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High affinity nerve growth factor receptor (EC 2.7.10.1) (Neurotrophic tyrosine kinase receptor type 1) (Slow nerve growth factor receptor) (p140-TrkA) (Trk-A)

 NTRK1_RAT               Reviewed;         799 AA.
P35739;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
22-NOV-2017, entry version 178.
RecName: Full=High affinity nerve growth factor receptor;
EC=2.7.10.1;
AltName: Full=Neurotrophic tyrosine kinase receptor type 1;
AltName: Full=Slow nerve growth factor receptor;
AltName: Full=p140-TrkA;
Short=Trk-A;
Flags: Precursor;
Name=Ntrk1; Synonyms=Trk, Trka;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TRKA-II), FUNCTION AS RECEPTOR FOR
NGF, AND SUBCELLULAR LOCATION.
PubMed=1312719; DOI=10.1073/pnas.89.6.2374;
Meakin S.O., Suter U., Drinkwater C.C., Welcher A.A., Shooter E.M.;
"The rat trk protooncogene product exhibits properties characteristic
of the slow nerve growth factor receptor.";
Proc. Natl. Acad. Sci. U.S.A. 89:2374-2378(1992).
[2]
ALTERNATIVE SPLICING (ISOFORMS TRKA-I AND TRKA-II).
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).
[3]
FUNCTION AS RECEPTOR FOR NGF, AND SUBCELLULAR LOCATION.
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).
[4]
INTERACTION WITH SHC1.
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).
[5]
INTERACTION WITH PLCG1; SHC1; SH2B1 AND SH2B2, AND MUTAGENESIS OF
VAL-527.
PubMed=9856458; DOI=10.1016/S0896-6273(00)80620-0;
Qian X., Riccio A., Zhang Y., Ginty D.D.;
"Identification and characterization of novel substrates of Trk
receptors in developing neurons.";
Neuron 21:1017-1029(1998).
[6]
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).
[7]
INTERACTION WITH KIDINS220.
PubMed=11150334;
Kong H., Boulter J., Weber J.L., Lai C., Chao M.V.;
"An evolutionarily conserved transmembrane protein that is a novel
downstream target of neurotrophin and ephrin receptors.";
J. Neurosci. 21:176-185(2001).
[8]
INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=12471037; DOI=10.1074/jbc.M208468200;
Geetha T., Wooten M.W.;
"Association of the atypical protein kinase C-interacting protein
p62/ZIP with nerve growth factor receptor TrkA regulates receptor
trafficking and Erk5 signaling.";
J. Biol. Chem. 278:4730-4739(2003).
[9]
INTERACTION WITH KIDINS220, AND DOMAIN.
PubMed=15167895; DOI=10.1038/sj.emboj.7600253;
Arevalo J.C., Yano H., Teng K.K., Chao M.V.;
"A unique pathway for sustained neurotrophin signaling through an
ankyrin-rich membrane-spanning protein.";
EMBO J. 23:2358-2368(2004).
[10]
INTERACTION WITH NGFR AND KIDINS220, AND DOMAIN.
PubMed=15378608; DOI=10.1002/jnr.20262;
Chang M.-S., Arevalo J.C., Chao M.V.;
"Ternary complex with Trk, p75, and an ankyrin-rich membrane spanning
protein.";
J. Neurosci. Res. 78:186-192(2004).
[11]
ENZYME REGULATION, AND INTERACTION WITH SH2D1A.
PubMed=16223723; DOI=10.1074/jbc.M506554200;
Lo K.Y., Chin W.H., Ng Y.P., Cheng A.W., Cheung Z.H., Ip N.Y.;
"SLAM-associated protein as a potential negative regulator in Trk
signaling.";
J. Biol. Chem. 280:41744-41752(2005).
[12]
INTERACTION WITH RAB7A, AND SUBCELLULAR LOCATION.
PubMed=16306406; DOI=10.1523/JNEUROSCI.2029-05.2005;
Saxena S., Bucci C., Weis J., Kruttgen A.;
"The small GTPase Rab7 controls the endosomal trafficking and
neuritogenic signaling of the nerve growth factor receptor TrkA.";
J. Neurosci. 25:10930-10940(2005).
[13]
INTERACTION WITH PTPRS.
PubMed=17967490; DOI=10.1016/j.bbamcr.2007.06.008;
Faux C., Hawadle M., Nixon J., Wallace A., Lee S., Murray S.,
Stoker A.;
"PTPsigma binds and dephosphorylates neurotrophin receptors and can
suppress NGF-dependent neurite outgrowth from sensory neurons.";
Biochim. Biophys. Acta 1773:1689-1700(2007).
