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P18502 (PTC_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Protein patched
Alternative name(s):
Hedgehog receptor
Gene names
Name:ptc
ORF Names:CG2411
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1286 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Segmentation polarity protein. Acts as a receptor for the hedgehog protein (HH). Associates with the smoothened protein (SMO) to transduce the hedgehog signal leading to the activation of wingless, decapentaplegic and patched itself. Participates in cell interactions that establish pattern within the segment and the imaginal disks during development. In the absence of HH, represses the constitutive signaling activity of smo through fused (FU).

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the patched family.

Contains 1 SSD (sterol-sensing) domain.

Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Receptor
Segmentation polarity protein
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBolwig's organ morphogenesis

Inferred from mutant phenotype PubMed 10704398. Source: FlyBase

anterior/posterior lineage restriction, imaginal disc

Traceable author statement PubMed 10625531. Source: FlyBase

anterior/posterior pattern specification

Non-traceable author statement PubMed 11932020. Source: FlyBase

axon guidance

Inferred from mutant phenotype PubMed 15754211. Source: FlyBase

dephosphorylation

Traceable author statement PubMed 11932020. Source: FlyBase

determination of genital disc primordium

Inferred from mutant phenotype PubMed 15893978. Source: FlyBase

embryonic pattern specification

Traceable author statement PubMed 11102367. Source: FlyBase

eye-antennal disc morphogenesis

Inferred from mutant phenotype PubMed 11934850. Source: FlyBase

germ-line stem cell division

Traceable author statement PubMed 12459723. Source: FlyBase

gonad development

Inferred from mutant phenotype PubMed 21377458. Source: FlyBase

imaginal disc-derived wing morphogenesis

Inferred from mutant phenotype PubMed 16648592. Source: FlyBase

lipid homeostasis

Inferred from mutant phenotype PubMed 18198278. Source: FlyBase

negative regulation of smoothened signaling pathway

Inferred from genetic interaction PubMed 9874371. Source: FlyBase

oogenesis

Inferred from mutant phenotype PubMed 8898240. Source: FlyBase

ovarian follicle cell development

Traceable author statement PubMed 10822261. Source: FlyBase

peripheral nervous system development

Traceable author statement PubMed 11102367. Source: FlyBase

proteolysis

Traceable author statement PubMed 11932020. Source: FlyBase

receptor-mediated endocytosis

Inferred from direct assay PubMed 18198278. Source: GOC

regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 11279500. Source: FlyBase

regulation of protein import into nucleus

Inferred from mutant phenotype PubMed 14597576. Source: FlyBase

segment polarity determination

Inferred from electronic annotation. Source: UniProtKB-KW

smoothened signaling pathway

Inferred from mutant phenotype PubMed 14597576PubMed 8898207. Source: FlyBase

somatic stem cell division

Traceable author statement PubMed 12459723. Source: FlyBase

wing disc anterior/posterior pattern formation

Traceable author statement PubMed 11253649. Source: FlyBase

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 8898240. Source: FlyBase

endocytic vesicle

Inferred from direct assay PubMed 18198278. Source: FlyBase

integral component of membrane

Traceable author statement PubMed 11102367. Source: FlyBase

integral component of plasma membrane

Inferred from direct assay PubMed 10966113. Source: FlyBase

perinuclear region of cytoplasm

Inferred from direct assay PubMed 8898240. Source: FlyBase

plasma membrane

Inferred from direct assay PubMed 8898240. Source: FlyBase

   Molecular_functionhedgehog receptor activity

Inferred from mutant phenotype PubMed 8898207. Source: FlyBase

lipoprotein particle receptor activity

Inferred from direct assay PubMed 18198278. Source: FlyBase

transmembrane signaling receptor activity

Non-traceable author statement PubMed 11253649. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12861286Protein patched
PRO_0000205973

Regions

Topological domain1 – 7676Cytoplasmic Potential
Transmembrane77 – 9216Helical; Potential
Topological domain93 – 427335Extracellular Potential
Transmembrane428 – 44821Helical; Potential
Topological domain449 – 46517Cytoplasmic Potential
Transmembrane466 – 48621Helical; Potential
Topological domain487 – 4926Extracellular Potential
Transmembrane493 – 51119Helical; Potential
Topological domain512 – 53221Cytoplasmic Potential
Transmembrane533 – 55321Helical; Potential
Topological domain554 – 5629Extracellular Potential
Transmembrane563 – 58321Helical; Potential
Topological domain584 – 67794Cytoplasmic Potential
Transmembrane678 – 69922Helical; Potential
Topological domain700 – 931232Extracellular Potential
Transmembrane932 – 95221Helical; Potential
Topological domain953 – 9553Cytoplasmic Potential
Transmembrane956 – 97621Helical; Potential
Topological domain977 – 100731Extracellular Potential
Transmembrane1008 – 102821Helical; Potential
Topological domain1029 – 105628Cytoplasmic Potential
Transmembrane1057 – 107721Helical; Potential
Topological domain1078 – 10825Extracellular Potential
Transmembrane1083 – 110321Helical; Potential
Topological domain1104 – 1286183Cytoplasmic Potential
Domain428 – 583156SSD
Compositional bias1227 – 12326Poly-Pro

Amino acid modifications

Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation3881N-linked (GlcNAc...) Potential
Glycosylation8071N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1111R → G in CAA35591. Ref.2
Sequence conflict2741G → A in CAA35591. Ref.2
Sequence conflict3321A → R in AAA28696. Ref.1
Sequence conflict6361P → A in CAA35591. Ref.2
Sequence conflict862 – 8643DVF → ASSPTELLRANCIRNR Ref.2
Sequence conflict8661Y → N Ref.2

Sequences

Sequence LengthMass (Da)Tools
P18502 [UniParc].

Last modified November 2, 2001. Version 2.
Checksum: 5F22A956F8BE0EC6

FASTA1,286142,831
        10         20         30         40         50         60 
MDRDSLPRVP DTHGDVVDEK LFSDLYIRTS WVDAQVALDQ IDKGKARGSR TAIYLRSVFQ 

        70         80         90        100        110        120 
SHLETLGSSV QKHAGKVLFV AILVLSTFCV GLKSAQIHSK VHQLWIQEGG RLEAELAYTQ 

       130        140        150        160        170        180 
KTIGEDESAT HQLLIQTTHD PNASVLHPQA LLAHLEVLVK ATAVKVHLYD TEWGLRDMCN 

       190        200        210        220        230        240 
MPSTPSFEGI YYIEQILRHL IPCSIITPLD CFWEGSQLLG PESAVVIPGL NQRLLWTTLN 

       250        260        270        280        290        300 
PASVMQYMKQ KMSEEKISFD FETVEQYMKR AAIGSGYMEK PCLNPLNPNC PDTAPNKNST 

       310        320        330        340        350        360 
QPPDVGAILS GGCYGYAAKH MHWPEELIVG GAKRNRSGHL RKAQALQSVV QLMTEKEMYD 

       370        380        390        400        410        420 
QWQDNYKVHH LGWTQEKAAE VLNAWQRNFS REVEQLLRKQ SRIATNYDIY VFSSAALDDI 

       430        440        450        460        470        480 
LAKFSHPSAL SIVIGVAVTV LYAFCTLLRW RDPVRGQSSV GVAGVLLMCF STAAGLGLSA 

       490        500        510        520        530        540 
LLGIVFNAAS TQVVPFLALG LGVDHIFMLT AAYAESNRRE QTKLILKKVG PSILFSACST 

       550        560        570        580        590        600 
AGSFFAAAFI PVPALKVFCL QAAIVMCSNL AAALLVFPAM ISLDLRRRTA GRADIFCCCF 

       610        620        630        640        650        660 
PVWKEQPKVA PPVLPLNNNN GRGARHPKSC NNNRVPLPAQ NPLLEQRADI PGSSHSLASF 

       670        680        690        700        710        720 
SLATFAFQHY TPFLMRSWVK FLTVMGFLAA LISSLYASTR LQDGLDIIDL VPKDSNEHKF 

       730        740        750        760        770        780 
LDAQTRLFGF YSMYAVTQGN FEYPTQQQLL RDYHDSFVRV PHVIKNDNGG LPDFWLLLFS 

       790        800        810        820        830        840 
EWLGNLQKIF DEEYRDGRLT KECWFPNASS DAILAYKLIV QTGHVDNPVD KELVLTNRLV 

       850        860        870        880        890        900 
NSDGIINQRA FYNYLSAWAT NDVFAYGASQ GKLYPEPRQY FHQPNEYDLK IPKSLPLVYA 

       910        920        930        940        950        960 
QMPFYLHGLT DTSQIKTLIG HIRDLSVKYE GFGLPNYPSG IPFIFWEQYM TLRSSLAMIL 

       970        980        990       1000       1010       1020 
ACVLLAALVL VSLLLLSVWA AVLVILSVLA SLAQIFGAMT LLGIKLSAIP AVILILSVGM 

      1030       1040       1050       1060       1070       1080 
MLCFNVLISL GFMTSVGNRQ RRVQLSMQMS LGPLVHGMLT SGVAVFMLST SPFEFVIRHF 

      1090       1100       1110       1120       1130       1140 
CWLLLVVLCV GACNSLLVFP ILLSMVGPEA ELVPLEHPDR ISTPSPLPVR SSKRSGKSYV 

      1150       1160       1170       1180       1190       1200 
VQGSRSSRGS CQKSHHHHHK DLNDPSLTTI TEEPQSWKSS NSSIQMPNDW TYQPREQRPA 

      1210       1220       1230       1240       1250       1260 
SYAAPPPAYH KAAAQQHHQH QGPPTTPPPP FPTAYPPELQ SIVVQPEVTV ETTHSDSNTT 

      1270       1280 
KVTATANIKV ELAMPGRAVR SYNFTS 

« Hide

References

« Hide 'large scale' references
[1]"The Drosophila patched gene encodes a putative membrane protein required for segmental patterning."
Hooper J.E., Scott M.P.
Cell 59:751-765(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A protein with several possible membrane-spanning domains encoded by the Drosophila segment polarity gene patched."
Nakano Y., Guerrero I., Hidalgo A., Taylor A., Whittle J.R.S., Ingham P.W.
Nature 341:508-513(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28999, M28418 Genomic DNA. Translation: AAA28696.1.
X17558 mRNA. Translation: CAA35591.1.
AE013599 Genomic DNA. Translation: AAF59062.1.
PIRS06119.
RefSeqNP_523661.2. NM_078937.3.
UniGeneDm.2630.

3D structure databases

ProteinModelPortalP18502.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid61701. 130 interactions.
DIPDIP-634N.

Protein family/group databases

TCDB2.A.6.6.2. the resistance-nodulation-cell division (rnd) superfamily.

Proteomic databases

PaxDbP18502.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0089427; FBpp0088443; FBgn0003892.
GeneID35851.
KEGGdme:Dmel_CG2411.
UCSCCG2411-RA. d. melanogaster.

Organism-specific databases

CTD35851.
FlyBaseFBgn0003892. ptc.

Phylogenomic databases

eggNOGNOG313603.
GeneTreeENSGT00680000099777.
HOGENOMHOG000228313.
InParanoidP18502.
KOK06225.
OMAPDRDYLH.
OrthoDBEOG7HMS06.
PhylomeDBP18502.

Enzyme and pathway databases

SignaLinkP18502.

Gene expression databases

BgeeP18502.

Family and domain databases

InterProIPR003392. Patched.
IPR000731. SSD.
IPR004766. TM_rcpt_patched.
[Graphical view]
PfamPF02460. Patched. 2 hits.
[Graphical view]
TIGRFAMsTIGR00918. 2A060602. 1 hit.
PROSITEPS50156. SSD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi35851.
NextBio795513.
PROP18502.

Entry information

Entry namePTC_DROME
AccessionPrimary (citable) accession number: P18502
Secondary accession number(s): Q9V4W3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 2, 2001
Last modified: April 16, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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