.
Tissue: Brain.
[2]"Phosphorylation of four amino acid residues in the carboxyl terminus of the rat somatostatin receptor subtype 3 is crucial for its desensitization and internalization."
Roth A., Kreienkamp H.-J., Meyerhof W., Richter D.
J. Biol. Chem. 272:23769-23774(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF SER-341; SER-346; SER-351 AND THR-357, PHOSPHORYLATION AT SER-341; SER-346; SER-351 AND THR-357.
[3]"Homo- and heterodimerization of somatostatin receptor subtypes. Inactivation of sst(3) receptor function by heterodimerization with sst(2A)."
Pfeiffer M., Koch T., Schroder H., Klutzny M., Kirscht S., Kreienkamp H.J., Hollt V., Schulz S.
J. Biol. Chem. 276:14027-14036(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63574 mRNA. Translation: CAA45130.1.
PIRS30508.
RefSeqNP_598206.1. NM_133522.1.
XP_006242028.1. XM_006241966.1.
UniGeneRn.10458.

3D structure databases

ProteinModelPortalP30936.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid251061. 1 interaction.
STRING10116.ENSRNOP00000009612.

Chemistry

BindingDBP30936.
ChEMBLCHEMBL2096977.
GuidetoPHARMACOLOGY357.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP30936.

Proteomic databases

PaxDbP30936.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000009612; ENSRNOP00000009612; ENSRNOG00000007332.
GeneID171044.
KEGGrno:171044.
UCSCRGD:620308. rat.

Organism-specific databases

CTD6753.
RGD620308. Sstr3.

Phylogenomic databases

eggNOGNOG274661.
GeneTreeENSGT00630000089736.
HOGENOMHOG000230485.
HOVERGENHBG106919.
InParanoidP30936.
KOK04219.
OMANASSAWP.
OrthoDBEOG7BKCVQ.
PhylomeDBP30936.
TreeFamTF315737.

Gene expression databases

GenevestigatorP30936.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000586. Somatstn_rcpt.
IPR001856. Somatstn_rcpt_3.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00246. SOMATOSTATNR.
PR00589. SOMATOSTTN3R.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio621561.
PROP30936.

Entry information

Entry nameSSR3_RAT
AccessionPrimary (citable) accession number: P30936
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries