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P91682 (SMO_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Protein smoothened
Alternative name(s):
SMOH
Smooth
dSMO
Gene names
Name:smo
ORF Names:CG11561
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1036 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Segment polarity protein required for correct patterning of every segment. G protein-coupled receptor that associates with the patched protein (ptc) to transduce the hedgehog (hh) signal through the activation of an inhibitory G-protein. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu).

Subunit structure

Interacts with cos. Ref.6

Subcellular location

Membrane; Multi-pass membrane protein.

Developmental stage

Expressed at all developmental stages, though the levels vary.

Sequence similarities

Belongs to the G-protein coupled receptor Fz/Smo family.

Contains 1 FZ (frizzled) domain.

Caution

It is uncertain whether Met-1, Met-9, Met-13 or Met-14 is the initiator.

Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
G-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBolwig's organ morphogenesis

Inferred from mutant phenotype PubMed 10704398. Source: FlyBase

Wnt signaling pathway

Traceable author statement PubMed 8330533. Source: FlyBase

adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway

Inferred from mutant phenotype PubMed 18987629. Source: FlyBase

anterior/posterior lineage restriction, imaginal disc

Traceable author statement PubMed 10625531. Source: FlyBase

axon extension involved in axon guidance

Inferred from Biological aspect of Ancestor. Source: RefGenome

blastoderm segmentation

Inferred from mutant phenotype Ref.2. Source: FlyBase

canonical Wnt signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

cardioblast differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

cerebellar cortex morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

ciliary receptor clustering involved in smoothened signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

determination of left/right symmetry

Inferred from Biological aspect of Ancestor. Source: RefGenome

eye morphogenesis

Inferred from mutant phenotype PubMed 16651542. Source: FlyBase

eye-antennal disc morphogenesis

Inferred from genetic interaction PubMed 11934850. Source: FlyBase

gonad development

Inferred from Biological aspect of Ancestor. Source: RefGenome

heart morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 15809036. Source: FlyBase

negative regulation of Notch signaling pathway

Inferred from genetic interaction PubMed 23667323. Source: FlyBase

negative regulation of apoptotic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuron fate commitment

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuron projection regeneration

Inferred from Biological aspect of Ancestor. Source: RefGenome

ovarian follicle cell development

Inferred from mutant phenotype PubMed 16256740. Source: FlyBase

positive regulation of establishment of protein localization to plasma membrane

Inferred from direct assay PubMed 17658259. Source: FlyBase

positive regulation of neuroblast proliferation

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of smoothened signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of apoptotic process

Inferred from genetic interaction PubMed 23018595. Source: FlyBase

regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 11279500. Source: FlyBase

signal transduction

Inferred from sequence or structural similarity PubMed 10908591. Source: FlyBase

smoothened signaling pathway

Inferred from mutant phenotype PubMed 14597665PubMed 8898207. Source: FlyBase

smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation

Inferred from Biological aspect of Ancestor. Source: RefGenome

somatic stem cell maintenance

Inferred from mutant phenotype PubMed 16256740. Source: FlyBase

vasculogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

wing disc anterior/posterior pattern formation

Traceable author statement PubMed 11253649. Source: FlyBase

   Cellular_componentcilium

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

endosome

Traceable author statement PubMed 15104233. Source: FlyBase

integral component of membrane

Inferred from sequence or structural similarity PubMed 10908591Ref.1. Source: FlyBase

integral component of plasma membrane

Inferred from direct assay PubMed 10966113. Source: FlyBase

neuronal cell body

Inferred from Biological aspect of Ancestor. Source: RefGenome

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionG-protein coupled receptor activity

Inferred from sequence or structural similarity Ref.1. Source: FlyBase

PDZ domain binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt-activated receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt-protein binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

hedgehog receptor activity

Non-traceable author statement PubMed 11253649. Source: FlyBase

protein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

transmembrane signaling receptor activity

Inferred from sequence or structural similarity PubMed 10908591. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

cosO168445EBI-142245,EBI-102069

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 10361005Protein smoothened
PRO_0000013019

Regions

Topological domain32 – 258227Extracellular Potential
Transmembrane259 – 27921Helical; Name=1; Potential
Topological domain280 – 2878Cytoplasmic Potential
Transmembrane288 – 30821Helical; Name=2; Potential
Topological domain309 – 33931Extracellular Potential
Transmembrane340 – 36021Helical; Name=3; Potential
Topological domain361 – 38121Cytoplasmic Potential
Transmembrane382 – 40221Helical; Name=4; Potential
Topological domain403 – 42119Extracellular Potential
Transmembrane422 – 44221Helical; Name=5; Potential
Topological domain443 – 46927Cytoplasmic Potential
Transmembrane470 – 49021Helical; Name=6; Potential
Topological domain491 – 53242Extracellular Potential
Transmembrane533 – 55321Helical; Name=7; Potential
Topological domain554 – 1036483Cytoplasmic Potential
Domain85 – 206122FZ
Compositional bias816 – 8194Poly-Ser

Amino acid modifications

Modified residue6581Phosphoserine Ref.7
Modified residue6591Phosphoserine Ref.7
Modified residue6671Phosphoserine Ref.7
Modified residue6701Phosphoserine Ref.7
Modified residue6731Phosphoserine Ref.7
Modified residue6871Phosphoserine Ref.7
Modified residue6901Phosphoserine Ref.7
Modified residue6931Phosphoserine Ref.7
Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation4191N-linked (GlcNAc...) Potential
Disulfide bond90 ↔ 155 Ref.8
Disulfide bond100 ↔ 148 Ref.8
Disulfide bond139 ↔ 179 Ref.8
Disulfide bond172 ↔ 194 Ref.8
Disulfide bond218 ↔ 238 By similarity
Disulfide bond242 ↔ 320 By similarity
Disulfide bond339 ↔ 413 By similarity
Disulfide bond513 ↔ 525 By similarity

Secondary structure

........................ 1036
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P91682 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 7797FC71A539A87A

FASTA1,036116,552
        10         20         30         40         50         60 
MQYLNFPRMP NIMMFLEVAI LCLWVVADAS ASSAKFGSTT PASAQQSDVE LEPINGTLNY 

        70         80         90        100        110        120 
RLYAKKGRDD KPWFDGLDSR HIQCVRRARC YPTSNATNTC FGSKLPYELS SLDLTDFHTE 

       130        140        150        160        170        180 
KELNDKLNDY YALKHVPKCW AAIQPFLCAV FKPKCEKING EDMVYLPSYE MCRITMEPCR 

       190        200        210        220        230        240 
ILYNTTFFPK FLRCNETLFP TKCTNGARGM KFNGTGQCLS PLVPTDTSAS YYPGIEGCGV 

       250        260        270        280        290        300 
RCKDPLYTDD EHRQIHKLIG WAGSICLLSN LFVVSTFFID WKNANKYPAV IVFYINLCFL 

       310        320        330        340        350        360 
IACVGWLLQF TSGSREDIVC RKDGTLRHSE PTAGENLSCI VIFVLVYYFL TAGMVWFVFL 

       370        380        390        400        410        420 
TYAWHWRAMG HVQDRIDKKG SYFHLVAWSL PLVLTITTMA FSEVDGNSIV GICFVGYINH 

       430        440        450        460        470        480 
SMRAGLLLGP LCGVILIGGY FITRGMVMLF GLKHFANDIK STSASNKIHL IIMRMGVCAL 

       490        500        510        520        530        540 
LTLVFILVAI ACHVTEFRHA DEWAQSFRQF IICKISSVFE EKSSCRIENR PSVGVLQLHL 

       550        560        570        580        590        600 
LCLFSSGIVM STWCWTPSSI ETWKRYIRKK CGKEVVEEVK MPKHKVIAQT WAKRKDFEDK 

       610        620        630        640        650        660 
GRLSITLYNT HTDPVGLNFD VNDLNSSETN DISSTWAAYL PQCVKRRMAL TGAATGNSSS 

       670        680        690        700        710        720 
HGPRKNSLDS EISVSVRHVS VESRRNSVDS QVSVKIAEMK TKVASRSRGK HGGSSSNRRT 

       730        740        750        760        770        780 
QRRRDYIAAA TGKSSRRRES STSVESQVIA LKKTTYPNAS HKVGVFAHHS SKKQHNYTSS 

       790        800        810        820        830        840 
MKRRTANAGL DPSILNEFLQ KNGDFIFPFL QNQDMSSSSE EDNSRASQKI QDLNVVVKQQ 

       850        860        870        880        890        900 
EISEDDHDGI KIEELPNSKQ VALENFLKNI KKSNESNSNR HSRNSARSQS KKSQKRHLKN 

       910        920        930        940        950        960 
PAADLDFRKD CVKYRSNDSL SCSSEELDVA LDVGSLLNSS FSGISMGKPH SRNSKTSCDV 

       970        980        990       1000       1010       1020 
GIQANPFELV PSYGEDELQQ AMRLLNAASR QRTEAANEDF GGTELQGLLG HSHRHQREPT 

      1030 
FMSESDKLKM LLLPSK 

« Hide

References

« Hide 'large scale' references
[1]"The Drosophila smoothened gene encodes a seven-pass membrane protein, a putative receptor for the hedgehog signal."
Alcedo J., Ayzenzon M., von Ohlen T., Noll M., Hooper J.E.
Cell 86:221-232(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"smoothened encodes a receptor-like serpentine protein required for hedgehog signalling."
van den Heuvel M., Ingham P.W.
Nature 382:547-551(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
[6]"Hedgehog-regulated Costal2-kinase complexes control phosphorylation and proteolytic processing of Cubitus interruptus."
Zhang W., Zhao Y., Tong C., Wang G., Wang B., Jia J., Jiang J.
Dev. Cell 8:267-278(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COS.
[7]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658; SER-659; SER-667; SER-670; SER-673; SER-687; SER-690 AND SER-693, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
[8]"Structural insights into the role of the Smoothened cysteine-rich domain in Hedgehog signalling."
Rana R., Carroll C.E., Lee H.J., Bao J., Marada S., Grace C.R., Guibao C.D., Ogden S.K., Zheng J.J.
Nat. Commun. 4:2965-2974(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 85-202, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U87613 Genomic DNA. Translation: AAC33180.1.
AF030334 Genomic DNA. Translation: AAB84275.1.
AE014134 Genomic DNA. Translation: AAF51518.2.
BT053691 mRNA. Translation: ACK77608.1.
PIRS71804.
RefSeqNP_523443.1. NM_078719.3.
UniGeneDm.244.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2MAHNMR-A85-202[»]
ProteinModelPortalP91682.
SMRP91682. Positions 76-202.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid59452. 17 interactions.
DIPDIP-19956N.
IntActP91682. 3 interactions.
MINTMINT-811118.

Protein family/group databases

GPCRDBSearch...

Proteomic databases

PRIDEP91682.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0078129; FBpp0077788; FBgn0003444.
GeneID33196.
KEGGdme:Dmel_CG11561.
UCSCCG11561-RA. d. melanogaster.

Organism-specific databases

CTD6608.
FlyBaseFBgn0003444. smo.

Phylogenomic databases

eggNOGNOG312505.
GeneTreeENSGT00750000117492.
InParanoidP91682.
KOK06226.
OMANANKYPA.
OrthoDBEOG74J972.
PhylomeDBP91682.

Enzyme and pathway databases

SignaLinkP91682.

Gene expression databases

BgeeP91682.

Family and domain databases

Gene3D1.10.2000.10. 1 hit.
InterProIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR017981. GPCR_2-like.
IPR026544. SMO.
[Graphical view]
PANTHERPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF35. PTHR11309:SF35. 1 hit.
PfamPF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
PRINTSPR00489. FRIZZLED.
SMARTSM00063. FRI. 1 hit.
[Graphical view]
SUPFAMSSF63501. SSF63501. 1 hit.
PROSITEPS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi33196.
NextBio782367.
PROP91682.

Entry information

Entry nameSMO_DROME
AccessionPrimary (citable) accession number: P91682
Secondary accession number(s): B7FNK1, Q9VPM8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries