PTC1_CHICK
ID PTC1_CHICK Reviewed; 1442 AA.
AC Q90693;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protein patched homolog 1;
DE Short=PTC;
DE Short=PTC1;
GN Name=PTCH1; Synonyms=PTC, PTCH;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Limb bud;
RX PubMed=8620849; DOI=10.1242/dev.122.4.1225;
RA Marigo V., Scott M.P., Johnson R.L., Goodrich L.V., Tabin C.J.;
RT "Conservation in hedgehog signaling: induction of a chicken patched homolog
RT by Sonic hedgehog in the developing limb.";
RL Development 122:1225-1233(1996).
RN [2]
RP CHARACTERIZATION.
RX PubMed=8906794; DOI=10.1038/384176a0;
RA Marigo V., Davey R.A., Zuo Y., Cunningham J.M., Tabin C.J.;
RT "Biochemical evidence that patched is the Hedgehog receptor.";
RL Nature 384:176-179(1996).
CC -!- FUNCTION: Acts as a receptor for sonic hedgehog (SHH), indian hedgehog
CC (IHH) and desert hedgehog (DHH). Associates with the smoothened protein
CC (SMO) to transduce the hedgehog's proteins signal.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expression is seen in the embryonic neural tube,
CC sclerotome, visceral mesoderm, and limb bud.
CC -!- DEVELOPMENTAL STAGE: In stage 10 embryo, expression is seen in neural
CC tube, and at lower levels in the notochord, epithelial somites,
CC endoderm and splanchnic mesoderm. At stage 18, PTC is broadly expressed
CC in the neural tube but excluded from the cells of the floor plate. At
CC stage 32, expression occurs in the mesodermal cells of the
CC gastrointestinal tract.
CC -!- INDUCTION: Activated by hedgehog; repressed by itself. {ECO:0000305}.
CC -!- PTM: Glycosylation is necessary for SHH binding.
CC -!- SIMILARITY: Belongs to the patched family. {ECO:0000305}.
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DR EMBL; U40074; AAC59898.1; -; mRNA.
DR PIR; T18538; T18538.
DR AlphaFoldDB; Q90693; -.
DR SMR; Q90693; -.
DR DIP; DIP-61762N; -.
DR IntAct; Q90693; 1.
DR STRING; 9031.ENSGALP00000020572; -.
DR PaxDb; Q90693; -.
DR VEuPathDB; HostDB:geneid_395806; -.
DR eggNOG; KOG1935; Eukaryota.
DR InParanoid; Q90693; -.
DR OrthoDB; 1190129at2759; -.
DR PhylomeDB; Q90693; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:Roslin.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0097108; F:hedgehog family protein binding; IBA:GO_Central.
DR GO; GO:0008158; F:hedgehog receptor activity; IBA:GO_Central.
DR GO; GO:0005119; F:smoothened binding; IBA:GO_Central.
DR GO; GO:0007224; P:smoothened signaling pathway; IBA:GO_Central.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR InterPro; IPR004766; TM_rcpt_patched.
DR Pfam; PF02460; Patched; 1.
DR Pfam; PF12349; Sterol-sensing; 1.
DR TIGRFAMs; TIGR00918; 2A060602; 1.
DR PROSITE; PS50156; SSD; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1442
FT /note="Protein patched homolog 1"
FT /id="PRO_0000205966"
FT TOPO_DOM 1..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..436
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..501
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 523..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..577
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..747
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 748..768
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 769..1026
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1027..1047
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1048..1053
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1054..1074
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1075..1082
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1083..1101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1102..1120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1121..1141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1142..1153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1154..1174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1175..1442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 438..598
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1206
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 999
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1442 AA; 160578 MW; 973E5F17FB8B6E43 CRC64;
MASAADALEP ESGSSTAGGG SHPVRAARSA RGRRRRSGGT RRAAAPDREY LQRPSYCDAA
FALEQIAKGR ATGRRAPLWL RAKFQRLLFN LGCYIQKNCG KFLVVGLLYS AFAVGLRAAN
LETNVEELWV EVGGRVSREL NYTRQKIGEE AMFNPQLMIQ TPQEDGTNVL TTEALRQHLD
SALQASRVHV YMYNRQWKLE HLCYKSGELI TEAGYMDQII EYLYPCLIIT PLDCFWEGAK
LQSGTAYLLG KPPLQWINFD PLEFLEELKK INYQVESWEE MLNKAEVGHG YMDRPCLNPA
DPDCPITAPN KNSTKPLDVA LVLSGGCYGL SRKYMHWQEE LIIGGTVKNS SGKLVSAQAL
QTMFQLMTPK QMYEHFKGYE YVSHINWNED KAAAILEAWQ RMYVEVVHQS VAQNSTQKVL
SFTTTTLDDI LKSFSDVSVI RVASGYLLML AYACLTMLRW DCAKSQGAVG LAGVLLVALS
VAAGLGLCSL IGISFNAATT QVLPFLALGV GVDDVFLLAH AFSETGQNKR IPFEDRTGEC
LKRTGASVAL TSISNVTAFF MAALIPIPAL RAFSLQAAVV VVFNFAMVLL IFPAILSMDL
YRREDRRLDI FCCFTSPCVT RVIQIEPQAY AENDNICYSS PPPYSSHSFA HETQITMQST
VQLRTEYDPH TQAYYTTAEP RSEISVQPVT VTQDSLSCQS PESASSTRDL LSQFSDSSVH
CLEPPCTKWT LSTFAEKHYA PFLLKPKAKV VVIFLFLGLL GLSLYGTTRV RDGLDLTDIV
PRDTREYDFI AAQFKYFSFY NMYIVTQKAD YPNVQHLLYE LHRSFSNVTY VLLEGDRQLP
KMWLHYFRDW LQGLQDAFDS DWETGKITYS NYKNGSDDAV LAYKLLVQTG NRAKPIDISQ
LTKQRLVDAD GIINPNAFYI YLTAWVSNDP VAYAASQANI RPHRPEWVHD KADYMPETRL
RIPAAEPIEY AQFPFYLNGL RETSDFVEAI EKVRAICNNY TSLGIASYPN GYPFLFWEQY
IGLRHWLLLS ISVVLACTFL VCALFLLNPW TAGIIVVVLA LMTVELFGMM GLIGIKLSAV
PVVILIASVG IGVEFTVHIA LAFLTAIGDK NRRAVLALEH MFAPVLDGAV STLLGVLMLA
GSEFDFIVRY FFAVLAILTI LGVLNGLVLL PVLLSFFGPY PEVSPACGRN RLPTPSPEPP
PSIVRFALPP GHTNNGSDSS DSEYSSQTTV SGISEELHHY EATQSPGIPV HQVVVEATEN
PVFARSTVVQ PESRHQSSPR LQSNPEAGTQ QVWHQGRQPK QEVREGLRPP PYRPRRDAFE
ISTEGHSGPS NKDRLNHKAH SHNMRSPAFG AMGVPGSAYC QPITTVTASA SVTVAVHPAV
HSHNSCRGSF PSCEEYNEDD RGMFEDPHVP FNVRCERRNS KVEVIELQDV ECEERTAGKI
SE
