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P91682

- SMO_DROME

UniProt

P91682 - SMO_DROME

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Protein

Protein smoothened

Gene
smo, CG11561
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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).

GO - Molecular functioni

  1. G-protein coupled receptor activity Source: FlyBase
  2. hedgehog receptor activity Source: FlyBase
  3. PDZ domain binding Source: RefGenome
  4. protein binding Source: UniProtKB
  5. transmembrane signaling receptor activity Source: FlyBase
  6. Wnt-activated receptor activity Source: RefGenome
  7. Wnt-protein binding Source: RefGenome

GO - Biological processi

  1. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: FlyBase
  2. anterior/posterior lineage restriction, imaginal disc Source: FlyBase
  3. axon extension involved in axon guidance Source: RefGenome
  4. blastoderm segmentation Source: FlyBase
  5. Bolwig's organ morphogenesis Source: FlyBase
  6. canonical Wnt signaling pathway Source: RefGenome
  7. cardioblast differentiation Source: RefGenome
  8. cerebellar cortex morphogenesis Source: RefGenome
  9. ciliary receptor clustering involved in smoothened signaling pathway Source: RefGenome
  10. determination of left/right symmetry Source: RefGenome
  11. eye-antennal disc morphogenesis Source: FlyBase
  12. eye morphogenesis Source: FlyBase
  13. gonad development Source: RefGenome
  14. heart morphogenesis Source: RefGenome
  15. negative regulation of apoptotic process Source: RefGenome
  16. negative regulation of G1/S transition of mitotic cell cycle Source: FlyBase
  17. negative regulation of Notch signaling pathway Source: FlyBase
  18. neuron fate commitment Source: RefGenome
  19. neuron projection regeneration Source: RefGenome
  20. ovarian follicle cell development Source: FlyBase
  21. positive regulation of establishment of protein localization to plasma membrane Source: FlyBase
  22. positive regulation of neuroblast proliferation Source: RefGenome
  23. positive regulation of smoothened signaling pathway Source: RefGenome
  24. regulation of apoptotic process Source: FlyBase
  25. regulation of mitotic cell cycle Source: FlyBase
  26. signal transduction Source: FlyBase
  27. smoothened signaling pathway Source: FlyBase
  28. smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation Source: RefGenome
  29. somatic stem cell maintenance Source: FlyBase
  30. vasculogenesis Source: RefGenome
  31. wing disc anterior/posterior pattern formation Source: FlyBase
  32. Wnt signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

SignaLinkiP91682.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein smoothened
Alternative name(s):
SMOH
Smooth
dSMO
Gene namesi
Name:smo
ORF Names:CG11561
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0003444. smo.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 258227Extracellular Reviewed predictionAdd
BLAST
Transmembranei259 – 27921Helical; Name=1; Reviewed predictionAdd
BLAST
Topological domaini280 – 2878Cytoplasmic Reviewed prediction
Transmembranei288 – 30821Helical; Name=2; Reviewed predictionAdd
BLAST
Topological domaini309 – 33931Extracellular Reviewed predictionAdd
BLAST
Transmembranei340 – 36021Helical; Name=3; Reviewed predictionAdd
BLAST
Topological domaini361 – 38121Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei382 – 40221Helical; Name=4; Reviewed predictionAdd
BLAST
Topological domaini403 – 42119Extracellular Reviewed predictionAdd
BLAST
Transmembranei422 – 44221Helical; Name=5; Reviewed predictionAdd
BLAST
Topological domaini443 – 46927Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei470 – 49021Helical; Name=6; Reviewed predictionAdd
BLAST
Topological domaini491 – 53242Extracellular Reviewed predictionAdd
BLAST
Transmembranei533 – 55321Helical; Name=7; Reviewed predictionAdd
BLAST
Topological domaini554 – 1036483Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cilium Source: RefGenome
  2. cytoplasm Source: RefGenome
  3. endosome Source: FlyBase
  4. integral component of membrane Source: FlyBase
  5. integral component of plasma membrane Source: FlyBase
  6. neuronal cell body Source: RefGenome
  7. plasma membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131 Reviewed predictionAdd
BLAST
Chaini32 – 10361005Protein smoothenedPRO_0000013019Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi90 ↔ 1551 Publication
Glycosylationi95 – 951N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi100 ↔ 1481 Publication
Disulfide bondi139 ↔ 1791 Publication
Disulfide bondi172 ↔ 1941 Publication
Glycosylationi184 – 1841N-linked (GlcNAc...) Reviewed prediction
Glycosylationi195 – 1951N-linked (GlcNAc...) Reviewed prediction
Glycosylationi213 – 2131N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi218 ↔ 238 By similarity
Disulfide bondi242 ↔ 320 By similarity
Glycosylationi336 – 3361N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi339 ↔ 413 By similarity
Glycosylationi419 – 4191N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi513 ↔ 525 By similarity
Modified residuei658 – 6581Phosphoserine1 Publication
Modified residuei659 – 6591Phosphoserine1 Publication
Modified residuei667 – 6671Phosphoserine1 Publication
Modified residuei670 – 6701Phosphoserine1 Publication
Modified residuei673 – 6731Phosphoserine1 Publication
Modified residuei687 – 6871Phosphoserine1 Publication
Modified residuei690 – 6901Phosphoserine1 Publication
Modified residuei693 – 6931Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiP91682.

