Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein smoothened

Gene

smo

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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

  • G-protein coupled receptor activity Source: FlyBase
  • patched binding Source: GO_Central
  • transmembrane signaling receptor activity Source: FlyBase
  • Wnt-protein binding Source: GO_Central

GO - Biological processi

  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: FlyBase
  • anterior/posterior lineage restriction, imaginal disc Source: FlyBase
  • blastoderm segmentation Source: FlyBase
  • Bolwig's organ morphogenesis Source: FlyBase
  • eye-antennal disc morphogenesis Source: FlyBase
  • eye morphogenesis Source: FlyBase
  • mucosal immune response Source: FlyBase
  • negative regulation of G1/S transition of mitotic cell cycle Source: FlyBase
  • negative regulation of Notch signaling pathway Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • positive regulation of establishment of protein localization to plasma membrane Source: FlyBase
  • regulation of apoptotic process Source: FlyBase
  • regulation of mitotic cell cycle Source: FlyBase
  • signal transduction Source: FlyBase
  • smoothened signaling pathway Source: FlyBase
  • somatic stem cell population maintenance Source: FlyBase
  • wing disc anterior/posterior pattern formation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

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

Enzyme and pathway databases

ReactomeiR-DME-5610787. Hedgehog 'off' state.
R-DME-5635838. Activation of SMO.
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
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0003444. smo.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini32 – 258ExtracellularSequence analysisAdd BLAST227
Transmembranei259 – 279Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini280 – 287CytoplasmicSequence analysis8
Transmembranei288 – 308Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini309 – 339ExtracellularSequence analysisAdd BLAST31
Transmembranei340 – 360Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini361 – 381CytoplasmicSequence analysisAdd BLAST21
Transmembranei382 – 402Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini403 – 421ExtracellularSequence analysisAdd BLAST19
Transmembranei422 – 442Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini443 – 469CytoplasmicSequence analysisAdd BLAST27
Transmembranei470 – 490Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini491 – 532ExtracellularSequence analysisAdd BLAST42
Transmembranei533 – 553Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini554 – 1036CytoplasmicSequence analysisAdd BLAST483

GO - Cellular componenti

  • cilium Source: FlyBase
  • dendrite Source: FlyBase
  • endosome Source: FlyBase
  • integral component of membrane Source: FlyBase
  • integral component of plasma membrane Source: FlyBase
  • neuronal cell body Source: FlyBase
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_000001301932 – 1036Protein smoothenedAdd BLAST1005

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi55N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi90 ↔ 155PROSITE-ProRule annotation1 Publication
Glycosylationi95N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi100 ↔ 148PROSITE-ProRule annotation1 Publication
Disulfide bondi139 ↔ 179PROSITE-ProRule annotation1 Publication
Disulfide bondi172 ↔ 194PROSITE-ProRule annotation1 Publication
Glycosylationi184N-linked (GlcNAc...)Sequence analysis1
Glycosylationi195N-linked (GlcNAc...)Sequence analysis1
Glycosylationi213N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi218 ↔ 238PROSITE-ProRule annotation
Disulfide bondi242 ↔ 320PROSITE-ProRule annotation
Glycosylationi336N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi339 ↔ 413PROSITE-ProRule annotation
Glycosylationi419N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi513 ↔ 525PROSITE-ProRule annotation
Modified residuei658Phosphoserine1 Publication1
Modified residuei659Phosphoserine1 Publication1
Modified residuei667Phosphoserine1 Publication1
Modified residuei670Phosphoserine1 Publication1
Modified residuei673Phosphoserine1 Publication1
Modified residuei687Phosphoserine1 Publication1
Modified residuei690Phosphoserine1 Publication1
Modified residuei693Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylation by CkIalpha and PKA regulates smo accumulation at the cell surface and its signaling activity in response to hh.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP91682.
PRIDEiP91682.

PTM databases

iPTMnetiP91682.

Expressioni

Developmental stagei

Expressed at all developmental stages, though the levels vary.

Gene expression databases

BgeeiFBgn0003444.
GenevisibleiP91682. DM.

Interactioni

Subunit structurei

Interacts with cos.1 Publication

Binary interactionsi

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi59452. 17 interactors.
DIPiDIP-19956N.
IntActiP91682. 4 interactors.
MINTiMINT-811118.
STRINGi7227.FBpp0077788.

