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Protein

Somatostatin receptor type 5

Gene

Sstr5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for somatostatin-28. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Increases cell growth inhibition activity of SSTR2 following heterodimerization.2 Publications

GO - Molecular functioni

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

GO - Biological processi

  1. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: RGD
  2. cellular response to estradiol stimulus Source: GO_Central
  3. cellular response to glucocorticoid stimulus Source: RGD
  4. negative regulation of cell proliferation Source: GO_Central
  5. neuropeptide signaling pathway Source: GO_Central
  6. regulation of insulin secretion Source: GO_Central
  7. somatostatin signaling pathway Source: GOC
  8. synaptic transmission Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3765. Sstr5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3535ExtracellularSequence AnalysisAdd
BLAST
Transmembranei36 – 6328Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini64 – 7310CytoplasmicSequence Analysis
Transmembranei74 – 9926Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini100 – 11112ExtracellularSequence AnalysisAdd
BLAST
Transmembranei112 – 13322Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini134 – 15522CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei156 – 17621Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini177 – 19620ExtracellularSequence AnalysisAdd
BLAST
Transmembranei197 – 22125Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini222 – 24726CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei248 – 27326Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini274 – 28310ExtracellularSequence Analysis
Transmembranei284 – 30825Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini309 – 36355CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. integral component of plasma membrane Source: GO_Central
  3. neuron projection Source: GO_Central
  4. plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363Somatostatin receptor type 5PRO_0000070132Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi13 – 131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi23 – 231N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi110 ↔ 185PROSITE-ProRule annotation
Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
Lipidationi320 – 3201S-palmitoyl cysteine; by ZDHHC5By similarity

Post-translational modificationi

Palmitoylated at Cys-320 by ZDHHC5, but not 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 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PRIDEiP30938.

PTM databases

PhosphoSiteiP30938.

Expressioni

Tissue specificityi

Prominent in the pituitary and small intestine. Low levels in islets and spleen. Not detected in kidney, pancreas, cerebellum, or cortex.2 Publications

Gene expression databases

GenevestigatoriP30938.

Interactioni

Subunit structurei

Heterodimer with SSTR2. Heterodimerization with SSTR2 increases cell growth inhibition activity of SSTR2 (By similarity).By similarity

Protein-protein interaction databases

IntActiP30938. 1 interaction.
MINTiMINT-1489396.
STRINGi10116.ENSRNOP00000025451.

Structurei

3D structure databases

ProteinModelPortaliP30938.
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.
HOGENOMiHOG000230485.
HOVERGENiHBG106919.
InParanoidiP30938.
PhylomeDBiP30938.

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.

P30938-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPLSLASTP SWNASAASSG NHNWSLVGSA SPMGARAVLV PVLYLLVCTV
60 70 80 90 100
GLSGNTLVIY VVLRHAKMKT VTNVYILNLA VADVLFMLGL PFLATQNAVV
110 120 130 140 150
SYWPFGSFLC RLVMTLDGIN QFTSIFCLMV MSVDRYLAVV HPLRSARWRR
160 170 180 190 200
PRVAKMASAA VWVFSLLMSL PLLVFADVQE GWGTCNLSWP EPVGLWGAAF
210 220 230 240 250
ITYTSVLGFF GPLLVICLCY LLIVVKVKAA GMRVGSSRRR RSEPKVTRMV
260 270 280 290 300
VVVVLVFVGC WLPFFIVNIV NLAFTLPEEP TSAGLYFFVV VLSYANSCAN
310 320 330 340 350
PLLYGFLSDN FRQSFRKVLC LRRGYGMEDA DAIEPRPDKS GRPQATLPTR
360
SCEANGLMQT SRI
Length:363
Mass (Da):39,971
Last modified:February 1, 1995 - v2
Checksum:i4BD4512960613B4A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04535 mRNA. Translation: AAA17029.1.
U01152 mRNA. Translation: AAC09011.1.
X74828 mRNA. Translation: CAA52825.1.
PIRiI57940.
UniGeneiRn.91342.

Genome annotation databases

UCSCiRGD:3765. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04535 mRNA. Translation: AAA17029.1.
U01152 mRNA. Translation: AAC09011.1.
X74828 mRNA. Translation: CAA52825.1.
PIRiI57940.
UniGeneiRn.91342.

3D structure databases

ProteinModelPortaliP30938.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP30938. 1 interaction.
MINTiMINT-1489396.
STRINGi10116.ENSRNOP00000025451.

Chemistry

BindingDBiP30938.
ChEMBLiCHEMBL4318.
GuidetoPHARMACOLOGYi359.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP30938.

Proteomic databases

PRIDEiP30938.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3765. rat.

Organism-specific databases

RGDi3765. Sstr5.

Phylogenomic databases

eggNOGiNOG274661.
HOGENOMiHOG000230485.
HOVERGENiHBG106919.
InParanoidiP30938.
PhylomeDBiP30938.

Miscellaneous databases

PROiP30938.

Gene expression databases

GenevestigatoriP30938.

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

  1. "Molecular cloning and expression of a pituitary somatostatin receptor with preferential affinity for somatostatin-28."
    O'Carroll A.-M., Lolait S.J., Konig M., Mahan L.C.
    Mol. Pharmacol. 42:939-946(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Pituitary.
  2. "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: SEQUENCE REVISION TO C-TERMINUS, FUNCTION, TISSUE SPECIFICITY.
    Tissue: Pituitary.
  3. "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: INTERACTION WITH ZDHHC5.

Entry informationi

Entry nameiSSR5_RAT
AccessioniPrimary (citable) accession number: P30938
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 1995
Last modified: February 4, 2015
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. 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.