Expressioni

Developmental stagei

Expressed at all developmental stages, though the levels vary.

Gene expression databases

BgeeiP91682.

Interactioni

Subunit structurei

Interacts with cos.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
cosO168445EBI-142245,EBI-102069

Protein-protein interaction databases

BioGridi59452. 17 interactions.
DIPiDIP-19956N.
IntActiP91682. 3 interactions.
MINTiMINT-811118.

Structurei

Secondary structure

1
1036
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi94 – 963
Beta strandi108 – 1103
Helixi112 – 1143
Helixi120 – 13112
Helixi132 – 1354
Helixi137 – 1404
Helixi146 – 1516
Beta strandi156 – 1605
Beta strandi162 – 1654
Helixi169 – 1768
Helixi180 – 1823
Helixi189 – 1924

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MAHNMR-A85-202[»]
ProteinModelPortaliP91682.
SMRiP91682. Positions 76-202.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 206122FZAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi816 – 8194Poly-Ser

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG312505.
GeneTreeiENSGT00750000117492.
InParanoidiP91682.
KOiK06226.
OMAiNANKYPA.
OrthoDBiEOG74J972.
PhylomeDBiP91682.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR017981. GPCR_2-like.
IPR026544. SMO.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF35. PTHR11309:SF35. 1 hit.
PfamiPF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
PRINTSiPR00489. FRIZZLED.
SMARTiSM00063. FRI. 1 hit.
[Graphical view]
SUPFAMiSSF63501. SSF63501. 1 hit.
PROSITEiPS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P91682-1 [UniParc]FASTAAdd to Basket