Structurei

Secondary structure

11036
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi94 – 96Combined sources3
Beta strandi108 – 110Combined sources3
Helixi112 – 114Combined sources3
Helixi120 – 131Combined sources12
Helixi132 – 135Combined sources4
Helixi137 – 140Combined sources4
Helixi146 – 151Combined sources6
Beta strandi156 – 160Combined sources5
Beta strandi162 – 165Combined sources4
Helixi169 – 176Combined sources8
Helixi180 – 182Combined sources3
Helixi189 – 192Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MAHNMR-A85-202[»]
ProteinModelPortaliP91682.
SMRiP91682.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini85 – 206FZPROSITE-ProRule annotationAdd BLAST122

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi816 – 819Poly-Ser4

Sequence similaritiesi

Contains 1 FZ (frizzled) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3577. Eukaryota.
ENOG410XRC8. LUCA.
GeneTreeiENSGT00760000118864.
InParanoidiP91682.
KOiK06226.
OMAiCKDPLYT.
OrthoDBiEOG091G04OK.
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.
SM01330. Frizzled. 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

        10         20         30         40         50
MQYLNFPRMP NIMMFLEVAI LCLWVVADAS ASSAKFGSTT PASAQQSDVE
60 70 80 90 100
LEPINGTLNY RLYAKKGRDD KPWFDGLDSR HIQCVRRARC YPTSNATNTC
110 120 130 140 150
FGSKLPYELS SLDLTDFHTE KELNDKLNDY YALKHVPKCW AAIQPFLCAV
160 170 180 190 200
FKPKCEKING EDMVYLPSYE MCRITMEPCR ILYNTTFFPK FLRCNETLFP
210 220 230 240 250
TKCTNGARGM KFNGTGQCLS PLVPTDTSAS YYPGIEGCGV RCKDPLYTDD
260 270 280 290 300
EHRQIHKLIG WAGSICLLSN LFVVSTFFID WKNANKYPAV IVFYINLCFL
310 320 330 340 350
IACVGWLLQF TSGSREDIVC RKDGTLRHSE PTAGENLSCI VIFVLVYYFL
360 370 380 390 400
TAGMVWFVFL TYAWHWRAMG HVQDRIDKKG SYFHLVAWSL PLVLTITTMA
410 420 430 440 450
FSEVDGNSIV GICFVGYINH SMRAGLLLGP LCGVILIGGY FITRGMVMLF
460 470 480 490 500
GLKHFANDIK STSASNKIHL IIMRMGVCAL LTLVFILVAI ACHVTEFRHA
510 520 530 540 550
DEWAQSFRQF IICKISSVFE EKSSCRIENR PSVGVLQLHL LCLFSSGIVM
560 570 580 590 600
STWCWTPSSI ETWKRYIRKK CGKEVVEEVK MPKHKVIAQT WAKRKDFEDK
610 620 630 640 650
GRLSITLYNT HTDPVGLNFD VNDLNSSETN DISSTWAAYL PQCVKRRMAL
660 670 680 690 700
TGAATGNSSS HGPRKNSLDS EISVSVRHVS VESRRNSVDS QVSVKIAEMK
710 720 730 740 750
TKVASRSRGK HGGSSSNRRT QRRRDYIAAA TGKSSRRRES STSVESQVIA
760 770 780 790 800
LKKTTYPNAS HKVGVFAHHS SKKQHNYTSS MKRRTANAGL DPSILNEFLQ
810 820 830 840 850
KNGDFIFPFL QNQDMSSSSE EDNSRASQKI QDLNVVVKQQ EISEDDHDGI
860 870 880 890 900
KIEELPNSKQ VALENFLKNI KKSNESNSNR HSRNSARSQS KKSQKRHLKN
910 920 930 940 950
PAADLDFRKD CVKYRSNDSL SCSSEELDVA LDVGSLLNSS FSGISMGKPH
960 970 980 990 1000
SRNSKTSCDV GIQANPFELV PSYGEDELQQ AMRLLNAASR QRTEAANEDF
1010 1020 1030
GGTELQGLLG HSHRHQREPT FMSESDKLKM LLLPSK
Length:1,036
Mass (Da):116,552
Last modified:May 1, 1997 - v1
Checksum:i7797FC71A539A87A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_078719.4.
UniGeneiDm.244.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_078719.4.
UniGeneiDm.244.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MAHNMR-A85-202[»]
ProteinModelPortaliP91682.
SMRiP91682.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59452. 17 interactors.
DIPiDIP-19956N.
IntActiP91682. 4 interactors.
MINTiMINT-811118.
STRINGi7227.FBpp0077788.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiP91682.

Proteomic databases

PaxDbiP91682.
PRIDEiP91682.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6608.
FlyBaseiFBgn0003444. smo.

Phylogenomic databases

eggNOGiKOG3577. Eukaryota.
ENOG410XRC8. LUCA.
GeneTreeiENSGT00760000118864.
InParanoidiP91682.
KOiK06226.
OMAiCKDPLYT.
OrthoDBiEOG091G04OK.
PhylomeDBiP91682.

Enzyme and pathway databases

ReactomeiR-DME-5610787. Hedgehog 'off' state.
R-DME-5635838. Activation of SMO.
SignaLinkiP91682.

Miscellaneous databases

GenomeRNAii33196.
PROiP91682.

Gene expression databases

BgeeiFBgn0003444.
GenevisibleiP91682. DM.

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.
SM01330. Frizzled. 1 hit.
[Graphical view]
SUPFAMiSSF63501. SSF63501. 1 hit.
PROSITEiPS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 148 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.Curated

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

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 one 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.