PTC1_DANRE
ID PTC1_DANRE Reviewed; 1220 AA.
AC Q98864;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein patched homolog 1;
DE Short=PTC1;
DE Short=Patched 1;
GN Name=ptch1; Synonyms=ptc1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=8787757; DOI=10.1242/dev.122.9.2835;
RA Concordet J.-P., Lewis K.E., Moore J.W., Goodrich L.V., Johnson R.L.,
RA Scott M.P., Ingham P.W.;
RT "Spatial regulation of the zebrafish patched homologue reflects the roles
RT of sonic hedgehog and protein kinase A in neural tube and somite
RT patterning.";
RL Development 122:2835-2846(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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in embryonic presomitic mesoderm,
CC neuroectoderm, tissue surrounding the notochord, ventral neural tube.
CC -!- DEVELOPMENTAL STAGE: At all stages, expression corresponds to the
CC localization of SHH. First detected during gastrulation. By 36 hours,
CC PTC1 appears in the first branchial arch and the posterior mesenchyme
CC of the fin bud; by 48 hours, in the hindbrain and foregut.
CC -!- INDUCTION: Activated by Sonic hedgehog.
CC -!- PTM: Glycosylation is necessary for SHH binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the patched family. {ECO:0000305}.
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DR EMBL; X98883; CAA67386.1; -; mRNA.
DR PIR; T18291; T18291.
DR AlphaFoldDB; Q98864; -.
DR SMR; Q98864; -.
DR STRING; 7955.ENSDARP00000071771; -.
DR PaxDb; Q98864; -.
DR ZFIN; ZDB-GENE-980526-44; ptch2.
DR eggNOG; KOG1935; Eukaryota.
DR InParanoid; Q98864; -.
DR PhylomeDB; Q98864; -.
DR SignaLink; Q98864; -.
DR PRO; PR:Q98864; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0043010; P:camera-type eye development; IMP:ZFIN.
DR GO; GO:0010002; P:cardioblast differentiation; IGI:ZFIN.
DR GO; GO:0048635; P:negative regulation of muscle organ development; IGI:ZFIN.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:ZFIN.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:ZFIN.
DR GO; GO:0009954; P:proximal/distal pattern formation; IMP:ZFIN.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:ZFIN.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:ZFIN.
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 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1220
FT /note="Protein patched homolog 1"
FT /id="PRO_0000205967"
FT TOPO_DOM 1..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..419
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..558
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 580..739
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 761..1016
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1017..1037
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1038..1044
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1066..1072
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1073..1093
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1094..1110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1111..1131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1132..1143
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1144..1164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1165..1220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 421..579
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 888
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1220 AA; 135544 MW; D10A9D04115F532D CRC64;
MASDPRDPGP AGGVFGDLPP SYTRSPPPVN SDLLRRPSYC HAAFALKQIS KGKAVGQKAP
LWIRARFQAF LFSLGCHIQR HCGKVLFIGL LVFGALSVGL RVAAIETDIE KLWVEAGSRV
SKELRYTKEK QGEESVFTSQ MLIQTPKQEG TNILTQEALL LHLEAALSAS KVQVSLYGKS
WDLNKICFKS GVPIIENVMI ERMIDKLFPC MIVTPLDCFW EGSKLQGGSA YLPGMPDIQW
MNLDPLKLME ELSQFTSLEG FREMLDKAQV GHAYMNRPCL DPSDTDCPHS APNKDPWQVP
NIAAELQGGC HGFSKKFMHW QEELILGERV KDSQNALQSA EALQTMFLLM SPKQLYEHFK
DDYEIHDINW NEDKATAILE SWQRKFVEVV HGSIPQNSSS NVYAFSTTTL NDIMKSFSDV
SVIRVAGGYL LMLAYACVTM LRWDCAKSQG AVGLAGVLLV ALSVAAGLGL CSLLGLSFNA
ATTQVLPSLA LGIGVDDMFL LGHSFTETRS NIPFKERTGD CLRRTGTSVA LTSVNNMIAF
FMAALVPIPA LRAFSLQAAV VVVFNFAMAL LIFPAILSLD LHRREDKRLD ILCCFYSPCS
SRVIQIQPQE LSDANDNHQR APATPTYTGS TITTSTHITT TVQAFTQCDA AGQHIVTILP
PTSQISTTPP SMVLSTPTPT TDPYGSQVFT TSSSTRDLLA QVEEPKEGRE CVPLPFFRWN
LSSFAREKYA PLLLKPETKT VVVVVFVALL SLSLYGTTMV HDGLYLTDIV PRDTQEYEFI
TAQFKYFSFY NMYLVTMDGF DYARSQRQLL QLHNAFNSVK YVVKDGNHKL PRMWLHYFQD
WLKGLQATFD ADWEAGKITY DSYRNGTEDG ALAYKPLIQT GSKKEPFNYS QLTSRRLVDG
DGLIPPEVFY IYLTVWVSND PLGYAASQAN FYPHPREWIH DKYDTTGENL RIPAAEPLEF
AQFPFYLNGL RQASDFIEAI ESVRTICEEF MRQGIKNYPN GYPFLFWEQY IGLRHWFLLS
ISVVLACTFL VCAILLLNPW TAGVIVFILP MMTVELFGIM GLIGIKLSAI PVVILIASVG
IGVEFTVHIA LGFLTAIGDR NTRSAVAMEH MFAPVIDGAI STLLGVLMLA GSEFDFIMRY
FFAVLAILTL LGILNGLVLL PVLLSLMGPP AEVVPANNAN HLQSPSPEPM PPPMNHHGYY
AGHIPKASHQ AFSETSDSEY
