ID PTC1_HUMAN Reviewed; 1447 AA. AC Q13635; A3KBI9; E9PEJ8; Q13463; Q5R1U7; Q5R1U9; Q5R1V0; Q5VZC0; Q5VZC2; AC Q86XG7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 2. DT 29-MAY-2024, entry version 223. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L), VARIANTS BCNS1 PRO-175 AND RP PRO-ASN-ILE-815 INS, AND VARIANT 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., Bonifas J.M., RA Quinn A.G., Myers R.M., Cox D.R., Epstein E.H. Jr., 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., Chidambaram A., RA Gerrard B., Vorechovsky I., Bale A.E., Toftgard R., Dean M., RA 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., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., 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., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., 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., Rogers J., RA 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 (ISOFORM RP 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., Miyashita T.; RT "Identification and characterization of multiple isoforms of a murine and RT 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 project: RT 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 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 Patched1 in RT 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-selectin RT 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., Wang Y., RA Zhou C.Z., He L.; RT "Indian hedgehog mutations causing brachydactyly type A1 impair Hedgehog RT signal transduction at multiple levels."; RL Cell Res. 21:1343-1357(2011). RN [9] RP VARIANTS BCNS1 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 BCNS1 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., Chenevix-Trench G.; RT "Most germ-line mutations in the nevoid basal cell carcinoma syndrome lead RT to a premature termination of the PATCHED protein, and no genotype- RT phenotype correlations are evident."; RL Am. J. Hum. Genet. 60:21-26(1997). RN [11] RP VARIANT BCNS1 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 basal RT 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., Sampson J.R., RA 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 BCNS1 SER-376; VAL-1083 INS AND TRP-1114, AND VARIANT BCC RP 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., Bonifas J.M., RA Zhang X., Scott M.P., Epstein E.H. Jr.; RT "Identification of mutations in the human PATCHED gene in sporadic basal RT cell carcinomas and in patients with the basal cell nevus 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>3.0.co;2-7; 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 BCNS1 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., Tekin M., RA Stratton R.F., Sujansky E., Bale S.J., Muenke M.; RT "Mutations in PATCHED-1, the receptor for SONIC HEDGEHOG, are associated RT with holoprosencephaly."; RL Hum. Genet. 110:297-301(2002). RN [18] RP ERRATUM OF PUBMED:11941477. RA Ming J.E., Kaupas M.E., Roessler E., Brunner H.G., Golabi M., Tekin M., RA Stratton R.F., Sujansky E., Bale S.J., Muenke M.; RL Hum. Genet. 111:464-464(2002). RN [19] RP VARIANTS BCNS1 PRO-230 AND 505-PHE-LEU-506 DELINS LEU-ARG. 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 syndrome RT 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., 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 in RT 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 hedgehog CC (IHH) and desert hedgehog (DHH). Associates with the smoothened protein CC (SMO) to transduce the hedgehog's proteins signal. Seems to have a CC tumor suppressor function, as inactivation of this protein is probably CC a necessary, if not sufficient step for tumorigenesis. CC {ECO:0000269|PubMed:21537345}. CC -!- SUBUNIT: Interacts with SNX17 (PubMed:15769472). Interacts with IHH CC (PubMed:21537345). Interacts with G-protein coupled receptor GPR37L1 CC (By similarity). {ECO:0000250|UniProtKB:Q61115, CC ECO:0000269|PubMed:15769472, ECO:0000269|PubMed:21537345}. CC -!- INTERACTION: CC Q13635; P14635: CCNB1; NbExp=2; IntAct=EBI-8775406, EBI-495332; CC Q13635; Q4KMG0: CDON; NbExp=2; IntAct=EBI-8775406, EBI-7016840; CC Q13635; P25098: GRK2; NbExp=2; IntAct=EBI-8775406, EBI-3904795; CC Q13635; Q15465: SHH; NbExp=2; IntAct=EBI-8775406, EBI-11666886; CC Q13635; P46937: YAP1; NbExp=3; IntAct=EBI-8775406, EBI-1044059; CC Q13635; O35158: Cdon; Xeno; NbExp=2; IntAct=EBI-8775406, EBI-7016767; CC Q13635; P21146: GRK2; Xeno; NbExp=4; IntAct=EBI-8775406, EBI-1036401; CC Q13635-1; Q15465: SHH; NbExp=11; IntAct=EBI-13635488, EBI-11666886; CC Q13635-3; Q92624: APPBP2; NbExp=3; IntAct=EBI-14199621, EBI-743771; CC Q13635-3; Q8TD46-4: CD200R1; NbExp=3; IntAct=EBI-14199621, EBI-12824513; CC Q13635-3; P04233-2: CD74; NbExp=3; IntAct=EBI-14199621, EBI-12222807; CC Q13635-3; P11912: CD79A; NbExp=3; IntAct=EBI-14199621, EBI-7797864; CC Q13635-3; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-14199621, EBI-18304435; CC Q13635-3; P31937: HIBADH; NbExp=3; IntAct=EBI-14199621, EBI-11427100; CC Q13635-3; P42858: HTT; NbExp=3; IntAct=EBI-14199621, EBI-466029; CC Q13635-3; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-14199621, EBI-17640454; CC Q13635-3; P27105: STOM; NbExp=3; IntAct=EBI-14199621, EBI-1211440; CC Q13635-3; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-14199621, EBI-12345267; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q61115}; CC Multi-pass membrane protein {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 in CC tumor cells but not in normal skin. CC -!- DEVELOPMENTAL STAGE: In the embryo, found in all major target tissues CC of sonic hedgehog, such as the ventral neural tube, somites, and CC tissues surrounding the zone of polarizing activity 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-1426 CC promotes endocytosis and both proteasomal and lysosomal degradation. CC {ECO:0000250|UniProtKB:Q61115}. CC -!- DISEASE: Basal cell nevus syndrome 1 (BCNS1) [MIM:109400]: A form of CC basal cell nevus syndrome, a disease characterized by nevoid basal cell CC carcinomas and developmental abnormalities such as rib and craniofacial CC alterations, polydactyly, syndactyly, and spina bifida. In addition, CC the patients suffer from a multitude of tumors like fibromas of the CC ovaries and heart, cysts of the skin, jaws and mesentery, as well as CC medulloblastomas and meningiomas. BCNS1 inheritance is autosomal CC dominant. {ECO:0000269|PubMed:11231326, ECO:0000269|PubMed:15459969, CC ECO:0000269|PubMed:8658145, ECO:0000269|PubMed:8840969, CC ECO:0000269|PubMed:8981943, ECO:0000269|PubMed:9341860, CC ECO:0000269|PubMed:9620294}. Note=The disease may be caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Basal cell carcinoma (BCC) [MIM:605462]: A common malignant CC skin neoplasm that typically appears on hair-bearing skin, most CC commonly on sun-exposed areas. BCC is slow growing and rarely CC metastasizes, but has potentialities for local invasion and CC destruction. It usually develops as a flat, firm, pale area that is CC small, raised, pink or red, translucent, shiny, and waxy, and the area CC may bleed following minor injury. Tumor size can vary from a few CC millimeters to several centimeters in diameter. CC {ECO:0000269|PubMed:8658145, ECO:0000269|PubMed:9620294}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Holoprosencephaly 7 (HPE7) [MIM:610828]: A structural anomaly CC of the brain, in which the developing forebrain fails to correctly CC separate into right and left hemispheres. Holoprosencephaly is CC genetically heterogeneous and associated with several distinct facies CC and phenotypic variability. {ECO:0000269|PubMed:11941477, CC ECO:0000269|PubMed:17001668, ECO:0000269|PubMed:17096318}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the patched family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/100/PTCH"; 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 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 PDB; 6N7G; EM; 6.80 A; A/B/D/E=1-1305. DR PDB; 6N7H; EM; 3.60 A; A/B=1-1305. DR PDB; 6N7K; EM; 6.50 A; A/B/D/E=1-1305. DR PDB; 6OEU; EM; 3.50 A; A=1-1447. DR PDB; 6OEV; EM; 3.80 A; A=1-1447. DR PDB; 6RMG; EM; 3.40 A; A=1-1188. DR PDB; 6RTW; X-ray; 1.90 A; A=136-423. DR PDB; 6RTX; X-ray; 1.95 A; A=139-428. DR PDB; 6RTY; X-ray; 2.10 A; A=136-423. DR PDB; 6RVC; X-ray; 2.20 A; A/B/C=772-1023. DR PDB; 6RVD; EM; 3.50 A; A/B=1-1447. DR PDBsum; 6DMB; -. DR PDBsum; 6DMO; -. DR PDBsum; 6DMY; -. DR PDBsum; 6E1H; -. DR PDBsum; 6N7G; -. DR PDBsum; 6N7H; -. DR PDBsum; 6N7K; -. DR PDBsum; 6OEU; -. DR PDBsum; 6OEV; -. DR PDBsum; 6RMG; -. DR PDBsum; 6RTW; -. DR PDBsum; 6RTX; -. DR PDBsum; 6RTY; -. DR PDBsum; 6RVC; -. DR PDBsum; 6RVD; -. DR AlphaFoldDB; Q13635; -. DR EMDB; EMD-0355; -. DR EMDB; EMD-0356; -. DR EMDB; EMD-0358; -. DR EMDB; EMD-7795; -. DR EMDB; EMD-7796; -. DR EMDB; EMD-7963; -. DR EMDB; EMD-7964; -. DR EMDB; EMD-7968; -. DR EMDB; EMD-8955; -. DR SMR; Q13635; -. DR BioGRID; 111699; 285. DR CORUM; Q13635; -. DR DIP; DIP-44940N; -. DR IntAct; Q13635; 78. DR MINT; Q13635; -. DR STRING; 9606.ENSP00000332353; -. DR ChEMBL; CHEMBL5169150; -. DR TCDB; 2.A.6.6.13; the resistance-nodulation-cell division (rnd) superfamily. DR GlyCosmos; Q13635; 6 sites, No reported glycans. DR GlyGen; Q13635; 9 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q13635; -. DR PhosphoSitePlus; Q13635; -. DR SwissPalm; Q13635; -. DR BioMuta; PTCH1; -. DR DMDM; 160415977; -. DR EPD; Q13635; -. DR jPOST; Q13635; -. DR MassIVE; Q13635; -. DR PaxDb; 9606-ENSP00000332353; -. DR PeptideAtlas; Q13635; -. DR ProteomicsDB; 59627; -. [Q13635-1] DR ProteomicsDB; 59628; -. [Q13635-2] DR ProteomicsDB; 59629; -. [Q13635-3] DR ProteomicsDB; 59630; -. [Q13635-4] DR ABCD; Q13635; 2 sequenced antibodies. DR Antibodypedia; 4435; 787 antibodies from 40 providers. DR DNASU; 5727; -. DR Ensembl; ENST00000331920.11; ENSP00000332353.6; ENSG00000185920.19. [Q13635-1] DR Ensembl; ENST00000429896.6; ENSP00000414823.2; ENSG00000185920.19. [Q13635-4] DR Ensembl; ENST00000430669.6; ENSP00000410287.2; ENSG00000185920.19. [Q13635-3] DR Ensembl; ENST00000437951.6; ENSP00000389744.2; ENSG00000185920.19. [Q13635-2] DR Ensembl; ENST00000692981.1; ENSP00000510238.1; ENSG00000185920.19. [Q13635-4] DR Ensembl; ENST00000711046.1; ENSP00000518556.1; ENSG00000185920.19. [Q13635-3] DR GeneID; 5727; -. DR KEGG; hsa:5727; -. DR MANE-Select; ENST00000331920.11; ENSP00000332353.6; NM_000264.5; NP_000255.2. DR UCSC; uc004avk.5; human. [Q13635-1] DR AGR; HGNC:9585; -. DR CTD; 5727; -. DR DisGeNET; 5727; -. DR GeneCards; PTCH1; -. DR GeneReviews; PTCH1; -. DR HGNC; HGNC:9585; PTCH1. DR HPA; ENSG00000185920; Tissue enhanced (cervix). 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; 2353; Schilbach-Rott syndrome. DR Orphanet; 220386; Semilobar holoprosencephaly. DR Orphanet; 280195; Septopreoptic holoprosencephaly. DR PharmGKB; PA33937; -. DR VEuPathDB; HostDB:ENSG00000185920; -. DR eggNOG; KOG1935; Eukaryota. DR GeneTree; ENSGT00940000159011; -. DR HOGENOM; CLU_002506_1_0_1; -. DR InParanoid; Q13635; -. DR OMA; HLYDTEW; -. DR OrthoDB; 1219406at2759; -. DR PhylomeDB; Q13635; -. DR TreeFam; TF106489; -. DR PathwayCommons; Q13635; -. 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 BioGRID-ORCS; 5727; 25 hits in 1167 CRISPR screens. DR ChiTaRS; PTCH1; human. DR GeneWiki; PTCH1; -. DR GenomeRNAi; 5727; -. DR Pharos; Q13635; Tbio. DR PRO; PR:Q13635; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q13635; Protein. DR Bgee; ENSG00000185920; Expressed in tibia and 197 other cell types or tissues. DR ExpressionAtlas; Q13635; baseline and differential. DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB. 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:0043231; C:intracellular membrane-bounded organelle; IDA:BHF-UCL. DR GO; GO:0030496; C:midbody; 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: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:0021904; P:dorsal/ventral neural tube patterning; 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:0072205; P:metanephric collecting duct development; IEP:UniProtKB. 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:0010839; P:negative regulation of keratinocyte 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:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl. 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:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; 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:0010157; P:response to chlorate; 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:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0048745; P:smooth muscle tissue development; IEP:UniProtKB. DR GO; GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB. DR GO; GO:0061053; P:somite development; IMP:BHF-UCL. DR GO; GO:0007286; P:spermatid development; IEA:Ensembl. DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IEA:Ensembl. DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl. DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2. DR InterPro; IPR003392; Ptc/Disp. DR InterPro; IPR000731; SSD. DR InterPro; IPR004766; TM_rcpt_patched. DR NCBIfam; TIGR00918; 2A060602; 1. DR PANTHER; PTHR46022; PROTEIN PATCHED; 1. DR PANTHER; PTHR46022:SF5; PROTEIN PATCHED HOMOLOG 1; 1. DR Pfam; PF02460; Patched; 2. DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2. DR PROSITE; PS50156; SSD; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disease variant; KW Glycoprotein; Holoprosencephaly; Isopeptide bond; Membrane; Phosphoprotein; KW Receptor; Reference proteome; Transmembrane; Transmembrane helix; KW Tumor suppressor; Ubl conjugation. FT CHAIN 1..1447 FT /note="Protein patched homolog 1" FT /id="PRO_0000205964" FT TOPO_DOM 1..100 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 101..121 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 122..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..748 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 749..769 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 770..1027 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1028..1048 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1049..1055 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1056..1076 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1077..1083 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1084..1104 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1105..1121 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1122..1141 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1142..1154 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1155..1175 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1176..1447 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 438..598 FT /note="SSD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1189..1234 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1270..1360 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1193..1207 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1214..1234 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1195 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q61115" FT MOD_RES 1197 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61115" 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 875 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1000 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CROSSLNK 1426 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q61115" FT VAR_SEQ 1..66 FT /note="MASAGNAAEPQDRGGGGSGCIGAPGRPAGGGRRRRTGGLRRAAAPDRDYLHR FT PSYCDAAFALEQIS -> MELLNRNRLVIVSPRCTPPKASGGPARRGFYTFRSFCKDGG FT GGEEEEENGGEEKDDRGDKETRSD (in isoform L')" FT /evidence="ECO:0000303|PubMed:15780749" FT /id="VSP_041369" FT VAR_SEQ 2..152 FT /note="Missing (in isoform S)" FT /evidence="ECO:0000303|PubMed:15780749, FT ECO:0000303|PubMed:17310997, ECO:0000303|PubMed:8647801" FT /id="VSP_041370" FT VAR_SEQ 2..67 FT /note="Missing (in isoform M)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:15780749" FT /id="VSP_041371" FT VARIANT 175 FT /note="L -> P (in BCNS1)" FT /evidence="ECO:0000269|PubMed:8658145" FT /id="VAR_007843" FT VARIANT 230 FT /note="T -> P (in BCNS1)" FT /evidence="ECO:0000269|PubMed:15459969" FT /id="VAR_020845" FT VARIANT 376 FT /note="F -> S (in BCNS1)" FT /evidence="ECO:0000269|PubMed:9620294" FT /id="VAR_007844" FT VARIANT 393 FT /note="A -> T (in HPE7; dbSNP:rs199476091)" FT /evidence="ECO:0000269|PubMed:11941477" FT /id="VAR_032952" FT VARIANT 443 FT /note="A -> G (in HPE7; dbSNP:rs878853845)" FT /evidence="ECO:0000269|PubMed:17001668" FT /id="VAR_032953" FT VARIANT 505..506 FT /note="FL -> LR (in BCNS1)" FT /evidence="ECO:0000269|PubMed:15459969" FT /id="VAR_020846" FT VARIANT 509 FT /note="G -> R (in BCNS1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:8840969" FT /id="VAR_010974" FT VARIANT 509 FT /note="G -> V (in BCNS1)" FT /evidence="ECO:0000269|PubMed:8840969" FT /id="VAR_010975" FT VARIANT 513 FT /note="D -> Y (in BCNS1)" FT /evidence="ECO:0000269|PubMed:8981943" FT /id="VAR_010976" FT VARIANT 728 FT /note="T -> M (in HPE7; dbSNP:rs115556836)" FT /evidence="ECO:0000269|PubMed:11941477, FT ECO:0000269|PubMed:17096318" FT /id="VAR_032954" FT VARIANT 751 FT /note="V -> G (in HPE7)" FT /evidence="ECO:0000269|PubMed:17001668" FT /id="VAR_032955" FT VARIANT 815 FT /note="I -> IPNI (in BCNS1)" FT /evidence="ECO:0000269|PubMed:8658145" FT /id="VAR_007845" FT VARIANT 816 FT /note="Missing (in BCNS1)" FT /evidence="ECO:0000269|PubMed:8840969" FT /id="VAR_010977" FT VARIANT 827 FT /note="S -> G (in HPE7; dbSNP:rs199476092)" FT /evidence="ECO:0000269|PubMed:11941477" FT /id="VAR_032956" FT VARIANT 829 FT /note="V -> M (in squamous cell carcinoma; FT dbSNP:rs201125580)" FT /evidence="ECO:0000269|PubMed:11286632" FT /id="VAR_010978" FT VARIANT 908 FT /note="V -> G (in HPE7; dbSNP:rs199476093)" FT /evidence="ECO:0000269|PubMed:17001668" FT /id="VAR_032957" FT VARIANT 1052 FT /note="T -> M (in HPE7; dbSNP:rs138911275)" FT /evidence="ECO:0000269|PubMed:11941477, FT ECO:0000269|PubMed:17001668" FT /id="VAR_032958" FT VARIANT 1069 FT /note="G -> R (in BCNS1)" FT /evidence="ECO:0000269|PubMed:8981943" FT /id="VAR_010979" FT VARIANT 1083 FT /note="V -> VV (in BCNS1)" FT /evidence="ECO:0000269|PubMed:9620294" FT /id="VAR_007846" FT VARIANT 1114 FT /note="R -> W (in BCNS1 and BCC; dbSNP:rs587776689)" FT /evidence="ECO:0000269|PubMed:9620294" FT /id="VAR_007847" FT VARIANT 1132 FT /note="S -> P (in BCNS1; dbSNP:rs878853856)" FT /evidence="ECO:0000269|PubMed:11231326" FT /id="VAR_010980" FT VARIANT 1132 FT /note="S -> Y (in BCNS1)" FT /evidence="ECO:0000269|PubMed:8840969" FT /id="VAR_010981" FT VARIANT 1195 FT /note="T -> S (in dbSNP:rs2236405)" FT /id="VAR_020440" FT VARIANT 1242 FT /note="E -> K (in squamous cell carcinoma; FT dbSNP:rs779417284)" FT /evidence="ECO:0000269|PubMed:11286632" FT /id="VAR_010982" FT VARIANT 1282 FT /note="P -> L (in dbSNP:rs2227968)" FT /id="VAR_020847" FT VARIANT 1315 FT /note="P -> L (in dbSNP:rs357564)" FT /evidence="ECO:0000269|PubMed:10200051, FT ECO:0000269|PubMed:10874314, ECO:0000269|PubMed:8647801, FT ECO:0000269|PubMed:8658145" FT /id="VAR_010983" FT VARIANT 1438 FT /note="E -> D (in BCNS1)" FT /evidence="ECO:0000269|PubMed:9341860" FT /id="VAR_010984" FT CONFLICT 1109 FT /note="G -> S (in Ref. 2; AAC50496)" FT /evidence="ECO:0000305" FT CONFLICT 1144 FT /note="E -> D (in Ref. 2; AAC50496)" FT /evidence="ECO:0000305" FT CONFLICT 1175 FT /note="L -> W (in Ref. 2; AAC50496)" FT /evidence="ECO:0000305" FT CONFLICT 1283 FT /note="R -> K (in Ref. 2; AAC50496)" FT /evidence="ECO:0000305" FT CONFLICT 1309 FT /note="E -> K (in Ref. 2; AAC50496)" FT /evidence="ECO:0000305" FT CONFLICT 1353 FT /note="A -> T (in Ref. 2; AAC50496)" FT /evidence="ECO:0000305" FT HELIX 48..51 FT /evidence="ECO:0007829|PDB:6RMG" FT TURN 53..55 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 58..67 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 74..77 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 78..96 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 99..113 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 114..118 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 125..128 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 135..146 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 155..164 FT /evidence="ECO:0007829|PDB:6RTW" FT HELIX 172..186 FT /evidence="ECO:0007829|PDB:6RTW" FT STRAND 189..192 FT /evidence="ECO:0007829|PDB:6RTW" FT STRAND 195..198 FT /evidence="ECO:0007829|PDB:6RTW" FT HELIX 199..202 FT /evidence="ECO:0007829|PDB:6RTW" FT STRAND 205..210 FT /evidence="ECO:0007829|PDB:6RTW" FT HELIX 214..223 FT /evidence="ECO:0007829|PDB:6RTW" FT HELIX 231..234 FT /evidence="ECO:0007829|PDB:6RTW" FT HELIX 236..241 FT /evidence="ECO:0007829|PDB:6RTW" FT STRAND 249..253 FT /evidence="ECO:0007829|PDB:6RMG" FT TURN 256..258 FT /evidence="ECO:0007829|PDB:6RTW" FT HELIX 261..269 FT /evidence="ECO:0007829|PDB:6RTW" FT TURN 270..272 FT /evidence="ECO:0007829|PDB:6RTW" FT HELIX 276..285 FT /evidence="ECO:0007829|PDB:6RTW" FT TURN 288..293 FT /evidence="ECO:0007829|PDB:6RTW" FT STRAND 299..301 FT /evidence="ECO:0007829|PDB:6OEU" FT TURN 309..312 FT /evidence="ECO:0007829|PDB:6RTW" FT HELIX 319..323 FT /evidence="ECO:0007829|PDB:6RTW" FT TURN 332..334 FT /evidence="ECO:0007829|PDB:6RTW" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 339..342 FT /evidence="ECO:0007829|PDB:6RTW" FT STRAND 343..345 FT /evidence="ECO:0007829|PDB:6RTW" FT STRAND 347..349 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 354..356 FT /evidence="ECO:0007829|PDB:6RTW" FT STRAND 358..366 FT /evidence="ECO:0007829|PDB:6RTW" FT HELIX 369..376 FT /evidence="ECO:0007829|PDB:6RTW" FT HELIX 380..382 FT /evidence="ECO:0007829|PDB:6RTW" FT STRAND 383..385 FT /evidence="ECO:0007829|PDB:6RVD" FT HELIX 389..409 FT /evidence="ECO:0007829|PDB:6RTW" FT STRAND 413..415 FT /evidence="ECO:0007829|PDB:6OEU" FT STRAND 416..422 FT /evidence="ECO:0007829|PDB:6RTW" FT HELIX 426..434 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 439..457 FT /evidence="ECO:0007829|PDB:6RMG" FT TURN 462..464 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 467..490 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 497..499 FT /evidence="ECO:0007829|PDB:6RMG" FT TURN 500..502 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 503..511 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 512..514 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 515..523 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 526..528 FT /evidence="ECO:0007829|PDB:6RMG" FT TURN 532..534 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 536..543 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 546..553 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 556..561 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 568..573 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 576..590 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 592..604 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 732..738 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 741..744 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 747..769 FT /evidence="ECO:0007829|PDB:6RMG" FT TURN 777..780 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 783..785 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 788..796 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 801..809 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 812..814 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 816..825 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 826..828 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 829..832 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 836..838 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 844..864 FT /evidence="ECO:0007829|PDB:6RVC" FT STRAND 869..871 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 873..876 FT /evidence="ECO:0007829|PDB:6E1H" FT HELIX 878..887 FT /evidence="ECO:0007829|PDB:6RVC" FT STRAND 893..895 FT /evidence="ECO:0007829|PDB:6RVC" FT HELIX 899..903 FT /evidence="ECO:0007829|PDB:6RVC" FT HELIX 910..912 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 916..918 FT /evidence="ECO:0007829|PDB:6RVC" FT HELIX 919..929 FT /evidence="ECO:0007829|PDB:6RVC" FT HELIX 931..934 FT /evidence="ECO:0007829|PDB:6RVC" FT TURN 957..959 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 972..978 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 984..1004 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 1007..1012 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 1013..1016 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 1017..1019 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 1020..1022 FT /evidence="ECO:0007829|PDB:6E1H" FT HELIX 1024..1047 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 1051..1074 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 1081..1102 FT /evidence="ECO:0007829|PDB:6RMG" FT TURN 1103..1106 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 1108..1110 FT /evidence="ECO:0007829|PDB:6E1H" FT HELIX 1111..1120 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 1124..1137 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 1138..1140 FT /evidence="ECO:0007829|PDB:6RMG" FT STRAND 1142..1145 FT /evidence="ECO:0007829|PDB:6OEU" FT STRAND 1146..1148 FT /evidence="ECO:0007829|PDB:6RMG" FT TURN 1149..1152 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 1153..1167 FT /evidence="ECO:0007829|PDB:6RMG" FT HELIX 1170..1177 FT /evidence="ECO:0007829|PDB:6RMG" 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 //