ID PTC1_HUMAN Reviewed; 1447 AA. AC Q13635; A3KBI9; E9PEJ8; Q13463; Q5R1U7; Q5R1U9; Q5R1V0; Q5VZC0; AC Q5VZC2; Q86XG7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 2. DT 05-DEC-2018, entry version 192. DE RecName: Full=Protein patched homolog 1; DE Short=PTC; DE Short=PTC1; GN Name=PTCH1; Synonyms=PTCH; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L), AND VARIANTS BCC PRO-175; RP PRO-ASN-ILE-815 INS AND LEU-1315. RC TISSUE=Lung; RX PubMed=8658145; DOI=10.1126/science.272.5268.1668; RA Johnson R.L., Rothman A.L., Xie J., Goodrich L.V., Bare J.W., RA Bonifas J.M., Quinn A.G., Myers R.M., Cox D.R., Epstein E.H. Jr., RA Scott M.P.; RT "Human homolog of patched, a candidate gene for the basal cell nevus RT syndrome."; RL Science 272:1668-1671(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM S), AND VARIANT LEU-1315. RC TISSUE=Fetal brain; RX PubMed=8647801; DOI=10.1074/jbc.271.21.12125; RA Hahn H., Christiansen J., Wicking C., Zaphiropolous P.G., RA Chidambaram A., Gerrard B., Vorechovsky I., Bale A.E., Toftgard R., RA Dean M., Wainwright B.J.; RT "A mammalian patched homolog is expressed in target tissues of sonic RT hedgehog and maps to a region associated with developmental RT abnormalities."; RL J. Biol. Chem. 271:12125-12128(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-324 (ISOFORM L'), NUCLEOTIDE SEQUENCE RP [MRNA] OF 1-259 (ISOFORM M), NUCLEOTIDE SEQUENCE [MRNA] OF 1-174 RP (ISOFORM S), AND ALTERNATIVE SPLICING. RX PubMed=15780749; DOI=10.1016/j.ygeno.2004.11.014; RA Nagao K., Toyoda M., Takeuchi-Inoue K., Fujii K., Yamada M., RA Miyashita T.; RT "Identification and characterization of multiple isoforms of a murine RT and human tumor suppressor, patched, having distinct first exons."; RL Genomics 85:462-471(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-183 (ISOFORM M). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-90 (ISOFORM S), AND ALTERNATIVE RP SPLICING. RX PubMed=17310997; DOI=10.1038/sj.onc.1210301; RA Shimokawa T., Svard J., Heby-Henricson K., Teglund S., Toftgard R., RA Zaphiropoulos P.G.; RT "Distinct roles of first exon variants of the tumor-suppressor RT Patched1 in Hedgehog signaling."; RL Oncogene 26:4889-4896(2007). RN [7] RP INTERACTION WITH SNX17. RX PubMed=15769472; DOI=10.1016/j.jmb.2005.02.004; RA Knauth P., Schlueter T., Czubayko M., Kirsch C., Florian V., RA Schreckenberger S., Hahn H., Bohnensack R.; RT "Functions of sorting nexin 17 domains and recognition motif for P- RT selectin trafficking."; RL J. Mol. Biol. 347:813-825(2005). RN [8] RP FUNCTION, AND INTERACTION WITH IHH. RX PubMed=21537345; DOI=10.1038/cr.2011.76; RA Ma G., Yu J., Xiao Y., Chan D., Gao B., Hu J., He Y., Guo S., Zhou J., RA Zhang L., Gao L., Zhang W., Kang Y., Cheah K.S., Feng G., Guo X., RA Wang Y., Zhou C.Z., He L.; RT "Indian hedgehog mutations causing brachydactyly type A1 impair RT Hedgehog signal transduction at multiple levels."; RL Cell Res. 21:1343-1357(2011). RN [9] RP VARIANTS BCNS ARG-509; VAL-509; GLN-816 DEL AND TYR-1132. RX PubMed=8840969; RA Chidambaram A., Goldstein A.M., Gailani M.R., Gerrard B., Bale S.J., RA DiGiovanna J.J., Bale A.E., Dean M.; RT "Mutations in the human homologue of the Drosophila patched gene in RT Caucasian and African-American nevoid basal cell carcinoma syndrome RT patients."; RL Cancer Res. 56:4599-4601(1996). RN [10] RP VARIANTS BCNS TYR-513 AND ARG-1069. RX PubMed=8981943; RA Wicking C., Shanley S., Smyth I., Gillies S., Negus K., Graham S., RA Suthers G., Haites N., Edwards M., Wainwright B.J., RA Chenevix-Trench G.; RT "Most germ-line mutations in the nevoid basal cell carcinoma syndrome RT lead to a premature termination of the PATCHED protein, and no RT genotype-phenotype correlations are evident."; RL Am. J. Hum. Genet. 60:21-26(1997). RN [11] RP VARIANT NBCCS ASP-1438. RX PubMed=9341860; DOI=10.1007/s004390050541; RA Lench N.J., Telford E.A.R., High A.S., Markham A.F., Wicking C., RA Wainwright B.J.; RT "Characterisation of human patched germ line mutations in naevoid RT basal cell carcinoma syndrome."; RL Hum. Genet. 100:497-502(1997). RN [12] RP VARIANT LEU-1315. RX PubMed=10200051; RX DOI=10.1002/(SICI)1098-1004(1998)11:6<480::AID-HUMU9>3.0.CO;2-4; RA Hasenpusch-Theil K., Bataille V., Laehdetie J., Obermayr F., RA Sampson J.R., Frischauf A.-M.; RT "Gorlin syndrome: identification of 4 novel germ-line mutations of the RT human patched (PTCH) gene."; RL Hum. Mutat. 11:480-480(1998). RN [13] RP VARIANTS BCNS SER-376 AND VAL-1083 INS, AND VARIANT BCC TRP-1114. RX PubMed=9620294; DOI=10.1046/j.1523-1747.1998.00222.x; RA Aszterbaum M., Rothman A.L., Johnson R.L., Fisher M., Xie J., RA Bonifas J.M., Zhang X., Scott M.P., Epstein E.H. Jr.; RT "Identification of mutations in the human PATCHED gene in sporadic RT basal cell carcinomas and in patients with the basal cell nevus RT syndrome."; RL J. Invest. Dermatol. 110:885-888(1998). RN [14] RP VARIANT LEU-1315. RX PubMed=10874314; RX DOI=10.1002/1098-1004(200007)16:1<89::AID-HUMU18>3.3.CO;2-Z; RA Dong J., Gailani M.R., Pomeroy S.L., Reardon D., Bale A.E.; RT "Identification of PATCHED mutations in medulloblastomas by direct RT sequencing."; RL Hum. Mutat. 16:89-90(2000). RN [15] RP VARIANT BCNS PRO-1132. RX PubMed=11231326; DOI=10.1046/j.1523-1747.2001.01279-2.x; RA Reifenberger J., Arnold N., Kiechle M., Reifenberger G., Hauschild A.; RT "Coincident PTCH and BRCA1 germline mutations in a patient with nevoid RT basal cell carcinoma syndrome and familial breast cancer."; RL J. Invest. Dermatol. 116:472-474(2001). RN [16] RP VARIANTS SQUAMOUS CELL CARCINOMA MET-829 AND LYS-1242. RX PubMed=11286632; DOI=10.1046/j.1523-1747.2001.01301.x; RA Ping X.L., Ratner D., Zhang H., Wu X.L., Zhang M.J., Chen F.F., RA Silvers D.N., Peacocke M., Tsou H.C.; RT "PTCH mutations in squamous cell carcinoma of the skin."; RL J. Invest. Dermatol. 116:614-616(2001). RN [17] RP VARIANTS HPE7 THR-393; MET-728; GLY-827 AND MET-1052. RX PubMed=11941477; DOI=10.1007/s00439-002-0695-5; RA Ming J.E., Kaupas M.E., Roessler E., Brunner H.G., Golabi M., RA Tekin M., Stratton R.F., Sujansky E., Bale S.J., Muenke M.; RT "Mutations in PATCHED-1, the receptor for SONIC HEDGEHOG, are RT associated with holoprosencephaly."; RL Hum. Genet. 110:297-301(2002). RN [18] RP ERRATUM. RA Ming J.E., Kaupas M.E., Roessler E., Brunner H.G., Golabi M., RA Tekin M., Stratton R.F., Sujansky E., Bale S.J., Muenke M.; RL Hum. Genet. 111:464-464(2002). RN [19] RP VARIANTS BCNS PRO-230 AND 505-LEU-ARG-506. RX PubMed=15459969; DOI=10.1002/humu.9289; RA Savino M., d'Apolito M., Formica V., Baorda F., Mari F., Renieri A., RA Carabba E., Tarantino E., Andreucci E., Belli S., Lo Muzio L., RA Dallapiccola B., Zelante L., Savoia A.; RT "Spectrum of PTCH mutations in Italian nevoid basal cell-carcinoma RT syndrome patients: identification of thirteen novel alleles."; RL Hum. Mutat. 24:441-441(2004). RN [20] RP VARIANT HPE7 MET-728. RX PubMed=17096318; DOI=10.1002/ajmg.a.31370; RA Rahimov F., Ribeiro L.A., de Miranda E., Richieri-Costa A., RA Murray J.C.; RT "GLI2 mutations in four Brazilian patients: how wide is the phenotypic RT spectrum?"; RL Am. J. Med. Genet. A 140:2571-2576(2006). RN [21] RP VARIANTS HPE7 GLY-443; GLY-751; GLY-908 AND MET-1052. RX PubMed=17001668; DOI=10.1002/ajmg.a.31369; RA Ribeiro L.A., Murray J.C., Richieri-Costa A.; RT "PTCH mutations in four Brazilian patients with holoprosencephaly and RT in one with holoprosencephaly-like features and normal MRI."; RL Am. J. Med. Genet. A 140:2584-2586(2006). CC -!- FUNCTION: Acts as a receptor for sonic hedgehog (SHH), indian CC hedgehog (IHH) and desert hedgehog (DHH). Associates with the CC smoothened protein (SMO) to transduce the hedgehog's proteins CC signal. Seems to have a tumor suppressor function, as inactivation CC of this protein is probably a necessary, if not sufficient step CC for tumorigenesis. {ECO:0000269|PubMed:21537345}. CC -!- SUBUNIT: Interacts with SNX17 (PubMed:15769472). Interacts with CC IHH (PubMed:21537345). Interacts with G-protein coupled receptor CC GPR37L1 (By similarity). {ECO:0000250|UniProtKB:Q61115, CC ECO:0000269|PubMed:15769472, ECO:0000269|PubMed:21537345}. CC -!- INTERACTION: CC P14635:CCNB1; NbExp=2; IntAct=EBI-8775406, EBI-495332; CC P21146:GRK2 (xeno); NbExp=4; IntAct=EBI-8775406, EBI-1036401; CC P25098:GRK2; NbExp=2; IntAct=EBI-8775406, EBI-3904795; CC Q15465:SHH; NbExp=2; IntAct=EBI-8775406, EBI-11666886; CC P46937:YAP1; NbExp=3; IntAct=EBI-8775406, EBI-1044059; CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000250|UniProtKB:Q61115}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=L; Synonyms=1B; CC IsoId=Q13635-1; Sequence=Displayed; CC Name=L'; Synonyms=1Ckid; CC IsoId=Q13635-2; Sequence=VSP_041369; CC Name=M; Synonyms=1C; CC IsoId=Q13635-3; Sequence=VSP_041371; CC Name=S; Synonyms=1A, 1CdeltaE2; CC IsoId=Q13635-4; Sequence=VSP_041370; CC -!- TISSUE SPECIFICITY: In the adult, expressed in brain, lung, liver, CC heart, placenta, skeletal muscle, pancreas and kidney. Expressed CC in tumor cells but not in normal skin. CC -!- DEVELOPMENTAL STAGE: In the embryo, found in all major target CC tissues of sonic hedgehog, such as the ventral neural tube, CC somites, and tissues surrounding the zone of polarizing activity CC of the limb bud. CC -!- PTM: Glycosylation is necessary for SHH binding. {ECO:0000250}. CC -!- PTM: In the absence of Hh ligands, ubiquitination by ITCH at Lys- CC 1426 promotes endocytosis and both proteasomal and lysosomal CC degradation. {ECO:0000250|UniProtKB:Q61115}. CC -!- DISEASE: Basal cell nevus syndrome (BCNS) [MIM:109400]: An CC autosomal dominant disease characterized by nevoid basal cell CC carcinomas and developmental abnormalities such as rib and CC craniofacial alterations, polydactyly, syndactyly, and spina CC bifida. In addition, the patients suffer from a multitude of CC tumors like basal cell carcinomas, fibromas of the ovaries and CC heart, cysts of the skin, jaws and mesentery, as well as CC medulloblastomas and meningiomas. {ECO:0000269|PubMed:11231326, CC ECO:0000269|PubMed:15459969, ECO:0000269|PubMed:8840969, CC ECO:0000269|PubMed:8981943, ECO:0000269|PubMed:9620294}. Note=The CC disease may be caused by mutations affecting the gene represented CC in this entry. CC -!- DISEASE: Basal cell carcinoma (BCC) [MIM:605462]: A common CC malignant skin neoplasm that typically appears on hair-bearing CC skin, most commonly on sun-exposed areas. BCC is slow growing and CC rarely metastasizes, but has potentialities for local invasion and CC destruction. It usually develops as a flat, firm, pale area that CC is small, raised, pink or red, translucent, shiny, and waxy, and CC the area may bleed following minor injury. Tumor size can vary CC from a few millimeters to several centimeters in diameter. CC {ECO:0000269|PubMed:8658145, ECO:0000269|PubMed:9620294}. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- DISEASE: Holoprosencephaly 7 (HPE7) [MIM:610828]: A structural CC anomaly of the brain, in which the developing forebrain fails to CC correctly separate into right and left hemispheres. CC Holoprosencephaly is genetically heterogeneous and associated with CC several distinct facies and phenotypic variability. CC {ECO:0000269|PubMed:11941477, ECO:0000269|PubMed:17001668, CC ECO:0000269|PubMed:17096318}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the patched family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/PTCHID100.html"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U59464; AAC50550.1; -; mRNA. DR EMBL; U43148; AAC50496.1; -; mRNA. DR EMBL; AL161729; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB189436; BAD74184.1; -; mRNA. DR EMBL; AB189437; BAD74185.1; -; mRNA. DR EMBL; AB189438; BAD74186.1; -; mRNA. DR EMBL; AB189439; BAD74187.1; -; mRNA. DR EMBL; AB189440; BAD74188.1; -; mRNA. DR EMBL; BC043542; AAH43542.1; -; mRNA. DR EMBL; AB239329; BAF47712.1; -; mRNA. DR CCDS; CCDS43851.1; -. [Q13635-4] DR CCDS; CCDS47995.1; -. [Q13635-2] DR CCDS; CCDS47996.1; -. [Q13635-3] DR CCDS; CCDS6714.1; -. [Q13635-1] DR RefSeq; NP_000255.2; NM_000264.3. [Q13635-1] DR RefSeq; NP_001077071.1; NM_001083602.1. [Q13635-3] DR RefSeq; NP_001077072.1; NM_001083603.1. [Q13635-2] DR RefSeq; NP_001077073.1; NM_001083604.1. [Q13635-4] DR RefSeq; NP_001077074.1; NM_001083605.1. [Q13635-4] DR RefSeq; NP_001077075.1; NM_001083606.1. [Q13635-4] DR RefSeq; NP_001077076.1; NM_001083607.1. [Q13635-4] DR UniGene; Hs.494538; -. DR PDB; 6D4H; EM; 3.50 A; A=1-1447. DR PDB; 6D4J; EM; 3.80 A; A=1-1447. DR PDB; 6DMB; EM; 3.90 A; A=1-1305. DR PDB; 6DMO; EM; 4.10 A; A=1-1305. DR PDB; 6DMY; EM; 3.60 A; A=1-1305. DR PDB; 6E1H; EM; 3.50 A; A/B=1-1447. DR PDBsum; 6D4H; -. DR PDBsum; 6D4J; -. DR PDBsum; 6DMB; -. DR PDBsum; 6DMO; -. DR PDBsum; 6DMY; -. DR PDBsum; 6E1H; -. DR ProteinModelPortal; Q13635; -. DR SMR; Q13635; -. DR BioGrid; 111699; 185. DR CORUM; Q13635; -. DR DIP; DIP-44940N; -. DR IntAct; Q13635; 18. DR MINT; Q13635; -. DR STRING; 9606.ENSP00000332353; -. DR TCDB; 2.A.6.6.13; the resistance-nodulation-cell division (rnd) superfamily. DR iPTMnet; Q13635; -. DR PhosphoSitePlus; Q13635; -. DR BioMuta; PTCH1; -. DR DMDM; 160415977; -. DR EPD; Q13635; -. DR PaxDb; Q13635; -. DR PeptideAtlas; Q13635; -. DR PRIDE; Q13635; -. DR ProteomicsDB; 59627; -. DR ProteomicsDB; 59628; -. [Q13635-2] DR ProteomicsDB; 59629; -. [Q13635-3] DR ProteomicsDB; 59630; -. [Q13635-4] DR DNASU; 5727; -. DR Ensembl; ENST00000331920; ENSP00000332353; ENSG00000185920. [Q13635-1] DR Ensembl; ENST00000375274; ENSP00000364423; ENSG00000185920. [Q13635-2] DR Ensembl; ENST00000418258; ENSP00000396135; ENSG00000185920. [Q13635-4] DR Ensembl; ENST00000421141; ENSP00000399981; ENSG00000185920. [Q13635-4] DR Ensembl; ENST00000429896; ENSP00000414823; ENSG00000185920. [Q13635-4] DR Ensembl; ENST00000430669; ENSP00000410287; ENSG00000185920. [Q13635-3] DR Ensembl; ENST00000437951; ENSP00000389744; ENSG00000185920. [Q13635-3] DR GeneID; 5727; -. DR KEGG; hsa:5727; -. DR UCSC; uc004avk.5; human. [Q13635-1] DR CTD; 5727; -. DR DisGeNET; 5727; -. DR EuPathDB; HostDB:ENSG00000185920.15; -. DR GeneCards; PTCH1; -. DR GeneReviews; PTCH1; -. DR HGNC; HGNC:9585; PTCH1. DR HPA; CAB013717; -. DR HPA; HPA075072; -. DR MalaCards; PTCH1; -. DR MIM; 109400; phenotype. DR MIM; 601309; gene. DR MIM; 605462; phenotype. DR MIM; 610828; phenotype. DR neXtProt; NX_Q13635; -. DR OpenTargets; ENSG00000185920; -. DR Orphanet; 93925; Alobar holoprosencephaly. DR Orphanet; 377; Gorlin syndrome. DR Orphanet; 93924; Lobar holoprosencephaly. DR Orphanet; 280200; Microform holoprosencephaly. DR Orphanet; 93926; Midline interhemispheric variant of holoprosencephaly. DR Orphanet; 77301; Monosomy 9q22.3. DR Orphanet; 220386; Semilobar holoprosencephaly. DR Orphanet; 280195; Septopreoptic holoprosencephaly. DR PharmGKB; PA33937; -. DR eggNOG; KOG1935; Eukaryota. DR eggNOG; ENOG410XRKU; LUCA. DR GeneTree; ENSGT00940000159011; -. DR HOVERGEN; HBG067607; -. DR InParanoid; Q13635; -. DR KO; K06225; -. DR OMA; LFGFYSM; -. DR OrthoDB; EOG091G0LGQ; -. DR PhylomeDB; Q13635; -. DR TreeFam; TF106489; -. DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors). DR Reactome; R-HSA-5610787; Hedgehog 'off' state. DR Reactome; R-HSA-5632681; Ligand-receptor interactions. DR Reactome; R-HSA-5632684; Hedgehog 'on' state. DR Reactome; R-HSA-5635838; Activation of SMO. DR SignaLink; Q13635; -. DR SIGNOR; Q13635; -. DR ChiTaRS; PTCH1; human. DR GeneWiki; PTCH1; -. DR GenomeRNAi; 5727; -. DR PRO; PR:Q13635; -. DR Proteomes; UP000005640; Chromosome 9. DR Bgee; ENSG00000185920; Expressed in 222 organ(s), highest expression level in tibia. DR CleanEx; HS_PTCH1; -. DR ExpressionAtlas; Q13635; baseline and differential. DR Genevisible; Q13635; HS. DR GO; GO:0044295; C:axonal growth cone; IEA:Ensembl. DR GO; GO:0005901; C:caveola; IDA:BHF-UCL. DR GO; GO:0060170; C:ciliary membrane; TAS:Reactome. DR GO; GO:0044294; C:dendritic growth cone; IEA:Ensembl. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:BHF-UCL. DR GO; GO:0030496; C:midbody; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL. DR GO; GO:0030332; F:cyclin binding; IPI:BHF-UCL. DR GO; GO:0097108; F:hedgehog family protein binding; IPI:BHF-UCL. DR GO; GO:0008158; F:hedgehog receptor activity; IBA:GO_Central. DR GO; GO:0008201; F:heparin binding; IEA:Ensembl. DR GO; GO:0005113; F:patched binding; IEA:Ensembl. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0005119; F:smoothened binding; IPI:BHF-UCL. DR GO; GO:0009887; P:animal organ morphogenesis; ISS:UniProtKB. DR GO; GO:0007420; P:brain development; ISS:BHF-UCL. DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl. DR GO; GO:0061005; P:cell differentiation involved in kidney development; IEA:Ensembl. DR GO; GO:0001709; P:cell fate determination; IEA:Ensembl. DR GO; GO:0072203; P:cell proliferation involved in metanephros development; IEA:Ensembl. DR GO; GO:0071397; P:cellular response to cholesterol; IMP:BHF-UCL. DR GO; GO:0071679; P:commissural neuron axon guidance; IEA:Ensembl. DR GO; GO:0009953; P:dorsal/ventral pattern formation; ISS:UniProtKB. DR GO; GO:0030326; P:embryonic limb morphogenesis; ISS:UniProtKB. DR GO; GO:0048568; P:embryonic organ development; IEA:Ensembl. DR GO; GO:0009957; P:epidermal cell fate specification; IEA:Ensembl. DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl. DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl. DR GO; GO:0035137; P:hindlimb morphogenesis; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl. DR GO; GO:0035108; P:limb morphogenesis; IMP:BHF-UCL. DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl. DR GO; GO:0060603; P:mammary gland duct morphogenesis; IEA:Ensembl. DR GO; GO:0060644; P:mammary gland epithelial cell differentiation; IEA:Ensembl. DR GO; GO:0051782; P:negative regulation of cell division; IEA:Ensembl. DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:BHF-UCL. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl. DR GO; GO:0040015; P:negative regulation of multicellular organism growth; ISS:UniProtKB. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:BHF-UCL. DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0021997; P:neural plate axis specification; ISS:BHF-UCL. DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl. DR GO; GO:0021532; P:neural tube patterning; IMP:BHF-UCL. DR GO; GO:0060037; P:pharyngeal system development; IMP:BHF-UCL. DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:BHF-UCL. DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl. DR GO; GO:0030850; P:prostate gland development; IEA:Ensembl. DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL. DR GO; GO:0016485; P:protein processing; ISS:UniProtKB. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl. DR GO; GO:0008589; P:regulation of smoothened signaling pathway; ISS:UniProtKB. DR GO; GO:0072001; P:renal system development; IEP:UniProtKB. DR GO; GO:0010157; P:response to chlorate; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl. DR GO; GO:0007224; P:smoothened signaling pathway; IEP:UniProtKB. DR GO; GO:0060831; P:smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IEA:Ensembl. DR GO; GO:0061053; P:somite development; IMP:BHF-UCL. DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IEA:Ensembl. 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 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Complete proteome; KW Disease mutation; Glycoprotein; Holoprosencephaly; Isopeptide bond; KW Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome; KW Transmembrane; Transmembrane helix; Tumor suppressor; Ubl conjugation. FT CHAIN 1 1447 Protein patched homolog 1. FT /FTId=PRO_0000205964. FT TOPO_DOM 1 100 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TOPO_DOM 122 436 Extracellular. {ECO:0000255}. FT TRANSMEM 437 457 Helical. {ECO:0000255}. FT TOPO_DOM 458 472 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 473 493 Helical. {ECO:0000255}. FT TOPO_DOM 494 501 Extracellular. {ECO:0000255}. FT TRANSMEM 502 522 Helical. {ECO:0000255}. FT TOPO_DOM 523 547 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 548 568 Helical. {ECO:0000255}. FT TOPO_DOM 569 577 Extracellular. {ECO:0000255}. FT TRANSMEM 578 598 Helical. {ECO:0000255}. FT TOPO_DOM 599 748 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 749 769 Helical. {ECO:0000255}. FT TOPO_DOM 770 1027 Extracellular. {ECO:0000255}. FT TRANSMEM 1028 1048 Helical. {ECO:0000255}. FT TOPO_DOM 1049 1055 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 1056 1076 Helical. {ECO:0000255}. FT TOPO_DOM 1077 1083 Extracellular. {ECO:0000255}. FT TRANSMEM 1084 1104 Helical. {ECO:0000255}. FT TOPO_DOM 1105 1121 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 1122 1141 Helical. {ECO:0000255}. FT TOPO_DOM 1142 1154 Extracellular. {ECO:0000255}. FT TRANSMEM 1155 1175 Helical. {ECO:0000255}. FT TOPO_DOM 1176 1447 Cytoplasmic. {ECO:0000255}. FT DOMAIN 438 598 SSD. {ECO:0000255|PROSITE- FT ProRule:PRU00199}. FT COMPBIAS 14 31 Gly-rich. FT MOD_RES 1195 1195 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q61115}. FT MOD_RES 1197 1197 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61115}. FT CARBOHYD 141 141 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 312 312 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 349 349 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 414 414 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 875 875 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1000 1000 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CROSSLNK 1426 1426 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250|UniProtKB:Q61115}. FT VAR_SEQ 1 66 MASAGNAAEPQDRGGGGSGCIGAPGRPAGGGRRRRTGGLRR FT AAAPDRDYLHRPSYCDAAFALEQIS -> MELLNRNRLVIV FT SPRCTPPKASGGPARRGFYTFRSFCKDGGGGEEEEENGGEE FT KDDRGDKETRSD (in isoform L'). FT {ECO:0000303|PubMed:15780749}. FT /FTId=VSP_041369. FT VAR_SEQ 2 152 Missing (in isoform S). FT {ECO:0000303|PubMed:15780749, FT ECO:0000303|PubMed:17310997, FT ECO:0000303|PubMed:8647801}. FT /FTId=VSP_041370. FT VAR_SEQ 2 67 Missing (in isoform M). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:15780749}. FT /FTId=VSP_041371. FT VARIANT 175 175 L -> P (in BCNS; sporadic BCC). FT {ECO:0000269|PubMed:8658145}. FT /FTId=VAR_007843. FT VARIANT 230 230 T -> P (in BCNS). FT {ECO:0000269|PubMed:15459969}. FT /FTId=VAR_020845. FT VARIANT 376 376 F -> S (in BCNS). FT {ECO:0000269|PubMed:9620294}. FT /FTId=VAR_007844. FT VARIANT 393 393 A -> T (in HPE7; dbSNP:rs199476091). FT {ECO:0000269|PubMed:11941477}. FT /FTId=VAR_032952. FT VARIANT 443 443 A -> G (in HPE7; dbSNP:rs878853845). FT {ECO:0000269|PubMed:17001668}. FT /FTId=VAR_032953. FT VARIANT 505 506 FL -> LR (in BCNS). FT /FTId=VAR_020846. FT VARIANT 509 509 G -> R (in BCNS; unknown pathological FT significance). FT {ECO:0000269|PubMed:8840969}. FT /FTId=VAR_010974. FT VARIANT 509 509 G -> V (in BCNS). FT {ECO:0000269|PubMed:8840969}. FT /FTId=VAR_010975. FT VARIANT 513 513 D -> Y (in BCNS). FT {ECO:0000269|PubMed:8981943}. FT /FTId=VAR_010976. FT VARIANT 728 728 T -> M (in HPE7; dbSNP:rs115556836). FT {ECO:0000269|PubMed:11941477, FT ECO:0000269|PubMed:17096318}. FT /FTId=VAR_032954. FT VARIANT 751 751 V -> G (in HPE7). FT {ECO:0000269|PubMed:17001668}. FT /FTId=VAR_032955. FT VARIANT 815 815 I -> IPNI (in BCNS). FT /FTId=VAR_007845. FT VARIANT 816 816 Missing (in BCNS). FT {ECO:0000269|PubMed:8840969}. FT /FTId=VAR_010977. FT VARIANT 827 827 S -> G (in HPE7; dbSNP:rs199476092). FT {ECO:0000269|PubMed:11941477}. FT /FTId=VAR_032956. FT VARIANT 829 829 V -> M (in squamous cell carcinoma; FT dbSNP:rs201125580). FT {ECO:0000269|PubMed:11286632}. FT /FTId=VAR_010978. FT VARIANT 908 908 V -> G (in HPE7; dbSNP:rs199476093). FT {ECO:0000269|PubMed:17001668}. FT /FTId=VAR_032957. FT VARIANT 1052 1052 T -> M (in HPE7; dbSNP:rs138911275). FT {ECO:0000269|PubMed:11941477, FT ECO:0000269|PubMed:17001668}. FT /FTId=VAR_032958. FT VARIANT 1069 1069 G -> R (in BCNS). FT {ECO:0000269|PubMed:8981943}. FT /FTId=VAR_010979. FT VARIANT 1083 1083 V -> VV (in BCNS). FT {ECO:0000269|PubMed:9620294}. FT /FTId=VAR_007846. FT VARIANT 1114 1114 R -> W (in BCNS and BCC; FT dbSNP:rs587776689). FT {ECO:0000269|PubMed:9620294}. FT /FTId=VAR_007847. FT VARIANT 1132 1132 S -> P (in BCNS; dbSNP:rs878853856). FT {ECO:0000269|PubMed:11231326}. FT /FTId=VAR_010980. FT VARIANT 1132 1132 S -> Y (in BCNS). FT {ECO:0000269|PubMed:8840969}. FT /FTId=VAR_010981. FT VARIANT 1195 1195 T -> S (in dbSNP:rs2236405). FT /FTId=VAR_020440. FT VARIANT 1242 1242 E -> K (in squamous cell carcinoma; FT dbSNP:rs779417284). FT {ECO:0000269|PubMed:11286632}. FT /FTId=VAR_010982. FT VARIANT 1282 1282 P -> L (in dbSNP:rs2227968). FT /FTId=VAR_020847. FT VARIANT 1315 1315 P -> L (in dbSNP:rs357564). FT {ECO:0000269|PubMed:10200051, FT ECO:0000269|PubMed:10874314, FT ECO:0000269|PubMed:8647801, FT ECO:0000269|PubMed:8658145}. FT /FTId=VAR_010983. FT VARIANT 1438 1438 E -> D (in BCNS; sporadic NBCCS). FT {ECO:0000269|PubMed:9341860}. FT /FTId=VAR_010984. FT CONFLICT 1109 1109 G -> S (in Ref. 2; AAC50496). FT {ECO:0000305}. FT CONFLICT 1144 1144 E -> D (in Ref. 2; AAC50496). FT {ECO:0000305}. FT CONFLICT 1175 1175 L -> W (in Ref. 2; AAC50496). FT {ECO:0000305}. FT CONFLICT 1283 1283 R -> K (in Ref. 2; AAC50496). FT {ECO:0000305}. FT CONFLICT 1309 1309 E -> K (in Ref. 2; AAC50496). FT {ECO:0000305}. FT CONFLICT 1353 1353 A -> T (in Ref. 2; AAC50496). FT {ECO:0000305}. FT HELIX 78 95 {ECO:0000244|PDB:6D4H}. FT HELIX 97 99 {ECO:0000244|PDB:6E1H}. FT HELIX 101 113 {ECO:0000244|PDB:6D4H}. FT HELIX 114 117 {ECO:0000244|PDB:6D4H}. FT TURN 126 128 {ECO:0000244|PDB:6D4H}. FT TURN 132 134 {ECO:0000244|PDB:6D4H}. FT HELIX 135 146 {ECO:0000244|PDB:6D4H}. FT STRAND 147 151 {ECO:0000244|PDB:6D4H}. FT STRAND 157 160 {ECO:0000244|PDB:6D4H}. FT STRAND 163 167 {ECO:0000244|PDB:6D4H}. FT HELIX 172 186 {ECO:0000244|PDB:6D4H}. FT STRAND 194 196 {ECO:0000244|PDB:6D4H}. FT HELIX 202 205 {ECO:0000244|PDB:6D4H}. FT HELIX 220 223 {ECO:0000244|PDB:6D4H}. FT TURN 224 226 {ECO:0000244|PDB:6D4H}. FT STRAND 234 236 {ECO:0000244|PDB:6E1H}. FT HELIX 245 255 {ECO:0000244|PDB:6D4H}. FT STRAND 256 258 {ECO:0000244|PDB:6D4H}. FT STRAND 264 266 {ECO:0000244|PDB:6D4H}. FT HELIX 270 276 {ECO:0000244|PDB:6D4H}. FT HELIX 284 290 {ECO:0000244|PDB:6D4H}. FT STRAND 302 304 {ECO:0000244|PDB:6D4H}. FT STRAND 310 312 {ECO:0000244|PDB:6E1H}. FT STRAND 313 315 {ECO:0000244|PDB:6D4H}. FT HELIX 320 323 {ECO:0000244|PDB:6D4H}. FT STRAND 330 335 {ECO:0000244|PDB:6D4H}. FT HELIX 339 342 {ECO:0000244|PDB:6D4H}. FT STRAND 348 353 {ECO:0000244|PDB:6D4H}. FT STRAND 358 363 {ECO:0000244|PDB:6E1H}. FT HELIX 369 373 {ECO:0000244|PDB:6D4H}. FT TURN 378 380 {ECO:0000244|PDB:6D4H}. FT STRAND 384 386 {ECO:0000244|PDB:6D4H}. FT HELIX 389 410 {ECO:0000244|PDB:6D4H}. FT STRAND 413 415 {ECO:0000244|PDB:6D4H}. FT STRAND 419 422 {ECO:0000244|PDB:6D4H}. FT HELIX 424 434 {ECO:0000244|PDB:6D4H}. FT HELIX 439 453 {ECO:0000244|PDB:6D4H}. FT HELIX 454 457 {ECO:0000244|PDB:6D4H}. FT STRAND 460 462 {ECO:0000244|PDB:6D4H}. FT STRAND 463 465 {ECO:0000244|PDB:6E1H}. FT HELIX 470 490 {ECO:0000244|PDB:6D4H}. FT HELIX 497 501 {ECO:0000244|PDB:6D4H}. FT HELIX 503 525 {ECO:0000244|PDB:6D4H}. FT STRAND 531 534 {ECO:0000244|PDB:6E1H}. FT HELIX 536 562 {ECO:0000244|PDB:6D4H}. FT STRAND 563 567 {ECO:0000244|PDB:6D4H}. FT HELIX 568 589 {ECO:0000244|PDB:6D4H}. FT HELIX 592 605 {ECO:0000244|PDB:6D4H}. FT HELIX 733 743 {ECO:0000244|PDB:6D4H}. FT HELIX 748 769 {ECO:0000244|PDB:6D4H}. FT TURN 777 780 {ECO:0000244|PDB:6D4H}. FT STRAND 783 785 {ECO:0000244|PDB:6D4H}. FT HELIX 786 797 {ECO:0000244|PDB:6D4H}. FT STRAND 804 807 {ECO:0000244|PDB:6D4H}. FT TURN 812 814 {ECO:0000244|PDB:6D4H}. FT HELIX 817 824 {ECO:0000244|PDB:6D4H}. FT HELIX 825 827 {ECO:0000244|PDB:6D4H}. FT STRAND 830 832 {ECO:0000244|PDB:6D4H}. FT STRAND 836 840 {ECO:0000244|PDB:6D4H}. FT HELIX 844 862 {ECO:0000244|PDB:6D4H}. FT HELIX 869 877 {ECO:0000244|PDB:6D4H}. FT STRAND 881 883 {ECO:0000244|PDB:6D4H}. FT STRAND 891 894 {ECO:0000244|PDB:6E1H}. FT HELIX 898 900 {ECO:0000244|PDB:6E1H}. FT HELIX 903 907 {ECO:0000244|PDB:6D4H}. FT STRAND 910 914 {ECO:0000244|PDB:6D4H}. FT STRAND 916 918 {ECO:0000244|PDB:6D4H}. FT HELIX 919 929 {ECO:0000244|PDB:6D4H}. FT HELIX 931 937 {ECO:0000244|PDB:6D4H}. FT STRAND 957 959 {ECO:0000244|PDB:6D4H}. FT STRAND 972 975 {ECO:0000244|PDB:6D4H}. FT HELIX 984 1002 {ECO:0000244|PDB:6D4H}. FT STRAND 1008 1012 {ECO:0000244|PDB:6E1H}. FT HELIX 1013 1016 {ECO:0000244|PDB:6D4H}. FT STRAND 1017 1019 {ECO:0000244|PDB:6D4H}. FT HELIX 1020 1023 {ECO:0000244|PDB:6D4H}. FT HELIX 1025 1046 {ECO:0000244|PDB:6D4H}. FT HELIX 1050 1074 {ECO:0000244|PDB:6D4H}. FT HELIX 1080 1101 {ECO:0000244|PDB:6D4H}. FT HELIX 1102 1105 {ECO:0000244|PDB:6D4H}. FT STRAND 1106 1110 {ECO:0000244|PDB:6D4H}. FT HELIX 1115 1130 {ECO:0000244|PDB:6D4H}. FT HELIX 1133 1136 {ECO:0000244|PDB:6D4H}. FT HELIX 1137 1140 {ECO:0000244|PDB:6D4H}. FT STRAND 1143 1147 {ECO:0000244|PDB:6D4H}. FT HELIX 1148 1151 {ECO:0000244|PDB:6D4H}. FT HELIX 1153 1173 {ECO:0000244|PDB:6D4H}. SQ SEQUENCE 1447 AA; 160545 MW; F2937247BC812F85 CRC64; MASAGNAAEP QDRGGGGSGC IGAPGRPAGG GRRRRTGGLR RAAAPDRDYL HRPSYCDAAF ALEQISKGKA TGRKAPLWLR AKFQRLLFKL GCYIQKNCGK FLVVGLLIFG AFAVGLKAAN LETNVEELWV EVGGRVSREL NYTRQKIGEE AMFNPQLMIQ TPKEEGANVL TTEALLQHLD SALQASRVHV YMYNRQWKLE HLCYKSGELI TETGYMDQII EYLYPCLIIT PLDCFWEGAK LQSGTAYLLG KPPLRWTNFD PLEFLEELKK INYQVDSWEE MLNKAEVGHG YMDRPCLNPA DPDCPATAPN KNSTKPLDMA LVLNGGCHGL SRKYMHWQEE LIVGGTVKNS TGKLVSAHAL QTMFQLMTPK QMYEHFKGYE YVSHINWNED KAAAILEAWQ RTYVEVVHQS VAQNSTQKVL SFTTTTLDDI LKSFSDVSVI RVASGYLLML AYACLTMLRW DCSKSQGAVG LAGVLLVALS VAAGLGLCSL IGISFNAATT QVLPFLALGV GVDDVFLLAH AFSETGQNKR IPFEDRTGEC LKRTGASVAL TSISNVTAFF MAALIPIPAL RAFSLQAAVV VVFNFAMVLL IFPAILSMDL YRREDRRLDI FCCFTSPCVS RVIQVEPQAY TDTHDNTRYS PPPPYSSHSF AHETQITMQS TVQLRTEYDP HTHVYYTTAE PRSEISVQPV TVTQDTLSCQ SPESTSSTRD LLSQFSDSSL HCLEPPCTKW TLSSFAEKHY APFLLKPKAK VVVIFLFLGL LGVSLYGTTR VRDGLDLTDI VPRETREYDF IAAQFKYFSF YNMYIVTQKA DYPNIQHLLY DLHRSFSNVK YVMLEENKQL PKMWLHYFRD WLQGLQDAFD SDWETGKIMP NNYKNGSDDG VLAYKLLVQT GSRDKPIDIS QLTKQRLVDA DGIINPSAFY IYLTAWVSND PVAYAASQAN IRPHRPEWVH DKADYMPETR LRIPAAEPIE YAQFPFYLNG LRDTSDFVEA IEKVRTICSN YTSLGLSSYP NGYPFLFWEQ YIGLRHWLLL FISVVLACTF LVCAVFLLNP WTAGIIVMVL ALMTVELFGM MGLIGIKLSA VPVVILIASV GIGVEFTVHV ALAFLTAIGD KNRRAVLALE HMFAPVLDGA VSTLLGVLML AGSEFDFIVR YFFAVLAILT ILGVLNGLVL LPVLLSFFGP YPEVSPANGL NRLPTPSPEP PPSVVRFAMP PGHTHSGSDS SDSEYSSQTT VSGLSEELRH YEAQQGAGGP AHQVIVEATE NPVFAHSTVV HPESRHHPPS NPRQQPHLDS GSLPPGRQGQ QPRRDPPREG LWPPPYRPRR DAFEISTEGH SGPSNRARWG PRGARSHNPR NPASTAMGSS VPGYCQPITT VTASASVTVA VHPPPVPGPG RNPRGGLCPG YPETDHGLFE DPHVPFHVRC ERRDSKVEVI ELQDVECEER PRGSSSN //