[14]
IDENTIFICATION IN A COMPLEX WITH KIDINS220; MAGI2 AND RAPGEF2,
INTERACTION WITH RAPGEF2, AND SUBCELLULAR LOCATION.
PubMed=17724123; DOI=10.1083/jcb.200610073;
Hisata S., Sakisaka T., Baba T., Yamada T., Aoki K., Matsuda M.,
Takai Y.;
"Rap1-PDZ-GEF1 interacts with a neurotrophin receptor at late
endosomes, leading to sustained activation of Rap1 and ERK and neurite
outgrowth.";
J. Cell Biol. 178:843-860(2007).
[15]
INTERACTION WITH NRADD.
PubMed=18624909; DOI=10.1111/j.1471-4159.2008.05539.x;
Wong A.W., Willingham M., Xiao J., Kilpatrick T.J., Murray S.S.;
"Neurotrophin receptor homolog-2 regulates nerve growth factor
signaling.";
J. Neurochem. 106:1964-1976(2008).
[16]
FUNCTION IN CELL DEATH.
PubMed=20811452; DOI=10.1038/nature09336;
Nikoletopoulou V., Lickert H., Frade J.M., Rencurel C.,
Giallonardo P., Zhang L., Bibel M., Barde Y.A.;
"Neurotrophin receptors TrkA and TrkC cause neuronal death whereas
TrkB does not.";
Nature 467:59-63(2010).
-!- 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:1312719, PubMed:1850821). 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. Upon dimeric NGF ligand-binding, undergoes
homodimerization, autophosphorylation and activation. 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:0000269|PubMed:1312719, ECO:0000269|PubMed:1850821,
ECO:0000269|PubMed:20811452}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- 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 (By similarity). SH2D1A inhibits the
autophosphorylation of the receptor, and alters the recruitment
and activation of downstream effectors and signaling cascades.
Regulated by NGFR (By similarity). {ECO:0000250}.
-!- SUBUNIT: Exists in a dynamic equilibrium between monomeric (low
affinity) and dimeric (high affinity) structures. Homodimerization
is induced by binding of a NGF dimer (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 (PubMed:17724123). Interacts with
RAPGEF2; the interaction is strengthened after NGF stimulation
(PubMed:17724123). Interacts with SQSTM1; bridges NTRK1 to NGFR.
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. Interacts (phosphorylated upon activation by NGF) with
SHC1; mediates SHC1 phosphorylation and activation. Interacts
(phosphorylated upon activation by NGF) with PLCG1; mediates PLCG1
phosphorylation and activation. Interacts (phosphorylated) with
SH2B1 and SH2B2. Interacts with GRB2. Interacts with PIK3R1.
Interacts with FRS2. Interacts with SORT1; may regulate NTRK1
anterograde axonal transport. Interacts with SH2D1A; regulates
NTRK1. Interacts with NRADD (PubMed:18624909). Interacts with
RAB7A (PubMed:16306406). Interacts with PTPRS (PubMed:17967490).
{ECO:0000250, ECO:0000269|PubMed:11150334,
ECO:0000269|PubMed:11244088, ECO:0000269|PubMed:12471037,
ECO:0000269|PubMed:15167895, ECO:0000269|PubMed:15378608,
ECO:0000269|PubMed:16223723, ECO:0000269|PubMed:16306406,
ECO:0000269|PubMed:17724123, ECO:0000269|PubMed:17967490,
ECO:0000269|PubMed:18624909, ECO:0000269|PubMed:8155326,
ECO:0000269|PubMed:9856458}.
-!- INTERACTION:
P62994:Grb2; NbExp=6; IntAct=EBI-976667, EBI-401775;
P07174:Ngfr; NbExp=2; IntAct=EBI-976667, EBI-1038810;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1312719,
ECO:0000269|PubMed:16306406, ECO:0000269|PubMed:1850821}; Single-
pass type I membrane protein {ECO:0000305|PubMed:1850821}. Early
endosome membrane {ECO:0000269|PubMed:17724123}; Single-pass type
I membrane protein {ECO:0000305}. Late endosome membrane
{ECO:0000269|PubMed:17724123}; Single-pass type I membrane protein
{ECO:0000305}. Note=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 (PubMed:17724123).
