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Protein

Somatostatin receptor type 5

Gene

Sstr5

Organism
Mus musculus (Mouse)
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.

GO - Molecular functioni

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

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: MGI
  4. G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: GO_Central
  5. negative regulation of cell proliferation Source: GO_Central
  6. neuropeptide signaling pathway Source: GO_Central
  7. positive regulation of cytokinesis Source: MGI
  8. regulation of insulin secretion Source: MGI
  9. somatostatin signaling pathway Source: GO_Central
  10. synaptic transmission Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_235286. Peptide ligand-binding receptors.
REACT_250376. 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
Synonyms:Smstr5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:894282. Sstr5.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

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 – 11011ExtracellularSequence AnalysisAdd
BLAST
Transmembranei111 – 13222Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini133 – 15422CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei155 – 17521Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini176 – 19520ExtracellularSequence AnalysisAdd
BLAST
Transmembranei196 – 22025Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini221 – 24626CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei247 – 27226Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini273 – 28210ExtracellularSequence Analysis
Transmembranei283 – 30725Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini308 – 36255CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 362362Somatostatin receptor type 5PRO_0000070131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi13 – 131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi23 – 231N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi109 ↔ 184PROSITE-ProRule annotation
Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence Analysis
Lipidationi319 – 3191S-palmitoyl cysteine; by ZDHHC51 Publication

Post-translational modificationi

Palmitoylated at Cys-319 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.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PRIDEiO08858.

PTM databases

PhosphoSiteiO08858.

Expressioni

Tissue specificityi

Expressed in adult brain but not in liver, heart, spleen, or kidney.1 Publication

Gene expression databases

BgeeiO08858.
CleanExiMM_SSTR5.
GenevestigatoriO08858.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiO08858. 1 interaction.
MINTiMINT-1489456.
STRINGi10090.ENSMUSP00000051085.

Structurei

3D structure databases

ProteinModelPortaliO08858.
SMRiO08858. Positions 35-319.
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.
HOVERGENiHBG106919.
InParanoidiO08858.
KOiK04221.
OMAiNAVSYWP.
OrthoDBiEOG7BKCVQ.
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.

O08858-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEPLSLTSTP SWNASAASSS SHNWSLVDPV SPMGARAVLV PVLYLLVCTV
60 70 80 90 100
GLGGNTLVIY VVLRYAKMKT VTNVYILNLA VADVLFMLGL PFLATQNAVS
110 120 130 140 150
YWPFGSFLCR LVMTLDGINQ FTSIFCLMVM SVDRYLAVVH PLRSARWRRP
160 170 180 190 200
RVAKLASAAV WVFSLLMSLP LLVFADVQEG WGTCNLSWPE PVGLWGAAFI
210 220 230 240 250
TYTSVLGFFG PLLVICLCYL LIVVKVKAAG MRVGSSRRRR SERKVTRMVV
260 270 280 290 300
VVVLVFVGCW LPFFIVNIVN LAFTLPEEPT SAGLYFFVVV LSYANSCANP
310 320 330 340 350
LLYGFLSDNF RQSFRKALCL RRGYGVEDAD AIEPRPDKSG RPQTTLPTRS
360
CEANGLMQTS RL
Length:362
Mass (Da):40,008
Last modified:July 27, 2011 - v3
Checksum:iC069149B8A8141C4
GO

Sequence cautioni

The sequence AAB88302.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71T → A in AAC53353. (PubMed:9300821)Curated
Sequence conflicti7 – 71T → A in AAB61418. 1 PublicationCurated
Sequence conflicti7 – 71T → A in AAB86492. 1 PublicationCurated
Sequence conflicti7 – 71T → A in AAB88302. 1 PublicationCurated
Sequence conflicti7 – 71T → A in AAI45944. (PubMed:15489334)Curated
Sequence conflicti7 – 71T → A in AAI50806. (PubMed:15489334)Curated
Sequence conflicti20 – 201S → G in AAC53353. (PubMed:9300821)Curated
Sequence conflicti20 – 201S → G in AAB61418. 1 PublicationCurated
Sequence conflicti20 – 201S → G in AAB86492. 1 PublicationCurated
Sequence conflicti20 – 201S → G in AAB88302. 1 PublicationCurated
Sequence conflicti20 – 201S → G in AAI45944. (PubMed:15489334)Curated
Sequence conflicti20 – 201S → G in AAI50806. (PubMed:15489334)Curated
Sequence conflicti99 – 991V → VV in AAC53353. (PubMed:9300821)Curated
Sequence conflicti303 – 3053YGF → LWL in AAB61418. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82697 Genomic DNA. Translation: AAC53353.1.
AF004740 Genomic DNA. Translation: AAB61418.1.
AF030441 Genomic DNA. Translation: AAB86492.1.
AF035777 Genomic DNA. Translation: AAB88302.1. Different initiation.
AK133609 mRNA. Translation: BAE21747.1.
AK133767 mRNA. Translation: BAE21829.1.
AC131323 Genomic DNA. No translation available.
BC145943 mRNA. Translation: AAI45944.1.
BC150805 mRNA. Translation: AAI50806.1.
CCDSiCCDS28520.1.
RefSeqiNP_001177937.1. NM_001191008.1.
NP_035555.1. NM_011425.3.
XP_006524010.1. XM_006523947.1.
UniGeneiMm.353282.
Mm.489569.
Mm.491029.

Genome annotation databases

EnsembliENSMUST00000051864; ENSMUSP00000051085; ENSMUSG00000050824.
ENSMUST00000165183; ENSMUSP00000128787; ENSMUSG00000050824.
GeneIDi20609.
KEGGimmu:20609.
UCSCiuc008bax.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82697 Genomic DNA. Translation: AAC53353.1.
AF004740 Genomic DNA. Translation: AAB61418.1.
AF030441 Genomic DNA. Translation: AAB86492.1.
AF035777 Genomic DNA. Translation: AAB88302.1. Different initiation.
AK133609 mRNA. Translation: BAE21747.1.
AK133767 mRNA. Translation: BAE21829.1.
AC131323 Genomic DNA. No translation available.
BC145943 mRNA. Translation: AAI45944.1.
BC150805 mRNA. Translation: AAI50806.1.
CCDSiCCDS28520.1.
RefSeqiNP_001177937.1. NM_001191008.1.
NP_035555.1. NM_011425.3.
XP_006524010.1. XM_006523947.1.
UniGeneiMm.353282.
Mm.489569.
Mm.491029.

3D structure databases

ProteinModelPortaliO08858.
SMRiO08858. Positions 35-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08858. 1 interaction.
MINTiMINT-1489456.
STRINGi10090.ENSMUSP00000051085.

Chemistry

BindingDBiO08858.
ChEMBLiCHEMBL2111427.
GuidetoPHARMACOLOGYi359.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiO08858.

Proteomic databases

PRIDEiO08858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000051864; ENSMUSP00000051085; ENSMUSG00000050824.
ENSMUST00000165183; ENSMUSP00000128787; ENSMUSG00000050824.
GeneIDi20609.
KEGGimmu:20609.
UCSCiuc008bax.2. mouse.

Organism-specific databases

CTDi6755.
MGIiMGI:894282. Sstr5.

Phylogenomic databases

eggNOGiNOG274661.
GeneTreeiENSGT00760000118797.
HOVERGENiHBG106919.
InParanoidiO08858.
KOiK04221.
OMAiNAVSYWP.
OrthoDBiEOG7BKCVQ.
TreeFamiTF315737.

Enzyme and pathway databases

ReactomeiREACT_235286. Peptide ligand-binding receptors.
REACT_250376. G alpha (i) signalling events.

Miscellaneous databases

NextBioi298963.
PROiO08858.
SOURCEiSearch...

Gene expression databases

BgeeiO08858.
CleanExiMM_SSTR5.
GenevestigatoriO08858.

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. "Isolation and characterization of the gene encoding the type 5 mouse (Mus musculus) somatostatin receptor (msst5)."
    Lublin A.L., Diehl N.L., Hochgeschwender U.
    Gene 195:63-66(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Strain: 129/SvJ.
    Tissue: Liver.
  2. Moldovan S., DeMayo F., Brunicardi F.C.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  3. Gordon D.F., Woodmansee W.W., Wood W.M., Knauf H., James R.A.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/c.
    Tissue: Liver.
  4. Baumeister H., Roosterman D., Schafer J., Kreuzer O., Meyerhof W.
    Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pituitary.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  8. "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: TOPOLOGY, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-319.

Entry informationi

Entry nameiSSR5_MOUSE
AccessioniPrimary (citable) accession number: O08858
Secondary accession number(s): A6H6N8, O08998, Q3UZM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 116 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. 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.