GenomeNet

Database: UniProt
Entry: Q13635
LinkDB: Q13635
Original site: Q13635 
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-SEP-2021, entry version 211.
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=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=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   SMR; Q13635; -.
DR   BioGRID; 111699; 206.
DR   CORUM; Q13635; -.
DR   DIP; DIP-44940N; -.
DR   IntAct; Q13635; 78.
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   Antibodypedia; 4435; 692 antibodies.
DR   DNASU; 5727; -.
DR   Ensembl; ENST00000331920; ENSP00000332353; ENSG00000185920. [Q13635-1]
DR   Ensembl; ENST00000429896; ENSP00000414823; ENSG00000185920. [Q13635-4]
DR   Ensembl; ENST00000430669; ENSP00000410287; ENSG00000185920. [Q13635-3]
DR   Ensembl; ENST00000437951; ENSP00000389744; ENSG00000185920. [Q13635-2]
DR   GeneID; 5727; -.
DR   KEGG; hsa:5727; -.
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; Low tissue specificity.
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; 5 hits in 1018 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 233 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: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: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: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: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; 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
//
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