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P32745 (SSR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length418 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

Subunit structure

Homodimer and heterodimer with SSTR2. Heterodimerization with SSTR2 inactivates SSTR3 receptor function By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Note: Internalized into endoplasmic vesicles upon somatostatin-stimulation By similarity.

Tissue specificity

Brain, pituitary and pancreas. Ref.1

Post-translational modification

Phosphorylated. Phosphorylation increases upon somatostatin binding By similarity.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger

Traceable author statement PubMed 8405411. Source: ProtInc

cell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

cellular response to estradiol stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to glucocorticoid stimulus

Inferred from electronic annotation. Source: Ensembl

cerebellum development

Inferred from electronic annotation. Source: Ensembl

forebrain development

Inferred from electronic annotation. Source: Ensembl

hormone-mediated apoptotic signaling pathway

Traceable author statement PubMed 8961277. Source: ProtInc

negative regulation of cell proliferation

Traceable author statement PubMed 8961277. Source: ProtInc

response to starvation

Inferred from electronic annotation. Source: Ensembl

somatostatin signaling pathway

Traceable author statement PubMed 8405411. Source: GOC

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentciliary membrane

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

nonmotile primary cilium

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 19071123PubMed 22651821. Source: IntAct

somatostatin receptor activity

Traceable author statement PubMed 8405411. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MPDZO759705EBI-6266935,EBI-821405
MpdzO551642EBI-6266935,EBI-7401093From a different organism.
SSTR2P308743EBI-6266935,EBI-6266898

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418Somatostatin receptor type 3
PRO_0000070124

Regions

Topological domain1 – 4343Extracellular Potential
Transmembrane44 – 6926Helical; Name=1; Potential
Topological domain70 – 7910Cytoplasmic Potential
Transmembrane80 – 10122Helical; Name=2; Potential
Topological domain102 – 11615Extracellular Potential
Transmembrane117 – 13822Helical; Name=3; Potential
Topological domain139 – 16123Cytoplasmic Potential
Transmembrane162 – 18120Helical; Name=4; Potential
Topological domain182 – 20524Extracellular Potential
Transmembrane206 – 23126Helical; Name=5; Potential
Topological domain232 – 25726Cytoplasmic Potential
Transmembrane258 – 27922Helical; Name=6; Potential
Topological domain280 – 29314Extracellular Potential
Transmembrane294 – 31623Helical; Name=7; Potential
Topological domain317 – 418102Cytoplasmic Potential
Compositional bias346 – 36015Glu-rich (acidic)

Amino acid modifications

Modified residue3481Phosphothreonine By similarity
Glycosylation171N-linked (GlcNAc...) Potential
Glycosylation301N-linked (GlcNAc...) Potential
Disulfide bond116 ↔ 191 By similarity

Natural variations

Natural variant331A → V.
Corresponds to variant rs4988466 [ dbSNP | Ensembl ].
VAR_029219
Natural variant371P → L.
Corresponds to variant rs34943557 [ dbSNP | Ensembl ].
VAR_049440
Natural variant2511S → F.
Corresponds to variant rs6413537 [ dbSNP | Ensembl ].
VAR_020072
Natural variant3361R → C.
Corresponds to variant rs4988469 [ dbSNP | Ensembl ].
VAR_029220
Natural variant4111S → T.
Corresponds to variant rs229568 [ dbSNP | Ensembl ].
VAR_011853
Natural variant4141R → H.
Corresponds to variant rs4988471 [ dbSNP | Ensembl ].
VAR_029221

Sequences

Sequence LengthMass (Da)Tools
P32745 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 1227095F801190C4

FASTA41845,847
        10         20         30         40         50         60 
MDMLHPSSVS TTSEPENASS AWPPDATLGN VSAGPSPAGL AVSGVLIPLV YLVVCVVGLL 

        70         80         90        100        110        120 
GNSLVIYVVL RHTASPSVTN VYILNLALAD ELFMLGLPFL AAQNALSYWP FGSLMCRLVM 

       130        140        150        160        170        180 
AVDGINQFTS IFCLTVMSVD RYLAVVHPTR SARWRTAPVA RTVSAAVWVA SAVVVLPVVV 

       190        200        210        220        230        240 
FSGVPRGMST CHMQWPEPAA AWRAGFIIYT AALGFFGPLL VICLCYLLIV VKVRSAGRRV 

       250        260        270        280        290        300 
WAPSCQRRRR SERRVTRMVV AVVALFVLCW MPFYVLNIVN VVCPLPEEPA FFGLYFLVVA 

       310        320        330        340        350        360 
LPYANSCANP ILYGFLSYRF KQGFRRVLLR PSRRVRSQEP TVGPPEKTEE EDEEEEDGEE 

       370        380        390        400        410 
SREGGKGKEM NGRVSQITQP GTSGQERPPS RVASKEQQLL PQEASTGEKS STMRISYL 

« Hide

References

« Hide 'large scale' references
[1]"Somatostatin receptors, an expanding gene family: cloning and functional characterization of human SSTR3, a protein coupled to adenylyl cyclase."
Yamada Y., Reisine T., Law S.F., Ihara Y., Kubota A., Kagimoto S., Seino M., Seino Y., Bell G.I., Seino S.
Mol. Endocrinol. 6:2136-2142(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
[2]"A human somatostatin receptor (SSTR3), located on chromosome 22, displays preferential affinity for somatostatin-14 like peptides."
Corness J.D., Demchyshyn L.L., Seeman P., van Tol H.H.M., Srikant C.B., Kent G., Patel Y.C., Niznik H.B.
FEBS Lett. 321:279-284(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The human somatostatin receptor subtype 3 contains an upstream exon in the 5'-untranslated region: functional promoter studies."
Rasch A.C., Boehnke C., Petersenn S.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Kopatz S.A., Aronstam R.S., Sharma S.V.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96738 Genomic DNA. Translation: AAA60592.1.
AY277678 Genomic DNA. Translation: AAP32288.1.
AY322541 Genomic DNA. Translation: AAP84354.1.
CR456585 mRNA. Translation: CAG30471.1.
AK291165 mRNA. Translation: BAF83854.1.
Z82188 Genomic DNA. Translation: CAB45263.1.
BC096829 mRNA. Translation: AAH96829.1.
CCDSCCDS13944.1.
PIRA46226.
RefSeqNP_001042.1. NM_001051.4.
NP_001265616.1. NM_001278687.2.
XP_005261778.1. XM_005261721.2.
XP_006724374.1. XM_006724311.1.
UniGeneHs.225995.
Hs.255208.

3D structure databases

ProteinModelPortalP32745.
SMRP32745. Positions 37-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112631. 13 interactions.
IntActP32745. 9 interactions.
MINTMINT-6800539.
STRING9606.ENSP00000330138.

Chemistry

BindingDBP32745.
ChEMBLCHEMBL2028.
GuidetoPHARMACOLOGY357.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP32745.

Polymorphism databases

DMDM417815.

Proteomic databases

PaxDbP32745.
PRIDEP32745.

Protocols and materials databases

DNASU6753.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328544; ENSP00000330138; ENSG00000183473.
ENST00000402501; ENSP00000384904; ENSG00000183473.
GeneID6753.
KEGGhsa:6753.
UCSCuc003ara.3. human.

Organism-specific databases

CTD6753.
GeneCardsGC22M037600.
HGNCHGNC:11332. SSTR3.
HPACAB022647.
MIM182453. gene.
neXtProtNX_P32745.
PharmGKBPA36156.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG274661.
HOGENOMHOG000230485.
HOVERGENHBG106919.
InParanoidP32745.
KOK04219.
OMANASSAWP.
OrthoDBEOG7BKCVQ.
PhylomeDBP32745.
TreeFamTF315737.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP32745.
BgeeP32745.
CleanExHS_SSTR3.
GenevestigatorP32745.

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

GeneWikiSomatostatin_receptor_3.
GenomeRNAi6753.
NextBio26344.
PROP32745.
SOURCESearch...

Entry information

Entry nameSSR3_HUMAN
AccessionPrimary (citable) accession number: P32745
Secondary accession number(s): A8K550, Q53ZR7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries