PTC1_HUMAN
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 03-AUG-2022, entry version 214.
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), 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., 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 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., 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 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 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 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., 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 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., 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 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 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=4; 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=4; 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 (BCNS) [MIM:109400]: An autosomal
CC dominant disease characterized by nevoid basal cell carcinomas and
CC developmental abnormalities such as rib and craniofacial alterations,
CC polydactyly, syndactyly, and spina bifida. In addition, the patients
CC suffer from a multitude of tumors like basal cell carcinomas, fibromas
CC of the ovaries and heart, cysts of the skin, jaws and mesentery, as
CC well as 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 variants affecting the gene represented in
CC 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="http://atlasgeneticsoncology.org/Genes/PTCHID100.html";
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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 SMR; Q13635; -.
DR BioGRID; 111699; 283.
DR CORUM; Q13635; -.
DR DIP; DIP-44940N; -.
DR IntAct; Q13635; 79.
DR MINT; Q13635; -.
DR STRING; 9606.ENSP00000332353; -.
DR TCDB; 2.A.6.6.13; the resistance-nodulation-cell division (rnd) superfamily.
DR GlyGen; Q13635; 8 sites.
DR iPTMnet; Q13635; -.
DR PhosphoSitePlus; Q13635; -.
DR BioMuta; PTCH1; -.
DR DMDM; 160415977; -.
DR EPD; Q13635; -.
DR jPOST; Q13635; -.
DR MassIVE; Q13635; -.
DR PaxDb; Q13635; -.
DR PeptideAtlas; Q13635; -.
DR PRIDE; 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; 706 antibodies from 40 providers.
DR DNASU; 5727; -.
DR Ensembl; ENST00000331920.11; ENSP00000332353.6; ENSG00000185920.18. [Q13635-1]
DR Ensembl; ENST00000429896.6; ENSP00000414823.2; ENSG00000185920.18. [Q13635-4]
DR Ensembl; ENST00000430669.6; ENSP00000410287.2; ENSG00000185920.18. [Q13635-3]
DR Ensembl; ENST00000437951.6; ENSP00000389744.2; ENSG00000185920.18. [Q13635-2]
DR Ensembl; ENST00000692981.1; ENSP00000510238.1; ENSG00000185920.18. [Q13635-4]
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 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; LTKECWF; -.
DR OrthoDB; 1190129at2759; -.
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; 13 hits in 1079 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 195 other tissues.
DR ExpressionAtlas; Q13635; baseline and differential.
DR Genevisible; Q13635; HS.
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: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: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: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: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: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: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 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 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 BCNS; sporadic BCC)"
FT /evidence="ECO:0000269|PubMed:8658145"
FT /id="VAR_007843"
FT VARIANT 230
FT /note="T -> P (in BCNS)"
FT /evidence="ECO:0000269|PubMed:15459969"
FT /id="VAR_020845"
FT VARIANT 376
FT /note="F -> S (in BCNS)"
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 BCNS)"
FT /id="VAR_020846"
FT VARIANT 509
FT /note="G -> R (in BCNS; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:8840969"
FT /id="VAR_010974"
FT VARIANT 509
FT /note="G -> V (in BCNS)"
FT /evidence="ECO:0000269|PubMed:8840969"
FT /id="VAR_010975"
FT VARIANT 513
FT /note="D -> Y (in BCNS)"
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 BCNS)"
FT /id="VAR_007845"
FT VARIANT 816
FT /note="Missing (in BCNS)"
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 BCNS)"
FT /evidence="ECO:0000269|PubMed:8981943"
FT /id="VAR_010979"
FT VARIANT 1083
FT /note="V -> VV (in BCNS)"
FT /evidence="ECO:0000269|PubMed:9620294"
FT /id="VAR_007846"
FT VARIANT 1114
FT /note="R -> W (in BCNS and BCC; dbSNP:rs587776689)"
FT /evidence="ECO:0000269|PubMed:9620294"
FT /id="VAR_007847"
FT VARIANT 1132
FT /note="S -> P (in BCNS; dbSNP:rs878853856)"
FT /evidence="ECO:0000269|PubMed:11231326"
FT /id="VAR_010980"
FT VARIANT 1132
FT /note="S -> Y (in BCNS)"
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 BCNS; sporadic NBCCS)"
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
