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O08858 (SSR5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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 5
Short name=SS-5-R
Short name=SS5-R
Short name=SS5R
Gene names
Name:Sstr5
Synonyms:Smstr5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for somatostatin-28. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase.

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.8.

Post-translational modification

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. Ref.8

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362Somatostatin receptor type 5
PRO_0000070131

Regions

Topological domain1 – 3535Extracellular Potential
Transmembrane36 – 6328Helical; Name=1; Potential
Topological domain64 – 7310Cytoplasmic Potential
Transmembrane74 – 9926Helical; Name=2; Potential
Topological domain100 – 11011Extracellular Potential
Transmembrane111 – 13222Helical; Name=3; Potential
Topological domain133 – 15422Cytoplasmic Potential
Transmembrane155 – 17521Helical; Name=4; Potential
Topological domain176 – 19520Extracellular Potential
Transmembrane196 – 22025Helical; Name=5; Potential
Topological domain221 – 24626Cytoplasmic Potential
Transmembrane247 – 27226Helical; Name=6; Potential
Topological domain273 – 28210Extracellular Potential
Transmembrane283 – 30725Helical; Name=7; Potential
Topological domain308 – 36255Cytoplasmic Potential

Amino acid modifications

Lipidation3191S-palmitoyl cysteine; by ZDHHC5 Ref.8
Glycosylation131N-linked (GlcNAc...) Potential
Glycosylation231N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Potential
Disulfide bond109 ↔ 184 By similarity

Experimental info

Sequence conflict71T → A in AAC53353. Ref.1
Sequence conflict71T → A in AAB61418. Ref.2
Sequence conflict71T → A in AAB86492. Ref.3
Sequence conflict71T → A in AAB88302. Ref.4
Sequence conflict71T → A in AAI45944. Ref.7
Sequence conflict71T → A in AAI50806. Ref.7
Sequence conflict201S → G in AAC53353. Ref.1
Sequence conflict201S → G in AAB61418. Ref.2
Sequence conflict201S → G in AAB86492. Ref.3
Sequence conflict201S → G in AAB88302. Ref.4
Sequence conflict201S → G in AAI45944. Ref.7
Sequence conflict201S → G in AAI50806. Ref.7
Sequence conflict991V → VV in AAC53353. Ref.1
Sequence conflict303 – 3053YGF → LWL in AAB61418. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O08858 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: C069149B8A8141C4

FASTA36240,008
        10         20         30         40         50         60 
MEPLSLTSTP SWNASAASSS SHNWSLVDPV SPMGARAVLV PVLYLLVCTV GLGGNTLVIY 

        70         80         90        100        110        120 
VVLRYAKMKT VTNVYILNLA VADVLFMLGL PFLATQNAVS YWPFGSFLCR LVMTLDGINQ 

       130        140        150        160        170        180 
FTSIFCLMVM SVDRYLAVVH PLRSARWRRP RVAKLASAAV WVFSLLMSLP LLVFADVQEG 

       190        200        210        220        230        240 
WGTCNLSWPE PVGLWGAAFI TYTSVLGFFG PLLVICLCYL LIVVKVKAAG MRVGSSRRRR 

       250        260        270        280        290        300 
SERKVTRMVV VVVLVFVGCW LPFFIVNIVN LAFTLPEEPT SAGLYFFVVV LSYANSCANP 

       310        320        330        340        350        360 
LLYGFLSDNF RQSFRKALCL RRGYGVEDAD AIEPRPDKSG RPQTTLPTRS CEANGLMQTS 


RL

« Hide

References

« Hide 'large scale' references
[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].
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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00116387.
RefSeqNP_001177937.1. NM_001191008.1.
NP_035555.1. NM_011425.3.
UniGeneMm.353282.
Mm.489569.
Mm.491029.

3D structure databases

ProteinModelPortalO08858.
SMRO08858. Positions 32-315.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1489456.
STRING10090.ENSMUSP00000051085.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteO08858.

Proteomic databases

PRIDEO08858.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000051864; ENSMUSP00000051085; ENSMUSG00000050824.
ENSMUST00000165183; ENSMUSP00000128787; ENSMUSG00000050824.
GeneID20609.
KEGGmmu:20609.

Organism-specific databases

CTD6755.
MGIMGI:894282. Sstr5.

Phylogenomic databases

eggNOGNOG274661.
GeneTreeENSGT00630000089736.
HOVERGENHBG106919.
InParanoidA6H6N8.
KOK04221.
OMAGLMQTSK.
OrthoDBEOG4Q84Z1.

Gene expression databases

BgeeO08858.
CleanExMM_SSTR5.
GenevestigatorO08858.
GermOnlineENSMUSG00000050824. Mus musculus.

Family and domain databases

InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000586. Somatstn_rcpt.
IPR001184. Somatstn_rcpt_5.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00246. SOMATOSTATNR.
PR00591. SOMATOSTTN5R.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBO08858.
ChEMBLCHEMBL2733.
NextBio298963.
SOURCESearch...

Entry information

Entry nameSSR5_MOUSE
AccessionPrimary (citable) accession number: O08858
Secondary accession number(s): A6H6N8, O08998, Q3UZM7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents