PTC_DROME
ID PTC_DROME Reviewed; 1286 AA.
AC P18502; Q9V4W3;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Protein patched;
DE AltName: Full=Hedgehog receptor;
GN Name=ptc; ORFNames=CG2411;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2582494; DOI=10.1016/0092-8674(89)90021-4;
RA Hooper J.E., Scott M.P.;
RT "The Drosophila patched gene encodes a putative membrane protein required
RT for segmental patterning.";
RL Cell 59:751-765(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2797178; DOI=10.1038/341508a0;
RA Nakano Y., Guerrero I., Hidalgo A., Taylor A., Whittle J.R.S., Ingham P.W.;
RT "A protein with several possible membrane-spanning domains encoded by the
RT Drosophila segment polarity gene patched.";
RL Nature 341:508-513(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
CC -!- FUNCTION: Segmentation polarity protein. Acts as a receptor for the
CC hedgehog protein (HH). Associates with the smoothened protein (SMO) to
CC transduce the hedgehog signal leading to the activation of wingless,
CC decapentaplegic and patched itself. Participates in cell interactions
CC that establish pattern within the segment and the imaginal disks during
CC development. In the absence of HH, represses the constitutive signaling
CC activity of smo through fused (FU).
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the patched family. {ECO:0000305}.
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DR EMBL; M28999; AAA28696.1; -; Genomic_DNA.
DR EMBL; M28418; AAA28696.1; JOINED; Genomic_DNA.
DR EMBL; X17558; CAA35591.1; -; mRNA.
DR EMBL; AE013599; AAF59062.1; -; Genomic_DNA.
DR PIR; S06119; S06119.
DR RefSeq; NP_523661.2; NM_078937.4.
DR AlphaFoldDB; P18502; -.
DR SMR; P18502; -.
DR BioGRID; 61701; 156.
DR DIP; DIP-634N; -.
DR IntAct; P18502; 2.
DR STRING; 7227.FBpp0088443; -.
DR TCDB; 2.A.6.6.2; the resistance-nodulation-cell division (rnd) superfamily.
DR GlyGen; P18502; 5 sites.
DR PaxDb; P18502; -.
DR PRIDE; P18502; -.
DR EnsemblMetazoa; FBtr0089427; FBpp0088443; FBgn0003892.
DR GeneID; 35851; -.
DR KEGG; dme:Dmel_CG2411; -.
DR UCSC; CG2411-RA; d. melanogaster.
DR CTD; 35851; -.
DR FlyBase; FBgn0003892; ptc.
DR VEuPathDB; VectorBase:FBgn0003892; -.
DR eggNOG; KOG1935; Eukaryota.
DR GeneTree; ENSGT00940000167988; -.
DR HOGENOM; CLU_002506_1_0_1; -.
DR InParanoid; P18502; -.
DR OMA; LTKECWF; -.
DR OrthoDB; 1190129at2759; -.
DR PhylomeDB; P18502; -.
DR Reactome; R-DME-209338; Assembly of the 'signalling complexes'.
DR Reactome; R-DME-5610787; Hedgehog 'off' state.
DR Reactome; R-DME-5632684; Hedgehog 'on' state.
DR SignaLink; P18502; -.
DR BioGRID-ORCS; 35851; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35851; -.
DR PRO; PR:P18502; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003892; Expressed in wing disc and 16 other tissues.
DR ExpressionAtlas; P18502; baseline and differential.
DR Genevisible; P18502; DM.
DR GO; GO:0009925; C:basal plasma membrane; IDA:FlyBase.
DR GO; GO:0005929; C:cilium; IDA:FlyBase.
DR GO; GO:0030139; C:endocytic vesicle; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0097108; F:hedgehog family protein binding; IDA:FlyBase.
DR GO; GO:0008158; F:hedgehog receptor activity; IMP:FlyBase.
DR GO; GO:0030228; F:lipoprotein particle receptor activity; IDA:FlyBase.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:FlyBase.
DR GO; GO:0005119; F:smoothened binding; IBA:GO_Central.
DR GO; GO:0048099; P:anterior/posterior lineage restriction, imaginal disc; TAS:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0001746; P:Bolwig's organ morphogenesis; IMP:FlyBase.
DR GO; GO:0035225; P:determination of genital disc primordium; IMP:FlyBase.
DR GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:FlyBase.
DR GO; GO:0008406; P:gonad development; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0055088; P:lipid homeostasis; IMP:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IDA:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0042981; P:regulation of apoptotic process; IGI:FlyBase.
DR GO; GO:2000274; P:regulation of epithelial cell migration, open tracheal system; IMP:FlyBase.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007367; P:segment polarity determination; IEA:UniProtKB-KW.
DR GO; GO:0007224; P:smoothened signaling pathway; IBA:GO_Central.
DR GO; GO:0048100; P:wing disc anterior/posterior pattern formation; TAS:FlyBase.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR InterPro; IPR004766; TM_rcpt_patched.
DR Pfam; PF02460; Patched; 2.
DR TIGRFAMs; TIGR00918; 2A060602; 1.
DR PROSITE; PS50156; SSD; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Segmentation polarity protein; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1286
FT /note="Protein patched"
FT /id="PRO_0000205973"
FT TOPO_DOM 1..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..427
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..492
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..562
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 584..677
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 678..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 700..931
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 932..952
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 953..955
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 956..976
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 977..1007
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1008..1028
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1029..1056
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1057..1077
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1078..1082
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1083..1103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1104..1286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 428..583
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT REGION 1116..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1236
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 111
FT /note="R -> G (in Ref. 2; CAA35591)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="G -> A (in Ref. 2; CAA35591)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="A -> R (in Ref. 1; AAA28696)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="P -> A (in Ref. 2; CAA35591)"
FT /evidence="ECO:0000305"
FT CONFLICT 862..864
FT /note="DVF -> ASSPTELLRANCIRNR (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 866
FT /note="Y -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1286 AA; 142831 MW; 5F22A956F8BE0EC6 CRC64;
MDRDSLPRVP DTHGDVVDEK LFSDLYIRTS WVDAQVALDQ IDKGKARGSR TAIYLRSVFQ
SHLETLGSSV QKHAGKVLFV AILVLSTFCV GLKSAQIHSK VHQLWIQEGG RLEAELAYTQ
KTIGEDESAT HQLLIQTTHD PNASVLHPQA LLAHLEVLVK ATAVKVHLYD TEWGLRDMCN
MPSTPSFEGI YYIEQILRHL IPCSIITPLD CFWEGSQLLG PESAVVIPGL NQRLLWTTLN
PASVMQYMKQ KMSEEKISFD FETVEQYMKR AAIGSGYMEK PCLNPLNPNC PDTAPNKNST
QPPDVGAILS GGCYGYAAKH MHWPEELIVG GAKRNRSGHL RKAQALQSVV QLMTEKEMYD
QWQDNYKVHH LGWTQEKAAE VLNAWQRNFS REVEQLLRKQ SRIATNYDIY VFSSAALDDI
LAKFSHPSAL SIVIGVAVTV LYAFCTLLRW RDPVRGQSSV GVAGVLLMCF STAAGLGLSA
LLGIVFNAAS TQVVPFLALG LGVDHIFMLT AAYAESNRRE QTKLILKKVG PSILFSACST
AGSFFAAAFI PVPALKVFCL QAAIVMCSNL AAALLVFPAM ISLDLRRRTA GRADIFCCCF
PVWKEQPKVA PPVLPLNNNN GRGARHPKSC NNNRVPLPAQ NPLLEQRADI PGSSHSLASF
SLATFAFQHY TPFLMRSWVK FLTVMGFLAA LISSLYASTR LQDGLDIIDL VPKDSNEHKF
LDAQTRLFGF YSMYAVTQGN FEYPTQQQLL RDYHDSFVRV PHVIKNDNGG LPDFWLLLFS
EWLGNLQKIF DEEYRDGRLT KECWFPNASS DAILAYKLIV QTGHVDNPVD KELVLTNRLV
NSDGIINQRA FYNYLSAWAT NDVFAYGASQ GKLYPEPRQY FHQPNEYDLK IPKSLPLVYA
QMPFYLHGLT DTSQIKTLIG HIRDLSVKYE GFGLPNYPSG IPFIFWEQYM TLRSSLAMIL
ACVLLAALVL VSLLLLSVWA AVLVILSVLA SLAQIFGAMT LLGIKLSAIP AVILILSVGM
MLCFNVLISL GFMTSVGNRQ RRVQLSMQMS LGPLVHGMLT SGVAVFMLST SPFEFVIRHF
CWLLLVVLCV GACNSLLVFP ILLSMVGPEA ELVPLEHPDR ISTPSPLPVR SSKRSGKSYV
VQGSRSSRGS CQKSHHHHHK DLNDPSLTTI TEEPQSWKSS NSSIQMPNDW TYQPREQRPA
SYAAPPPAYH KAAAQQHHQH QGPPTTPPPP FPTAYPPELQ SIVVQPEVTV ETTHSDSNTT
KVTATANIKV ELAMPGRAVR SYNFTS