« Hide

MQYLNFPRMP NIMMFLEVAI LCLWVVADAS ASSAKFGSTT PASAQQSDVE     50
LEPINGTLNY RLYAKKGRDD KPWFDGLDSR HIQCVRRARC YPTSNATNTC 100
FGSKLPYELS SLDLTDFHTE KELNDKLNDY YALKHVPKCW AAIQPFLCAV 150
FKPKCEKING EDMVYLPSYE MCRITMEPCR ILYNTTFFPK FLRCNETLFP 200
TKCTNGARGM KFNGTGQCLS PLVPTDTSAS YYPGIEGCGV RCKDPLYTDD 250
EHRQIHKLIG WAGSICLLSN LFVVSTFFID WKNANKYPAV IVFYINLCFL 300
IACVGWLLQF TSGSREDIVC RKDGTLRHSE PTAGENLSCI VIFVLVYYFL 350
TAGMVWFVFL TYAWHWRAMG HVQDRIDKKG SYFHLVAWSL PLVLTITTMA 400
FSEVDGNSIV GICFVGYINH SMRAGLLLGP LCGVILIGGY FITRGMVMLF 450
GLKHFANDIK STSASNKIHL IIMRMGVCAL LTLVFILVAI ACHVTEFRHA 500
DEWAQSFRQF IICKISSVFE EKSSCRIENR PSVGVLQLHL LCLFSSGIVM 550
STWCWTPSSI ETWKRYIRKK CGKEVVEEVK MPKHKVIAQT WAKRKDFEDK 600
GRLSITLYNT HTDPVGLNFD VNDLNSSETN DISSTWAAYL PQCVKRRMAL 650
TGAATGNSSS HGPRKNSLDS EISVSVRHVS VESRRNSVDS QVSVKIAEMK 700
TKVASRSRGK HGGSSSNRRT QRRRDYIAAA TGKSSRRRES STSVESQVIA 750
LKKTTYPNAS HKVGVFAHHS SKKQHNYTSS MKRRTANAGL DPSILNEFLQ 800
KNGDFIFPFL QNQDMSSSSE EDNSRASQKI QDLNVVVKQQ EISEDDHDGI 850
KIEELPNSKQ VALENFLKNI KKSNESNSNR HSRNSARSQS KKSQKRHLKN 900
PAADLDFRKD CVKYRSNDSL SCSSEELDVA LDVGSLLNSS FSGISMGKPH 950
SRNSKTSCDV GIQANPFELV PSYGEDELQQ AMRLLNAASR QRTEAANEDF 1000
GGTELQGLLG HSHRHQREPT FMSESDKLKM LLLPSK 1036
Length:1,036
Mass (Da):116,552
Last modified:May 1, 1997 - v1
Checksum:i7797FC71A539A87A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U87613 Genomic DNA. Translation: AAC33180.1.
AF030334 Genomic DNA. Translation: AAB84275.1.
AE014134 Genomic DNA. Translation: AAF51518.2.
BT053691 mRNA. Translation: ACK77608.1.
PIRiS71804.
RefSeqiNP_523443.1. NM_078719.3.
UniGeneiDm.244.

Genome annotation databases

EnsemblMetazoaiFBtr0078129; FBpp0077788; FBgn0003444.
GeneIDi33196.
KEGGidme:Dmel_CG11561.
UCSCiCG11561-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U87613 Genomic DNA. Translation: AAC33180.1 .
AF030334 Genomic DNA. Translation: AAB84275.1 .
AE014134 Genomic DNA. Translation: AAF51518.2 .
BT053691 mRNA. Translation: ACK77608.1 .
PIRi S71804.
RefSeqi NP_523443.1. NM_078719.3.
UniGenei Dm.244.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2MAH NMR - A 85-202 [» ]
ProteinModelPortali P91682.
SMRi P91682. Positions 76-202.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 59452. 17 interactions.
DIPi DIP-19956N.
IntActi P91682. 3 interactions.
MINTi MINT-811118.

Protein family/group databases

GPCRDBi Search...

Proteomic databases

PRIDEi P91682.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0078129 ; FBpp0077788 ; FBgn0003444 .
GeneIDi 33196.
KEGGi dme:Dmel_CG11561.
UCSCi CG11561-RA. d. melanogaster.

Organism-specific databases

CTDi 6608.
FlyBasei FBgn0003444. smo.

Phylogenomic databases

eggNOGi NOG312505.
GeneTreei ENSGT00750000117492.
InParanoidi P91682.
KOi K06226.
OMAi NANKYPA.
OrthoDBi EOG74J972.
PhylomeDBi P91682.

Enzyme and pathway databases

SignaLinki P91682.

Miscellaneous databases

GenomeRNAii 33196.
NextBioi 782367.
PROi P91682.

Gene expression databases

Bgeei P91682.

Family and domain databases

Gene3Di 1.10.2000.10. 1 hit.
InterProi IPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR017981. GPCR_2-like.
IPR026544. SMO.
[Graphical view ]
PANTHERi PTHR11309. PTHR11309. 1 hit.
PTHR11309:SF35. PTHR11309:SF35. 1 hit.
Pfami PF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view ]
PRINTSi PR00489. FRIZZLED.
SMARTi SM00063. FRI. 1 hit.
[Graphical view ]
SUPFAMi SSF63501. SSF63501. 1 hit.
PROSITEi PS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSMO_DROME
AccessioniPrimary (citable) accession number: P91682
Secondary accession number(s): B7FNK1, Q9VPM8
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi