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High affinity nerve growth factor receptor (EC 2.7.10.1) (Neurotrophic tyrosine kinase receptor type 1) (TRK1-transforming tyrosine kinase protein) (Tropomyosin-related kinase A) (Tyrosine kinase receptor) (Tyrosine kinase receptor A) (Trk-A) (gp140trk) (p140-TrkA)

 NTRK1_HUMAN             Reviewed;         796 AA.
P04629; B2R6T5; B7ZM34; P08119; Q15655; Q15656; Q5D056; Q5VZS2;
Q7Z5C3; Q9UIU7;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
02-MAY-2006, sequence version 4.
30-AUG-2017, entry version 226.
RecName: Full=High affinity nerve growth factor receptor;
EC=2.7.10.1 {ECO:0000269|PubMed:1281417, ECO:0000269|PubMed:2927393};
AltName: Full=Neurotrophic tyrosine kinase receptor type 1;
AltName: Full=TRK1-transforming tyrosine kinase protein;
AltName: Full=Tropomyosin-related kinase A;
AltName: Full=Tyrosine kinase receptor;
AltName: Full=Tyrosine kinase receptor A;
Short=Trk-A;
AltName: Full=gp140trk {ECO:0000303|PubMed:2927393};
AltName: Full=p140-TrkA;
Flags: Precursor;
Name=NTRK1;
Synonyms=MTC, TRK {ECO:0000303|PubMed:2927393},
TRKA {ECO:0000303|PubMed:9290260};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TRKA-I), CATALYTIC ACTIVITY,
PHOSPHORYLATION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
TISSUE=Colon;
PubMed=2927393; DOI=10.1128/MCB.9.1.24;
Martin-Zanca D., Oskam R., Mitra G., Copeland T.D., Barbacid M.;
"Molecular and biochemical characterization of the human trk proto-
oncogene.";
Mol. Cell. Biol. 9:24-33(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7823156;
Shelton D.L., Sutherland J., Gripp J., Camerato T., Armanini M.P.,
Phillips H.S., Carroll K., Spencer S.D., Levinson A.D.;
"Human trks: molecular cloning, tissue distribution, and expression of
extracellular domain immunoadhesins.";
J. Neurosci. 15:477-491(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9290260; DOI=10.1007/BF02766957;
Indo Y., Mardy S., Tsuruta M., Karim M.A., Matsuda I.;
"Structure and organization of the human TRKA gene encoding a high
affinity receptor for nerve growth factor.";
Jpn. J. Hum. Genet. 42:343-351(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TRKA-II), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-175 (ISOFORM 3).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS TRKA-I AND TRKA-II).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
PubMed=15870692; DOI=10.1038/sj.onc.1208697;
Fujimoto M., Kitazawa R., Maeda S., Kitazawa S.;
"Methylation adjacent to negatively regulating AP-1 site reactivates
TrkA gene expression during cancer progression.";
Oncogene 24:5108-5118(2005).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 399-796, AND CHROMOSOMAL TRANSLOCATION
WITH TPM3.
PubMed=2869410; DOI=10.1038/319743a0;
Martin-Zanca D., Hughes S.H., Barbacid M.;
"A human oncogene formed by the fusion of truncated tropomyosin and
protein tyrosine kinase sequences.";
Nature 319:743-748(1986).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 399-796.
PubMed=2966065;
Kozma S.C., Redmond S.M.S., Saurer S.M., Groner B., Hynes N.E.;
"Activation of the receptor kinase domain of the trk oncogene by
recombination with two different cellular sequences.";
EMBO J. 7:147-154(1988).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 399-796, AND CHROMOSOMAL TRANSLOCATION
WITH TFG.
PubMed=7565764; DOI=10.1128/MCB.15.11.6118;
Greco A., Mariani C., Miranda C., Lupas A., Pagliardini S., Pomati M.,
Pierotti M.A.;
"The DNA rearrangement that generates the TRK-T3 oncogene involves a
novel gene on chromosome 3 whose product has a potential coiled-coil
domain.";
Mol. Cell. Biol. 15:6118-6127(1995).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 486-796, AND CHROMOSOMAL REARRANGEMENT
WITH TPR.
PubMed=1532241;
Greco A., Pierotti M.A., Bongarzone I., Pagliardini S., Lanzi C.,
Della Porta G.;
"TRK-T1 is a novel oncogene formed by the fusion of TPR and TRK genes
in human papillary thyroid carcinomas.";
Oncogene 7:237-242(1992).
[12]
FUNCTION AS RECEPTOR FOR NGF.
PubMed=1850821; DOI=10.1038/350678a0;
Hempstead B.L., Martin-Zanca D., Kaplan D.R., Parada L.F., Chao M.V.;
"High-affinity NGF binding requires coexpression of the trk proto-
oncogene and the low-affinity NGF receptor.";
Nature 350:678-683(1991).
[13]
FUNCTION IN NGF SIGNALING, AND IDENTIFICATION AS THE HIGH AFFINITY NGF
RECEPTOR.
PubMed=1849459; DOI=10.1016/0092-8674(91)90419-Y;
Klein R., Jing S., Nanduri V., O'Rourke E., Barbacid M.;
"The trk proto-oncogene encodes a receptor for nerve growth factor.";
Cell 65:189-197(1991).
[14]
FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, PHOSPHORYLATION, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF LYS-544.
PubMed=1281417; DOI=10.1016/0896-6273(92)90066-M;
Jing S., Tapley P., Barbacid M.;
"Nerve growth factor mediates signal transduction through trk
homodimer receptors.";
Neuron 9:1067-1079(1992).
[15]
ALTERNATIVE SPLICING (ISOFORMS TRKA-I AND TRKA-II), FUNCTION IN CELL
SURVIVAL, NGF-BINDING, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
PubMed=8325889;
Barker P.A., Lomen-Hoerth C., Gensch E.M., Meakin S.O., Glass D.J.,
Shooter E.M.;
"Tissue-specific alternative splicing generates two isoforms of the
trkA receptor.";
J. Biol. Chem. 268:15150-15157(1993).
[16]
PHOSPHORYLATION AT TYR-791, INTERACTION WITH PLCG1, AND MUTAGENESIS OF
TYR-791.
PubMed=7510697;
Loeb D.M., Stephens R.M., Copeland T.D., Kaplan D.R., Greene L.A.;
"A Trk nerve growth factor (NGF) receptor point mutation affecting
interaction with phospholipase C-gamma 1 abolishes NGF-promoted
peripherin induction but not neurite outgrowth.";
J. Biol. Chem. 269:8901-8910(1994).
[17]
FUNCTION IN NEURONAL DIFFERENTIATION, FUNCTION IN PHOSPHORYLATION OF
SHC1 AND PLCG1, INTERACTION WITH SHC1, MUTAGENESIS OF TYR-496; LYS-544
AND TYR-791, AND PHOSPHORYLATION AT TYR-496 AND TYR-791.
PubMed=8155326; DOI=10.1016/0896-6273(94)90223-2;
Stephens R.M., Loeb D.M., Copeland T.D., Pawson T., Greene L.A.,
Kaplan D.R.;
"Trk receptors use redundant signal transduction pathways involving
SHC and PLC-gamma 1 to mediate NGF responses.";
Neuron 12:691-705(1994).
[18]
FUNCTION IN NF-KAPPA-B ACTIVATION, AND INTERACTION WITH SQSTM1.
PubMed=11244088; DOI=10.1074/jbc.C000869200;
Wooten M.W., Seibenhener M.L., Mamidipudi V., Diaz-Meco M.T.,
Barker P.A., Moscat J.;
"The atypical protein kinase C-interacting protein p62 is a scaffold
for NF-kappaB activation by nerve growth factor.";
J. Biol. Chem. 276:7709-7712(2001).
[19]
FUNCTION IN NEURONAL CELL PROLIFERATION AND DIFFERENTIATION, FUNCTION
IN SIGNALING CASCADE ACTIVATION, NGF-BINDING, SUBCELLULAR LOCATION,
ALTERNATIVE SPLICING (ISOFORM TRKA-III), CHARACTERIZATION OF ISOFORM
TRKA-III, PHOSPHORYLATION AT TYR-496; TYR-680; TYR-681 AND TYR-791,
INTERACTION WITH FRS2; GRB2; PIK3R1; PLCG1; SHC1, GLYCOSYLATION,
TISSUE SPECIFICITY, AND INDUCTION BY HYPOXIA.
PubMed=15488758; DOI=10.1016/j.ccr.2004.09.011;
Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A.,
Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A.,
Mackay A.R.;
"TrkA alternative splicing: a regulated tumor-promoting switch in
human neuroblastoma.";
Cancer Cell 6:347-360(2004).
[20]
INTERACTION WITH SORT1, AND ENZYME REGULATION.
PubMed=21102451; DOI=10.1038/nn.2689;
Vaegter C.B., Jansen P., Fjorback A.W., Glerup S., Skeldal S.,
Kjolby M., Richner M., Erdmann B., Nyengaard J.R., Tessarollo L.,
Lewin G.R., Willnow T.E., Chao M.V., Nykjaer A.;
"Sortilin associates with Trk receptors to enhance anterograde
transport and neurotrophin signaling.";
Nat. Neurosci. 14:54-61(2011).
[21]
STRUCTURE BY NMR OF 489-500.
PubMed=8524391; DOI=10.1038/378584a0;
Zhou M.-M., Ravichandran K.S., Olejniczak E.F., Petros A.M.,
Meadows R.P., Sattler M., Harlan J.E., Wade W.S., Burakoff S.J.,
Fesik S.W.;
"Structure and ligand recognition of the phosphotyrosine binding
domain of Shc.";
Nature 378:584-592(1995).
[22]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 278-386, AND DISULFIDE
BONDS.
PubMed=10388563; DOI=10.1006/jmbi.1999.2816;
Ultsch M.H., Wiesmann C., Simmons L.C., Henrich J., Yang M.,
Reilly D., Bass S.H., de Vos A.M.;
"Crystal structures of the neurotrophin-binding domain of TrkA, TrkB
and TrkC.";
J. Mol. Biol. 290:149-159(1999).
[23]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 282-382 IN COMPLEX WITH NGF,
SUBUNIT, AND DISULFIDE BONDS.
PubMed=10490030; DOI=10.1038/43705;
Wiesmann C., Ultsch M.H., Bass S.H., de Vos A.M.;
"Crystal structure of nerve growth factor in complex with the ligand-
binding domain of the TrkA receptor.";
Nature 401:184-188(1999).
[24]
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 36-382 IN COMPLEX WITH NGF,
HOMODIMERIZATION, SUBUNIT, SUBCELLULAR LOCATION, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-95; ASN-121; ASN-188; ASN-262; ASN-281 AND
ASN-358.
PubMed=17196528; DOI=10.1016/j.neuron.2006.09.034;
Wehrman T., He X., Raab B., Dukipatti A., Blau H., Garcia K.C.;
"Structural and mechanistic insights into nerve growth factor
interactions with the TrkA and p75 receptors.";
Neuron 53:25-38(2007).
[25]
VARIANT CIPA ARG-577.
PubMed=8696348; DOI=10.1038/ng0896-485;
Indo Y., Tsuruta M., Hayashida Y., Karim M.A., Ohta K., Kawano T.,
Mitsubuchi H., Tonoki H., Awaya Y., Matsuda I.;
"Mutations in the TRKA/NGF receptor gene in patients with congenital
insensitivity to pain with anhidrosis.";
Nat. Genet. 13:485-488(1996).
[26]
VARIANT CIPA PRO-780.
PubMed=10090906; DOI=10.1086/302319;
Greco A., Villa R., Tubino B., Romano L., Penso D., Pierotti M.A.;
"A novel NTRK1 mutation associated with congenital insensitivity to
pain with anhidrosis.";
Am. J. Hum. Genet. 64:1207-1210(1999).
[27]
VARIANTS CIPA PRO-213; TRP-649 AND SER-714, AND VARIANTS SER-85;
TYR-604 AND VAL-613.
PubMed=10330344; DOI=10.1086/302422;
Mardy S., Miura Y., Endo F., Matsuda I., Sztriha L., Frossard P.,
Moosa A., Ismail E.A.R., Macaya A., Andria G., Toscano E., Gibson W.,
Graham G.E., Indo Y.;
"Congenital insensitivity to pain with anhidrosis: novel mutations in
the TRKA (NTRK1) gene encoding a high-affinity receptor for nerve
growth factor.";
Am. J. Hum. Genet. 64:1570-1579(1999).
[28]
VARIANTS TYR-604; VAL-613 AND GLN-780.
PubMed=10443680; DOI=10.1210/jcem.84.8.5901;
Gimm O., Greco A., Hoang-Vu C., Dralle H., Pierotti M.A., Eng C.;
"Mutation analysis reveals novel sequence variants in NTRK1 in
sporadic human medullary thyroid carcinoma.";
J. Clin. Endocrinol. Metab. 84:2784-2787(1999).
[29]
VARIANT CIPA VAL-587.
PubMed=10233776; DOI=10.1046/j.1523-1747.1999.00569.x;
Yotsumoto S., Setoyama M., Hozumi H., Mizoguchi S., Fukumaru S.,
Kobayashi K., Saheki T., Kanzaki T.;
"A novel point mutation affecting the tyrosine kinase domain of the
TRKA gene in a family with congenital insensitivity to pain with
anhidrosis.";
J. Invest. Dermatol. 112:810-814(1999).
[30]
VARIANTS TYR-604 AND VAL-613.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[31]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[32]
VARIANT CIPA LEU-695, AND VARIANT VAL-613.
TISSUE=Peripheral blood;
PubMed=10861667;
DOI=10.1002/1096-8628(20000619)92:5<353::AID-AJMG12>3.0.CO;2-C;
Shatzky S., Moses S., Levy J., Pinsk V., Hershkovitz E., Herzog L.,
Shorer Z., Luder A., Parvari R.;
"Congenital insensitivity to pain with anhidrosis (CIPA) in Israeli-
Bedouins: genetic heterogeneity, novel mutations in the TRKA/NGF
receptor gene, clinical findings, and results of nerve conduction
studies.";
Am. J. Med. Genet. 92:353-360(2000).
[33]
VARIANTS CIPA PRO-93; ARG-522; ARG-577; CYS-654 AND TYR-674.
PubMed=10982191; DOI=10.1007/s004390051018;
Miura Y., Mardy S., Awaya Y., Nihei K., Endo F., Matsuda I., Indo Y.;
"Mutation and polymorphism analysis of the TRKA (NTRK1) gene encoding
a high-affinity receptor for nerve growth factor in congenital
insensitivity to pain with anhidrosis (CIPA) families.";
Hum. Genet. 106:116-124(2000).
[34]
VARIANT CIPA ARG-577.
PubMed=10567924;
DOI=10.1002/(SICI)1097-4652(200001)182:1<127::AID-JCP14>3.0.CO;2-0;
Greco A., Villa R., Fusetti L., Orlandi R., Pierotti M.A.;
"The Gly571Arg mutation, associated with the autonomic and sensory
disorder congenital insensitivity to pain with anhidrosis, causes the
inactivation of the NTRK1/nerve growth factor receptor.";
J. Cell. Physiol. 182:127-133(2000).
[35]
VARIANT CIPA CYS-359, AND VARIANTS TYR-604 AND VAL-613.
PubMed=11310631; DOI=10.1002/ana.103;
Houlden H., King R.H., Hashemi-Nejad A., Wood N.W., Mathias C.J.,
Reilly M., Thomas P.K.;
"A novel TRK A (NTRK1) mutation associated with hereditary sensory and
autonomic neuropathy type V.";
Ann. Neurol. 49:521-525(2001).
[36]
CHARACTERIZATION OF VARIANTS CIPA PRO-93; PRO-213; ARG-522; ARG-577;
TRP-649; CYS-654 AND SER-714, AND CHARACTERIZATION OF VARIANTS SER-85;
TYR-604; VAL-613 AND TYR-674.
PubMed=11159935; DOI=10.1093/hmg/10.3.179;
Mardy S., Miura Y., Endo F., Matsuda I., Indo Y.;
"Congenital insensitivity to pain with anhidrosis (CIPA): effect of
TRKA (NTRK1) missense mutations on autophosphorylation of the receptor
tyrosine kinase for nerve growth factor.";
Hum. Mol. Genet. 10:179-188(2001).
[37]
VARIANTS [LARGE SCALE ANALYSIS] ARG-80; VAL-107; MET-237; GLY-238;
GLY-260; GLN-444; CYS-452; THR-566; TYR-604; VAL-613; GLN-780 AND
ILE-790.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[38]
VARIANTS CIPA SER-572 AND ARG-717.
PubMed=18077166; DOI=10.1016/j.nmd.2007.10.005;
Huehne K., Zweier C., Raab K., Odent S., Bonnaure-Mallet M.,
Sixou J.L., Landrieu P., Goizet C., Sarlangue J., Baumann M.,
Eggermann T., Rauch A., Ruppert S., Stettner G.M., Rautenstrauss B.;
"Novel missense, insertion and deletion mutations in the neurotrophic
tyrosine kinase receptor type 1 gene (NTRK1) associated with
congenital insensitivity to pain with anhidrosis.";
Neuromuscul. Disord. 18:159-166(2008).
[39]
VARIANTS CIPA LYS-492 AND CYS-654, AND VARIANT TRP-6.
PubMed=22302274; DOI=10.1007/s00415-011-6397-y;
Davidson G.L., Murphy S.M., Polke J.M., Laura M., Salih M.A.,
Muntoni F., Blake J., Brandner S., Davies N., Horvath R., Price S.,
Donaghy M., Roberts M., Foulds N., Ramdharry G., Soler D., Lunn M.P.,
Manji H., Davis M.B., Houlden H., Reilly M.M.;
"Frequency of mutations in the genes associated with hereditary
sensory and autonomic neuropathy in a UK cohort.";
J. Neurol. 259:1673-1685(2012).
[40]
VARIANTS CIPA GLU-517; GLU-522; PRO-657; THR-699; SER-752; SER-763 AND
CYS-771, CHARACTERIZATION OF VARIANTS CIPA GLU-517; GLU-522; PRO-657;
THR-699; SER-752; SER-763 AND CYS-771, GLYCOSYLATION, SUBCELLULAR
LOCATION, AUTOPHOSPHORYLATION AFTER NGF STIMULATION, AND FUNCTION.
PubMed=27676246; DOI=10.1002/humu.23123;
Shaikh S.S., Chen Y.C., Halsall S.A., Nahorski M.S., Omoto K.,
Young G.T., Phelan A., Woods C.G.;
"A comprehensive functional analysis of NTRK1 missense mutations
causing hereditary sensory and autonomic neuropathy type IV (HSAN
IV).";
Hum. Mutat. 38:55-63(2017).
-!- FUNCTION: Receptor tyrosine kinase involved in the development and
the maturation of the central and peripheral nervous systems
through regulation of proliferation, differentiation and survival
of sympathetic and nervous neurons. High affinity receptor for NGF
which is its primary ligand (PubMed:1850821, PubMed:1849459,
PubMed:1281417, PubMed:8325889, PubMed:15488758, PubMed:17196528).
Can also bind and be activated by NTF3/neurotrophin-3. However,
NTF3 only supports axonal extension through NTRK1 but has no
effect on neuron survival (By similarity). Upon dimeric NGF
ligand-binding, undergoes homodimerization, autophosphorylation
and activation (PubMed:1281417). Recruits, phosphorylates and/or
activates several downstream effectors including SHC1, FRS2,
SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping
signaling cascades driving cell survival and differentiation.
Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that
regulates cell differentiation and survival. Through PLCG1
controls NF-Kappa-B activation and the transcription of genes
involved in cell survival. Through SHC1 and SH2B1 controls a Ras-
PI3 kinase-AKT1 signaling cascade that is also regulating
survival. In absence of ligand and activation, may promote cell
death, making the survival of neurons dependent on trophic
factors. {ECO:0000250|UniProtKB:P35739,
ECO:0000250|UniProtKB:Q3UFB7, ECO:0000269|PubMed:11244088,
ECO:0000269|PubMed:1281417, ECO:0000269|PubMed:15488758,
ECO:0000269|PubMed:17196528, ECO:0000269|PubMed:1849459,
ECO:0000269|PubMed:1850821, ECO:0000269|PubMed:27676246,
ECO:0000269|PubMed:8155326, ECO:0000269|PubMed:8325889}.
-!- FUNCTION: Isoform TrkA-III: Resistant to NGF, it constitutively
activates AKT1 and NF-kappa-B and is unable to activate the Ras-
MAPK signaling cascade. Antagonizes the anti-proliferative NGF-
NTRK1 signaling that promotes neuronal precursors differentiation.
Isoform TrkA-III promotes angiogenesis and has oncogenic activity
when overexpressed. {ECO:0000269|PubMed:15488758}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:1281417,
ECO:0000269|PubMed:2927393}.
-!- ENZYME REGULATION: The pro-survival signaling effect of NTRK1 in
neurons requires its endocytosis into signaling early endosomes
and its retrograde axonal transport. This is regulated by
different proteins including CFL1, RAC1 and SORT1. NTF3 is unable
to induce this signaling probably due to the lability of the NTF3-
NTRK1 complex in endosomes. SH2D1A inhibits the
autophosphorylation of the receptor, and alters the recruitment
and activation of downstream effectors and signaling cascades (By
similarity). Regulated by NGFR (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q3UFB7}.
-!- SUBUNIT: Exists in a dynamic equilibrium between monomeric (low
affinity) and dimeric (high affinity) structures. Homodimerization
is induced by binding of a NGF dimer (PubMed:1281417,
PubMed:10490030, PubMed:17196528). Interacts with SQSTM1; bridges
NTRK1 to NGFR (PubMed:11244088). Forms a ternary complex with NGFR
and KIDINS220; this complex is affected by the expression levels
of KIDINS220 and an increase in KIDINS220 expression leads to a
decreased association of NGFR and NTRK1 (By similarity). Interacts
with SH2D1A; regulates NTRK1 (By similarity). Interacts
(phosphorylated upon activation by NGF) with SHC1; mediates SHC1
phosphorylation and activation (PubMed:8155326, PubMed:15488758).
Interacts (phosphorylated upon activation by NGF) with PLCG1;
mediates PLCG1 phosphorylation and activation (PubMed:7510697,
PubMed:15488758). Interacts (phosphorylated) with SH2B1 and SH2B2
(By similarity). Interacts with GRB2 (PubMed:15488758). Interacts
with PIK3R1 (PubMed:15488758). Interacts with FRS2
(PubMed:15488758). Interacts with SORT1; may regulate NTRK1
anterograde axonal transport (PubMed:21102451). Interacts with
RAB7A (By similarity). Found in a complex, at least composed of
KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed
at late endosomes in a nerve growth factor (NGF)-dependent manner
(By similarity). Interacts with RAPGEF2; the interaction is
strengthened after NGF stimulation (By similarity). Interacts with
PTPRS (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P35739,
ECO:0000269|PubMed:10490030, ECO:0000269|PubMed:11244088,
ECO:0000269|PubMed:1281417, ECO:0000269|PubMed:15488758,
ECO:0000269|PubMed:17196528, ECO:0000269|PubMed:21102451,
ECO:0000269|PubMed:7510697, ECO:0000269|PubMed:8155326,
ECO:0000269|PubMed:8325889}.
-!- INTERACTION:
P22681:CBL; NbExp=2; IntAct=EBI-1028226, EBI-518228;
P01138:NGF; NbExp=2; IntAct=EBI-1028226, EBI-1028250;
Q8K4V6:Pirb (xeno); NbExp=2; IntAct=EBI-1028226, EBI-8602514;
P18031:PTPN1; NbExp=2; IntAct=EBI-1028226, EBI-968788;
Q99523:SORT1; NbExp=3; IntAct=EBI-1028226, EBI-1057058;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1281417,
ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:17196528,
ECO:0000269|PubMed:27676246, ECO:0000269|PubMed:2927393}; Single-
pass type I membrane protein {ECO:0000269|PubMed:1281417,
ECO:0000269|PubMed:15488758}. Early endosome membrane
{ECO:0000250|UniProtKB:P35739}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P35739}. Late endosome membrane
{ECO:0000250|UniProtKB:P35739}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P35739}. Note=Rapidly internalized
after NGF binding (PubMed:1281417). Internalized to endosomes upon
binding of NGF or NTF3 and further transported to the cell body
via a retrograde axonal transport. Localized at cell membrane and
early endosomes before nerve growth factor (NGF) stimulation.
Recruited to late endosomes after NGF stimulation. Colocalized
with RAPGEF2 at late endosomes. {ECO:0000250|UniProtKB:P35739,
ECO:0000269|PubMed:1281417}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=TrkA-I and TrkA-II isoforms have similar biological
properties but are differentially expressed.;
Name=TrkA-II; Synonyms=TrkAII;
IsoId=P04629-1; Sequence=Displayed;
Note=Major isoform.;
Name=TrkA-I; Synonyms=TrkAI;
IsoId=P04629-2; Sequence=VSP_002899;
Note=Has enhanced responsiveness to NTF3 neurotrophin.;
Name=3;
IsoId=P04629-3; Sequence=VSP_041905, VSP_002899;
Name=TrkA-III; Synonyms=TrkAIII;
IsoId=P04629-4; Sequence=VSP_042152, VSP_002899;
Note=Constitutively active. Does not bind NGF and does not
interact with GRB2 and FRS2.;
-!- TISSUE SPECIFICITY: Isoform TrkA-I is found in most non-neuronal
tissues. Isoform TrkA-II is primarily expressed in neuronal cells.
TrkA-III is specifically expressed by pluripotent neural stem and
neural crest progenitors. {ECO:0000269|PubMed:15488758,
ECO:0000269|PubMed:8325889}.
-!- INDUCTION: Isoform TrkA-III is up-regulated upon hypoxia in cells
normally expressing it. {ECO:0000269|PubMed:15488758}.
-!- DOMAIN: The transmembrane domain mediates interaction with
KIDINS220. {ECO:0000250}.
-!- DOMAIN: The extracellular domain mediates interaction with NGFR.
{ECO:0000250}.
-!- PTM: Ligand-mediated autophosphorylation (PubMed:2927393,
PubMed:1281417, PubMed:15488758, PubMed:7510697, PubMed:8155326,
PubMed:8325889, PubMed:27676246). Interaction with SQSTM1 is
phosphotyrosine-dependent. Autophosphorylation at Tyr-496 mediates
interaction and phosphorylation of SHC1 (PubMed:15488758,
PubMed:7510697, PubMed:8155326, PubMed:8325889).
{ECO:0000269|PubMed:1281417, ECO:0000269|PubMed:15488758,
ECO:0000269|PubMed:27676246, ECO:0000269|PubMed:2927393,
ECO:0000269|PubMed:7510697, ECO:0000269|PubMed:8155326,
ECO:0000269|PubMed:8325889}.
-!- PTM: N-glycosylated (PubMed:2927393). Isoform TrkA-I and isoform
TrkA-II are N-glycosylated. {ECO:0000269|PubMed:15488758,
ECO:0000269|PubMed:17196528, ECO:0000269|PubMed:27676246,
ECO:0000269|PubMed:2927393}.
-!- PTM: Ubiquitinated. Undergoes polyubiquitination upon activation;
regulated by NGFR. Ubiquitination regulates the internalization of
the receptor. {ECO:0000250|UniProtKB:Q3UFB7}.
-!- DISEASE: Congenital insensitivity to pain with anhidrosis (CIPA)
[MIM:256800]: Characterized by a congenital insensitivity to pain,
anhidrosis (absence of sweating), absence of reaction to noxious
stimuli, self-mutilating behavior, and mental retardation. This
rare autosomal recessive disorder is also known as congenital
sensory neuropathy with anhidrosis or hereditary sensory and
autonomic neuropathy type IV or familial dysautonomia type II.
{ECO:0000269|PubMed:10090906, ECO:0000269|PubMed:10233776,
ECO:0000269|PubMed:10330344, ECO:0000269|PubMed:10567924,
ECO:0000269|PubMed:10861667, ECO:0000269|PubMed:10982191,
ECO:0000269|PubMed:11159935, ECO:0000269|PubMed:11310631,
ECO:0000269|PubMed:18077166, ECO:0000269|PubMed:22302274,
ECO:0000269|PubMed:27676246, ECO:0000269|PubMed:8696348}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Note=Chromosomal aberrations involving NTRK1 are found in
papillary thyroid carcinomas (PTCs) (PubMed:2869410,
PubMed:7565764, PubMed:1532241). Translocation t(1;3)(q21;q11)
with TFG generates the TRKT3 (TRK-T3) transcript by fusing TFG to
the 3'-end of NTRK1 (PubMed:7565764). A rearrangement with TPM3
generates the TRK transcript by fusing TPM3 to the 3'-end of NTRK1
(PubMed:2869410). An intrachromosomal rearrangement that links the
protein kinase domain of NTRK1 to the 5'-end of the TPR gene forms
the fusion protein TRK-T1. TRK-T1 is a 55 kDa protein reacting
with antibodies against the C-terminus of the NTRK1 protein
(PubMed:1532241). {ECO:0000269|PubMed:1532241,
ECO:0000269|PubMed:2869410, ECO:0000269|PubMed:7565764}.
-!- MISCELLANEOUS: Trk also stands for tropomyosin-related kinase
since it was first isolated as an oncogenic protein which was the
result of a fusion between the tropomyosin gene TPM3 and NTRK1.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=CAA27243.1; Type=Erroneous termination; Positions=786; Note=Translated as Gln.; Evidence={ECO:0000305};
Sequence=CAA27243.1; Type=Frameshift; Positions=769; Evidence={ECO:0000305};
Sequence=CAA27243.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
Sequence=CAA29888.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
Sequence=CAA44719.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
Sequence=CAA59936.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M23102; AAA36770.1; -; mRNA.
EMBL; AB019488; BAA34355.1; -; Genomic_DNA.
EMBL; AK312704; BAG35582.1; -; mRNA.
EMBL; DB265639; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL158169; CAH70010.1; -; Genomic_DNA.
EMBL; BC062580; AAH62580.1; -; mRNA.
EMBL; BC136554; AAI36555.1; -; mRNA.
EMBL; BC144239; AAI44240.1; -; mRNA.
EMBL; AY321513; AAP88292.1; -; Genomic_DNA.
EMBL; X03541; CAA27243.1; ALT_SEQ; mRNA.
EMBL; X06704; CAA29888.1; ALT_SEQ; mRNA.
EMBL; X85960; CAA59936.1; ALT_SEQ; mRNA.
EMBL; X62947; CAA44719.1; ALT_SEQ; mRNA.
CCDS; CCDS1161.1; -. [P04629-1]
CCDS; CCDS30890.1; -. [P04629-3]
CCDS; CCDS30891.1; -. [P04629-2]
PIR; A30124; TVHUTT.
PIR; S23741; S23741.
RefSeq; NP_001007793.1; NM_001007792.1. [P04629-3]
RefSeq; NP_001012331.1; NM_001012331.1. [P04629-2]
RefSeq; NP_002520.2; NM_002529.3. [P04629-1]
UniGene; Hs.406293; -.
PDB; 1HE7; X-ray; 2.00 A; A=285-413.
PDB; 1SHC; NMR; -; B=489-500.
PDB; 1WWA; X-ray; 2.50 A; X/Y=278-386.
PDB; 1WWW; X-ray; 2.20 A; X/Y=282-382.
PDB; 2IFG; X-ray; 3.40 A; A/B=36-382.
PDB; 2N90; NMR; -; A/B=410-447.
PDB; 4AOJ; X-ray; 2.75 A; A/B/C=473-796.
PDB; 4CRP; NMR; -; A=282-383.
PDB; 4F0I; X-ray; 2.30 A; A/B=498-796.
PDB; 4GT5; X-ray; 2.40 A; A=498-796.
PDB; 4PMM; X-ray; 2.00 A; A=501-787.
PDB; 4PMP; X-ray; 1.80 A; A=501-787.
PDB; 4PMS; X-ray; 2.80 A; A=501-787.
PDB; 4PMT; X-ray; 2.10 A; A=501-787.
PDB; 4YNE; X-ray; 2.02 A; A=502-796.
PDB; 4YPS; X-ray; 2.10 A; A=502-796.
PDB; 5H3Q; X-ray; 2.10 A; A=473-796.
PDB; 5JFS; X-ray; 2.07 A; A=502-796.
PDB; 5JFV; X-ray; 1.59 A; A=502-796.
PDB; 5JFW; X-ray; 1.52 A; A=502-796.
PDB; 5JFX; X-ray; 1.63 A; A=502-796.
PDB; 5KMI; X-ray; 1.87 A; A=474-796.
PDB; 5KMJ; X-ray; 2.04 A; A=474-796.
PDB; 5KMK; X-ray; 2.24 A; A=474-796.
PDB; 5KML; X-ray; 2.01 A; A=474-796.
PDB; 5KMM; X-ray; 2.12 A; A=474-796.
PDB; 5KMN; X-ray; 2.14 A; A=474-796.
PDB; 5KMO; X-ray; 2.67 A; A=474-796.
PDBsum; 1HE7; -.
PDBsum; 1SHC; -.
PDBsum; 1WWA; -.
PDBsum; 1WWW; -.
PDBsum; 2IFG; -.
PDBsum; 2N90; -.
PDBsum; 4AOJ; -.
PDBsum; 4CRP; -.
PDBsum; 4F0I; -.
PDBsum; 4GT5; -.
PDBsum; 4PMM; -.
PDBsum; 4PMP; -.
PDBsum; 4PMS; -.
PDBsum; 4PMT; -.
PDBsum; 4YNE; -.
PDBsum; 4YPS; -.
PDBsum; 5H3Q; -.
PDBsum; 5JFS; -.
PDBsum; 5JFV; -.
PDBsum; 5JFW; -.
PDBsum; 5JFX; -.
PDBsum; 5KMI; -.
PDBsum; 5KMJ; -.
PDBsum; 5KMK; -.
PDBsum; 5KML; -.
PDBsum; 5KMM; -.
PDBsum; 5KMN; -.
PDBsum; 5KMO; -.
ProteinModelPortal; P04629; -.
SMR; P04629; -.
BioGrid; 110969; 1942.
DIP; DIP-5714N; -.
ELM; P04629; -.
IntAct; P04629; 17.
MINT; MINT-124106; -.
STRING; 9606.ENSP00000431418; -.
BindingDB; P04629; -.
ChEMBL; CHEMBL2815; -.
DrugBank; DB00321; Amitriptyline.
DrugBank; DB00619; Imatinib.
DrugBank; DB08896; Regorafenib.
GuidetoPHARMACOLOGY; 1817; -.
iPTMnet; P04629; -.
PhosphoSitePlus; P04629; -.
BioMuta; NTRK1; -.
DMDM; 94730402; -.
PaxDb; P04629; -.
PeptideAtlas; P04629; -.
PRIDE; P04629; -.
Ensembl; ENST00000368196; ENSP00000357179; ENSG00000198400. [P04629-2]
Ensembl; ENST00000392302; ENSP00000376120; ENSG00000198400. [P04629-3]
Ensembl; ENST00000524377; ENSP00000431418; ENSG00000198400. [P04629-1]
GeneID; 4914; -.
KEGG; hsa:4914; -.
UCSC; uc001fqf.2; human. [P04629-1]
CTD; 4914; -.
DisGeNET; 4914; -.
GeneCards; NTRK1; -.
GeneReviews; NTRK1; -.
HGNC; HGNC:8031; NTRK1.
HPA; CAB004606; -.
HPA; HPA035799; -.
HPA; HPA076570; -.
MalaCards; NTRK1; -.
MIM; 164970; gene.
MIM; 191315; gene.
MIM; 256800; phenotype.
neXtProt; NX_P04629; -.
OpenTargets; ENSG00000198400; -.
Orphanet; 99361; Familial medullary thyroid carcinoma.
Orphanet; 642; Hereditary sensory and autonomic neuropathy type 4.
Orphanet; 64752; Hereditary sensory and autonomic neuropathy type 5.
Orphanet; 146; Papillary or follicular thyroid carcinoma.
PharmGKB; PA31817; -.
eggNOG; ENOG410IMMI; Eukaryota.
eggNOG; ENOG410XTGG; LUCA.
GeneTree; ENSGT00760000118818; -.
HOVERGEN; HBG056735; -.
InParanoid; P04629; -.
KO; K03176; -.
OMA; PEVYAIM; -.
OrthoDB; EOG091G01JY; -.
PhylomeDB; P04629; -.
TreeFam; TF106465; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-167021; PLC-gamma1 signalling.
Reactome; R-HSA-167044; Signalling to RAS.
Reactome; R-HSA-170968; Frs2-mediated activation.
Reactome; R-HSA-170984; ARMS-mediated activation.
Reactome; R-HSA-177504; Retrograde neurotrophin signalling.
Reactome; R-HSA-187024; NGF-independant TRKA activation.
Reactome; R-HSA-187042; TRKA activation by NGF.
Reactome; R-HSA-187706; Signalling to p38 via RIT and RIN.
Reactome; R-HSA-198203; PI3K/AKT activation.
Reactome; R-HSA-198745; Signalling to STAT3.
SignaLink; P04629; -.
SIGNOR; P04629; -.
ChiTaRS; NTRK1; human.
EvolutionaryTrace; P04629; -.
GenomeRNAi; 4914; -.
PRO; PR:P04629; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000198400; -.
ExpressionAtlas; P04629; baseline and differential.
Genevisible; P04629; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005770; C:late endosome; ISS:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005004; F:GPI-linked ephrin receptor activity; IEA:Ensembl.
GO; GO:0019900; F:kinase binding; IEA:Ensembl.
GO; GO:0048406; F:nerve growth factor binding; IDA:UniProtKB.
GO; GO:0010465; F:nerve growth factor receptor activity; IDA:UniProtKB.
GO; GO:0043121; F:neurotrophin binding; TAS:ProtInc.
GO; GO:0005166; F:neurotrophin p75 receptor binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; IEA:Ensembl.
GO; GO:0060385; P:axonogenesis involved in innervation; ISS:UniProtKB.
GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
GO; GO:0061368; P:behavioral response to formalin induced pain; IEA:Ensembl.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IMP:UniProtKB.
GO; GO:0071316; P:cellular response to nicotine; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IEA:Ensembl.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IEA:Ensembl.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0042490; P:mechanoreceptor differentiation; IEA:Ensembl.
GO; GO:0007018; P:microtubule-based movement; TAS:Reactome.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0038180; P:nerve growth factor signaling pathway; IMP:UniProtKB.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IDA:UniProtKB.
GO; GO:0021553; P:olfactory nerve development; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IMP:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0043068; P:positive regulation of programmed cell death; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; TAS:BHF-UCL.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:UniProtKB.
GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0010623; P:programmed cell death involved in cell development; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0051599; P:response to hydrostatic pressure; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IEA:Ensembl.
GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl.
GO; GO:0048485; P:sympathetic nervous system development; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR031635; NTRK_C2.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR020461; Tyr_kinase_neurotrophic_rcpt_1.
InterPro; IPR020777; Tyr_kinase_NGF_rcpt.
InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
Pfam; PF13855; LRR_8; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF16920; TPKR_C2; 1.
PRINTS; PR01939; NTKRECEPTOR.
PRINTS; PR01940; NTKRECEPTOR1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00082; LRRCT; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 2.
SUPFAM; SSF52058; SSF52058; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Chromosomal rearrangement; Complete proteome; Developmental protein;
Differentiation; Disease mutation; Disulfide bond; Endosome;
Glycoprotein; Immunoglobulin domain; Kinase; Leucine-rich repeat;
Membrane; Neurogenesis; Nucleotide-binding; Phosphoprotein;
Polymorphism; Proto-oncogene; Receptor; Reference proteome; Repeat;
Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 796 High affinity nerve growth factor
receptor.
/FTId=PRO_0000016724.
TOPO_DOM 33 423 Extracellular. {ECO:0000255}.
TRANSMEM 424 439 Helical. {ECO:0000255}.
TOPO_DOM 440 796 Cytoplasmic. {ECO:0000255}.
REPEAT 90 113 LRR 1.
REPEAT 116 137 LRR 2.
DOMAIN 148 193 LRRCT.
DOMAIN 194 283 Ig-like C2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 299 365 Ig-like C2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 510 781 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 516 524 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 469 490 Interaction with SQSTM1. {ECO:0000250}.
ACT_SITE 650 650 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 544 544 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 398 399 Breakpoint for translocation to form TRK
and TRK-T3.
SITE 486 486 Breakpoint for translocation to form TRK-
T1.
SITE 496 496 Interaction with SHC1.
SITE 791 791 Interaction with PLCG1.
MOD_RES 496 496 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15488758,
ECO:0000269|PubMed:27676246,
ECO:0000269|PubMed:8155326}.
MOD_RES 676 676 Phosphotyrosine; by autocatalysis.
{ECO:0000305|PubMed:8325889}.
MOD_RES 680 680 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15488758}.
MOD_RES 681 681 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15488758}.
MOD_RES 791 791 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15488758,
ECO:0000269|PubMed:7510697,
ECO:0000269|PubMed:8155326}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17196528}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17196528}.
CARBOHYD 188 188 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:2IFG,
ECO:0000269|PubMed:17196528}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 262 262 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:2IFG,
ECO:0000269|PubMed:17196528}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:2IFG,
ECO:0000269|PubMed:17196528}.
CARBOHYD 318 318 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 338 338 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 358 358 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:2IFG,
ECO:0000269|PubMed:17196528}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 41 {ECO:0000244|PDB:2IFG}.
DISULFID 40 50 {ECO:0000244|PDB:2IFG}.
DISULFID 154 191 {ECO:0000244|PDB:2IFG,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17196528}.
DISULFID 215 265 {ECO:0000244|PDB:2IFG,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17196528}.
DISULFID 300 345 {ECO:0000244|PDB:1HE7,
ECO:0000244|PDB:1WWA,
ECO:0000244|PDB:1WWW,
ECO:0000244|PDB:2IFG,
ECO:0000244|PDB:4CRP}.
VAR_SEQ 1 71 MLRGGRRGQLGWHSWAAGPGSLLAWLILASAGAAPCPDACC
PHGSSGLRCTRDGALDSLHHLPGAENLTEL -> MKEAALI
CLAPSVPPILTVKSWDTMQLRAARSRCTNLLAAS (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041905.
VAR_SEQ 192 284 GVPTLKVQVPNASVDVGDDVLLRCQVEGRGLEQAGWILTEL
EQSATVMKSGGLPSLGLTLANVTSDLNRKNVTCWAENDVGR
AEVSVQVNVSF -> V (in isoform TrkA-III).
{ECO:0000305}.
/FTId=VSP_042152.
VAR_SEQ 393 398 Missing (in isoform TrkA-I, isoform 3 and
isoform TrkA-III).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2927393}.
/FTId=VSP_002899.
VARIANT 6 6 R -> W (in dbSNP:rs201472270).
{ECO:0000269|PubMed:22302274}.
/FTId=VAR_068480.
VARIANT 18 18 G -> E (in dbSNP:rs1007211).
/FTId=VAR_049714.
VARIANT 80 80 Q -> R (in dbSNP:rs55891455).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041461.
VARIANT 85 85 R -> S (in dbSNP:rs543320028).
{ECO:0000269|PubMed:10330344,
ECO:0000269|PubMed:11159935}.
/FTId=VAR_009623.
VARIANT 93 93 L -> P (in CIPA; aberrantly processed;
shows diminished autophosphorylation in
neuronal cells).
{ECO:0000269|PubMed:10982191,
ECO:0000269|PubMed:11159935}.
/FTId=VAR_009624.
VARIANT 107 107 A -> V (in an ovarian serous carcinoma
sample; somatic mutation;
dbSNP:rs540521894).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041462.
VARIANT 213 213 L -> P (in CIPA; aberrantly processed;
shows diminished autophosphorylation in
neuronal cells; dbSNP:rs747711259).
{ECO:0000269|PubMed:10330344,
ECO:0000269|PubMed:11159935}.
/FTId=VAR_009625.
VARIANT 237 237 T -> M (in dbSNP:rs55909005).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041463.
VARIANT 238 238 V -> G (in dbSNP:rs56000394).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041464.
VARIANT 260 260 R -> G (in dbSNP:rs35116695).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041465.
VARIANT 359 359 Y -> C (in CIPA; dbSNP:rs121964869).
{ECO:0000269|PubMed:11310631}.
/FTId=VAR_068481.
VARIANT 444 444 R -> Q (in dbSNP:rs56320207).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041466.
VARIANT 452 452 R -> C (in dbSNP:rs34900547).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041467.
VARIANT 492 492 E -> K (in CIPA; dbSNP:rs144901788).
{ECO:0000269|PubMed:22302274}.
/FTId=VAR_068482.
VARIANT 517 517 G -> E (in CIPA; following transfection
in neuroblastoma cells and NGF treatment,
small decrease in the percentage of cells
differentiated into neuronal phenotype,
but in differentiated cells, the average
neurite length is comparable to wild-
type; no effect on N-glycosylation,
subcellular location, nor on basal and
NGF-induced autophosphorylation; loss of
NGF-stimulated calcium flux;
dbSNP:rs606231467).
{ECO:0000269|PubMed:27676246}.
/FTId=VAR_077472.
VARIANT 522 522 G -> E (in CIPA; no effect on N-
glycosylation, nor on subcellular
location; reduced basal
autophosphorylation and complete loss of
NGF-induced autophosphorylation; loss of
NGF-stimulated calcium flux).
{ECO:0000269|PubMed:27676246}.
/FTId=VAR_077473.
VARIANT 522 522 G -> R (in CIPA; processed as wild-type
but shows significantly diminished
autophosphorylation in both neuronal and
non-neuronal cells).
{ECO:0000269|PubMed:10982191,
ECO:0000269|PubMed:11159935}.
/FTId=VAR_009626.
VARIANT 566 566 M -> T (in dbSNP:rs55892037).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041468.
VARIANT 572 572 I -> S (in CIPA).
{ECO:0000269|PubMed:18077166}.
/FTId=VAR_077474.
VARIANT 577 577 G -> R (in CIPA; loss of function;
processed as wild-type but shows
significantly diminished
autophosphorylation in both neuronal and
non-neuronal cells; dbSNP:rs121964866).
{ECO:0000269|PubMed:10567924,
ECO:0000269|PubMed:10982191,
ECO:0000269|PubMed:11159935,
ECO:0000269|PubMed:8696348}.
/FTId=VAR_004103.
VARIANT 587 587 M -> V (in CIPA; dbSNP:rs121964870).
{ECO:0000269|PubMed:10233776}.
/FTId=VAR_009627.
VARIANT 604 604 H -> Y (in dbSNP:rs6336).
{ECO:0000269|PubMed:10330344,
ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10443680,
ECO:0000269|PubMed:11159935,
ECO:0000269|PubMed:11310631,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_009628.
VARIANT 613 613 G -> V (in dbSNP:rs6339).
{ECO:0000269|PubMed:10330344,
ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10443680,
ECO:0000269|PubMed:10861667,
ECO:0000269|PubMed:11159935,
ECO:0000269|PubMed:11310631,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_009629.
VARIANT 649 649 R -> W (in CIPA; processed as wild-type
but shows significantly diminished
autophosphorylation in both neuronal and
non-neuronal cells; dbSNP:rs369353892).
{ECO:0000269|PubMed:10330344,
ECO:0000269|PubMed:11159935}.
/FTId=VAR_009630.
VARIANT 654 654 R -> C (in CIPA; processed as wild-type
but shows significantly diminished
autophosphorylation in both neuronal and
non-neuronal cells; dbSNP:rs764992664).
{ECO:0000269|PubMed:10982191,
ECO:0000269|PubMed:11159935,
ECO:0000269|PubMed:22302274}.
/FTId=VAR_009631.
VARIANT 657 657 L -> P (in CIPA; following transfection
in neuroblastoma cells and NGF treatment,
loss of differentiation into neuronal
phenotype; partially decreased N-
glycosylation; reduced expression at the
plasma membrane; reduced basal
autophosphorylation and complete loss of
NGF-induced autophosphorylation; loss of
NGF-stimulated calcium flux).
{ECO:0000269|PubMed:27676246}.
/FTId=VAR_077475.
VARIANT 674 674 D -> Y (in CIPA; unknown pathological
significance; might impair the function
of the enzyme without compromising
autophosphorylation; dbSNP:rs80356677).
{ECO:0000269|PubMed:10982191,
ECO:0000269|PubMed:11159935}.
/FTId=VAR_009632.
VARIANT 695 695 P -> L (in CIPA; dbSNP:rs121964868).
{ECO:0000269|PubMed:10861667}.
/FTId=VAR_009633.
VARIANT 699 699 I -> T (in CIPA; partially decreased N-
glycosylation; reduced expression at the
plasma membrane; reduced basal
autophosphorylation and complete loss of
NGF-induced autophosphorylation; loss of
NGF-stimulated calcium flux).
{ECO:0000269|PubMed:27676246}.
/FTId=VAR_077476.
VARIANT 714 714 G -> S (in CIPA; processed as wild-type
but shows significantly diminished
autophosphorylation in both neuronal and
non-neuronal cells; dbSNP:rs770727871).
{ECO:0000269|PubMed:10330344,
ECO:0000269|PubMed:11159935}.
/FTId=VAR_009634.
VARIANT 717 717 L -> R (in CIPA; found in a compound
heterozygote also carrying an premature
stop codon at position 558).
{ECO:0000269|PubMed:18077166}.
/FTId=VAR_077477.
VARIANT 752 752 C -> S (in CIPA; unknown pathological
significance; following transfection in
neuroblastoma cells and NGF treatment, no
effect on neurite outgrowth, nor neurite
length; no effect on N-glycosylation,
subcellular location, basal and NGF-
induced autophosphorylation, nor on NGF-
stimulated calcium flux).
{ECO:0000269|PubMed:27676246}.
/FTId=VAR_077478.
VARIANT 763 763 C -> S (in CIPA; following transfection
in neuroblastoma cells and NGF treatment,
decreased percentage of cells
differentiated into neuronal phenotype
and reduced neurite length compared with
wild-type; slightly decreased N-
glycosylation; reduced expression at the
plasma membrane; reduced basal and NGF-
induced autophosphorylation; small
reduction in NGF-stimulated calcium
flux). {ECO:0000269|PubMed:27676246}.
/FTId=VAR_077479.
VARIANT 771 771 R -> C (in CIPA; partially decreased N-
glycosylation; reduced expression at the
plasma membrane; reduced basal
autophosphorylation and complete loss of
NGF-induced autophosphorylation; loss of
NGF-stimulated calcium flux).
{ECO:0000269|PubMed:27676246}.
/FTId=VAR_077480.
VARIANT 780 780 R -> P (in CIPA; loss of function;
dbSNP:rs35669708).
{ECO:0000269|PubMed:10090906}.
/FTId=VAR_009635.
VARIANT 780 780 R -> Q (in dbSNP:rs35669708).
{ECO:0000269|PubMed:10443680,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_009636.
VARIANT 790 790 V -> I (in dbSNP:rs55948542).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041469.
MUTAGEN 496 496 Y->F: Loss of interaction with SHC1 and
altered phosphorylation of SHC1. Altered
neurite outgrowth and altered activation
of the MAPK pathway; when associated with
F-791. {ECO:0000269|PubMed:8155326}.
MUTAGEN 544 544 K->N: Loss of kinase activity.
{ECO:0000269|PubMed:1281417,
ECO:0000269|PubMed:8155326}.
MUTAGEN 791 791 Y->F: Loss of interaction with PLCG1 and
altered phosphorylation of PLCG1. Altered
neurite outgrowth and altered activation
of the MAPK pathway; when associated with
F-496. {ECO:0000269|PubMed:7510697,
ECO:0000269|PubMed:8155326}.
CONFLICT 263 263 V -> L (in Ref. 1; AAA36770).
{ECO:0000305}.
CONFLICT 300 300 C -> S (in Ref. 1; AAA36770).
{ECO:0000305}.
CONFLICT 529 529 C -> S (in Ref. 10; CAA59936).
{ECO:0000305}.
STRAND 38 40 {ECO:0000244|PDB:2IFG}.
STRAND 43 46 {ECO:0000244|PDB:2IFG}.
TURN 57 61 {ECO:0000244|PDB:2IFG}.
STRAND 69 72 {ECO:0000244|PDB:2IFG}.
HELIX 84 86 {ECO:0000244|PDB:2IFG}.
STRAND 94 97 {ECO:0000244|PDB:2IFG}.
HELIX 110 112 {ECO:0000244|PDB:2IFG}.
STRAND 119 121 {ECO:0000244|PDB:2IFG}.
TURN 133 135 {ECO:0000244|PDB:2IFG}.
STRAND 142 144 {ECO:0000244|PDB:2IFG}.
HELIX 154 156 {ECO:0000244|PDB:2IFG}.
HELIX 157 164 {ECO:0000244|PDB:2IFG}.
HELIX 171 173 {ECO:0000244|PDB:2IFG}.
STRAND 178 181 {ECO:0000244|PDB:2IFG}.
STRAND 195 199 {ECO:0000244|PDB:2IFG}.
STRAND 211 218 {ECO:0000244|PDB:2IFG}.
STRAND 227 230 {ECO:0000244|PDB:2IFG}.
STRAND 234 238 {ECO:0000244|PDB:2IFG}.
STRAND 244 253 {ECO:0000244|PDB:2IFG}.
TURN 257 260 {ECO:0000244|PDB:2IFG}.
STRAND 263 265 {ECO:0000244|PDB:2IFG}.
STRAND 276 278 {ECO:0000244|PDB:2IFG}.
STRAND 284 290 {ECO:0000244|PDB:1WWW}.
STRAND 298 305 {ECO:0000244|PDB:1HE7}.
STRAND 312 317 {ECO:0000244|PDB:1HE7}.
STRAND 326 333 {ECO:0000244|PDB:1HE7}.
STRAND 342 350 {ECO:0000244|PDB:1HE7}.
HELIX 353 355 {ECO:0000244|PDB:1HE7}.
STRAND 357 365 {ECO:0000244|PDB:1HE7}.
STRAND 368 376 {ECO:0000244|PDB:1HE7}.
HELIX 418 441 {ECO:0000244|PDB:2N90}.
STRAND 476 478 {ECO:0000244|PDB:5KML}.
HELIX 490 492 {ECO:0000244|PDB:5KMI}.
TURN 494 496 {ECO:0000244|PDB:1SHC}.
HELIX 507 509 {ECO:0000244|PDB:5JFW}.
STRAND 510 517 {ECO:0000244|PDB:5JFW}.
STRAND 520 522 {ECO:0000244|PDB:5JFW}.
STRAND 524 533 {ECO:0000244|PDB:5JFW}.
TURN 534 536 {ECO:0000244|PDB:5KMI}.
STRAND 537 545 {ECO:0000244|PDB:5JFW}.
HELIX 552 566 {ECO:0000244|PDB:5JFW}.
STRAND 575 579 {ECO:0000244|PDB:5JFW}.
STRAND 581 584 {ECO:0000244|PDB:5JFW}.
STRAND 586 590 {ECO:0000244|PDB:5JFW}.
HELIX 597 603 {ECO:0000244|PDB:5JFW}.
STRAND 605 607 {ECO:0000244|PDB:4F0I}.
HELIX 608 611 {ECO:0000244|PDB:4PMP}.
STRAND 615 617 {ECO:0000244|PDB:4YNE}.
STRAND 619 621 {ECO:0000244|PDB:5KMI}.
HELIX 624 643 {ECO:0000244|PDB:5JFW}.
STRAND 646 648 {ECO:0000244|PDB:5KML}.
HELIX 653 655 {ECO:0000244|PDB:5JFW}.
STRAND 656 659 {ECO:0000244|PDB:5JFW}.
HELIX 660 662 {ECO:0000244|PDB:5JFW}.
STRAND 663 666 {ECO:0000244|PDB:5JFW}.
HELIX 672 675 {ECO:0000244|PDB:5KMI}.
HELIX 677 679 {ECO:0000244|PDB:4PMP}.
STRAND 680 683 {ECO:0000244|PDB:5KMI}.
TURN 684 686 {ECO:0000244|PDB:5KMI}.
STRAND 687 689 {ECO:0000244|PDB:5KMI}.
HELIX 691 693 {ECO:0000244|PDB:5JFW}.
HELIX 696 701 {ECO:0000244|PDB:5JFW}.
HELIX 706 721 {ECO:0000244|PDB:5JFW}.
TURN 722 724 {ECO:0000244|PDB:5JFV}.
TURN 727 730 {ECO:0000244|PDB:5JFW}.
HELIX 733 742 {ECO:0000244|PDB:5JFW}.
HELIX 754 763 {ECO:0000244|PDB:5JFW}.
HELIX 768 770 {ECO:0000244|PDB:5JFW}.
HELIX 774 786 {ECO:0000244|PDB:5JFW}.
HELIX 789 793 {ECO:0000244|PDB:5KMI}.
SEQUENCE 796 AA; 87497 MW; 6C15C721E336B601 CRC64;
MLRGGRRGQL GWHSWAAGPG SLLAWLILAS AGAAPCPDAC CPHGSSGLRC TRDGALDSLH
HLPGAENLTE LYIENQQHLQ HLELRDLRGL GELRNLTIVK SGLRFVAPDA FHFTPRLSRL
NLSFNALESL SWKTVQGLSL QELVLSGNPL HCSCALRWLQ RWEEEGLGGV PEQKLQCHGQ
GPLAHMPNAS CGVPTLKVQV PNASVDVGDD VLLRCQVEGR GLEQAGWILT ELEQSATVMK
SGGLPSLGLT LANVTSDLNR KNVTCWAEND VGRAEVSVQV NVSFPASVQL HTAVEMHHWC
IPFSVDGQPA PSLRWLFNGS VLNETSFIFT EFLEPAANET VRHGCLRLNQ PTHVNNGNYT
LLAANPFGQA SASIMAAFMD NPFEFNPEDP IPVSFSPVDT NSTSGDPVEK KDETPFGVSV
AVGLAVFACL FLSTLLLVLN KCGRRNKFGI NRPAVLAPED GLAMSLHFMT LGGSSLSPTE
GKGSGLQGHI IENPQYFSDA CVHHIKRRDI VLKWELGEGA FGKVFLAECH NLLPEQDKML
VAVKALKEAS ESARQDFQRE AELLTMLQHQ HIVRFFGVCT EGRPLLMVFE YMRHGDLNRF
LRSHGPDAKL LAGGEDVAPG PLGLGQLLAV ASQVAAGMVY LAGLHFVHRD LATRNCLVGQ
GLVVKIGDFG MSRDIYSTDY YRVGGRTMLP IRWMPPESIL YRKFTTESDV WSFGVVLWEI
FTYGKQPWYQ LSNTEAIDCI TQGRELERPR ACPPEVYAIM RGCWQREPQQ RHSIKDVHAR
LQALAQAPPV YLDVLG


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