Recruited to late endosomes after NGF stimulation
(PubMed:17724123). Colocalized with RAPGEF2 at late endosomes
(PubMed:17724123). {ECO:0000269|PubMed:17724123}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Both isoforms have similar biological properties.;
Name=TrkA-II;
IsoId=P35739-1; Sequence=Displayed;
Name=TrkA-I;
IsoId=P35739-2; Sequence=VSP_002900;
-!- TISSUE SPECIFICITY: Isoform Trka-II is primarily expressed in
neuronal cells; isoform Trka-I is found in non-neuronal tissues.
-!- DOMAIN: The transmembrane domain mediates interaction with
KIDINS220.
-!- DOMAIN: The extracellular domain mediates interaction with NGFR.
-!- PTM: Ligand-mediated autophosphorylation. Interaction with SQSTM1
is phosphotyrosine-dependent. Autophosphorylation at Tyr-499
mediates interaction and phosphorylation of SHC1.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P04629}.
-!- PTM: Ubiquitinated. Undergoes polyubiquitination upon activation;
regulated by NGFR. Ubiquitination regulates the internalization of
the receptor. {ECO:0000250|UniProtKB:Q3UFB7}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; M85214; AAA42286.1; -; mRNA.
EMBL; L12225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A41981; TVRTTB.
RefSeq; NP_067600.1; NM_021589.1. [P35739-1]
UniGene; Rn.39098; -.
ProteinModelPortal; P35739; -.
SMR; P35739; -.
BioGrid; 248731; 21.
CORUM; P35739; -.
DIP; DIP-5716N; -.
IntAct; P35739; 5.
MINT; MINT-191667; -.
STRING; 10116.ENSRNOP00000018961; -.
ChEMBL; CHEMBL4220; -.
iPTMnet; P35739; -.
PhosphoSitePlus; P35739; -.
PaxDb; P35739; -.
Ensembl; ENSRNOT00000018961; ENSRNOP00000018961; ENSRNOG00000013953. [P35739-1]
GeneID; 59109; -.
KEGG; rno:59109; -.
UCSC; RGD:620144; rat. [P35739-1]
CTD; 4914; -.
RGD; 620144; Ntrk1.
eggNOG; KOG1026; Eukaryota.
eggNOG; ENOG410YGKQ; LUCA.
GeneTree; ENSGT00760000118818; -.
HOGENOM; HOG000264255; -.
HOVERGEN; HBG056735; -.
InParanoid; P35739; -.
KO; K03176; -.
OMA; PEVYAIM; -.
OrthoDB; EOG091G01JY; -.
PhylomeDB; P35739; -.
TreeFam; TF106465; -.
BRENDA; 2.7.10.1; 5301.
Reactome; R-RNO-170968; Frs2-mediated activation.
Reactome; R-RNO-170984; ARMS-mediated activation.
Reactome; R-RNO-177504; Retrograde neurotrophin signalling.
Reactome; R-RNO-187042; TRKA activation by NGF.
Reactome; R-RNO-198203; PI3K/AKT activation.
PRO; PR:P35739; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000013953; -.
ExpressionAtlas; P35739; baseline and differential.
Genevisible; P35739; RN.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; ISO:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005004; F:GPI-linked ephrin receptor activity; IDA:BHF-UCL.
GO; GO:0019900; F:kinase binding; IPI:RGD.
GO; GO:0048406; F:nerve growth factor binding; IDA:RGD.
GO; GO:0010465; F:nerve growth factor receptor activity; ISS:UniProtKB.
GO; GO:0005166; F:neurotrophin p75 receptor binding; IPI:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:Reactome.
GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
GO; GO:0007202; P:activation of phospholipase C activity; TAS:Reactome.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0007411; P:axon guidance; IMP:RGD.
GO; GO:0060385; P:axonogenesis involved in innervation; ISS:UniProtKB.
GO; GO:0030183; P:B cell differentiation; ISO:RGD.
GO; GO:0061368; P:behavioral response to formalin induced pain; ISO:RGD.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:UniProtKB.
GO; GO:0071316; P:cellular response to nicotine; IDA:RGD.
GO; GO:0007623; P:circadian rhythm; ISO:RGD.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:RGD.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:RGD.
GO; GO:0060384; P:innervation; ISO:RGD.
GO; GO:0007611; P:learning or memory; IMP:RGD.
GO; GO:0042490; P:mechanoreceptor differentiation; ISO:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
GO; GO:1901215; P:negative regulation of neuron death; IDA:RGD.
GO; GO:0038180; P:nerve growth factor signaling pathway; IDA:UniProtKB.
GO; GO:0007399; P:nervous system development; ISO:RGD.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISS:UniProtKB.
GO; GO:0021553; P:olfactory nerve development; IEP:RGD.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISS:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0043068; P:positive regulation of programmed cell death; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISS:UniProtKB.
GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:RGD.
GO; GO:0010623; P:programmed cell death involved in cell development; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
GO; GO:0014823; P:response to activity; IDA:RGD.
GO; GO:0048678; P:response to axon injury; IEP:RGD.
GO; GO:0042493; P:response to drug; IDA:RGD.
GO; GO:0051602; P:response to electrical stimulus; IDA:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0051599; P:response to hydrostatic pressure; IEP:RGD.
GO; GO:0035094; P:response to nicotine; IDA:RGD.
GO; GO:0031667; P:response to nutrient levels; IDA:RGD.
GO; GO:0009314; P:response to radiation; IEP:RGD.
GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
GO; GO:0060009; P:Sertoli cell development; IMP:RGD.
GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0048485; P:sympathetic nervous system development; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR032675; LRR_dom_sf.
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; SM00409; IG; 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;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond; Endosome;
Glycoprotein; Immunoglobulin domain; Kinase; Leucine-rich repeat;
Membrane; Neurogenesis; Nucleotide-binding; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 799 High affinity nerve growth factor
receptor.
/FTId=PRO_0000016725.
TOPO_DOM 33 418 Extracellular. {ECO:0000255}.
TRANSMEM 419 442 Helical. {ECO:0000255}.
TOPO_DOM 443 799 Cytoplasmic. {ECO:0000255}.
REPEAT 90 113 LRR 1.
REPEAT 116 137 LRR 2.
DOMAIN 148 219 LRRCT.
DOMAIN 196 285 Ig-like C2-type 1.
DOMAIN 295 368 Ig-like C2-type 2.
DOMAIN 513 784 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 519 527 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 472 493 Interaction with SQSTM1.
ACT_SITE 653 653 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 547 547 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 499 499 Interaction with SHC1. {ECO:0000250}.
SITE 794 794 Interaction with PLCG1. {ECO:0000250}.
MOD_RES 499 499 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P04629}.
MOD_RES 679 679 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P04629}.
MOD_RES 683 683 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P04629}.
MOD_RES 684 684 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P04629}.
MOD_RES 794 794 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P04629}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 190 190 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 255 255 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 325 325 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 361 361 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 404 404 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 41 {ECO:0000250|UniProtKB:P04629}.
DISULFID 40 50 {ECO:0000250|UniProtKB:P04629}.
DISULFID 154 193 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 217 267 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 302 348 {ECO:0000250|UniProtKB:P04629}.
VAR_SEQ 396 401 Missing (in isoform TrkA-I).
{ECO:0000305}.
/FTId=VSP_002900.
MUTAGEN 527 527 V->D: Loss of kinase activity.
{ECO:0000269|PubMed:9856458}.
SEQUENCE 799 AA; 87868 MW; D564E8801E8978F8 CRC64;
MLRGQRHGQL GWHRPAAGLG GLVTSLMLAC ACAASCRETC CPVGPSGLRC TRAGTLNTLR
GLRGAGNLTE LYVENQRDLQ RLEFEDLQGL GELRSLTIVK SGLRFVAPDA FHFTPRLSHL
NLSSNALESL SWKTVQGLSL QDLTLSGNPL HCSCALLWLQ RWEQEDLCGV YTQKLQGSGS
GDQFLPLGHN NSCGVPSVKI QMPNDSVEVG DDVFLQCQVE GQALQQADWI LTELEGTATM
KKSGDLPSLG LTLVNVTSDL NKKNVTCWAE NDVGRAEVSV QVSVSFPASV HLGKAVEQHH
WCIPFSVDGQ PAPSLRWFFN GSVLNETSFI FTQFLESALT NETMRHGCLR LNQPTHVNNG
NYTLLAANPY GQAAASIMAA FMDNPFEFNP EDPIPVSFSP VDTNSTSRDP VEKKDETPFG
VSVAVGLAVS AALFLSALLL VLNKCGQRSK FGINRPAVLA PEDGLAMSLH FMTLGGSSLS
PTEGKGSGLQ GHIMENPQYF SDTCVHHIKR QDIILKWELG EGAFGKVFLA ECYNLLNDQD
KMLVAVKALK ETSENARQDF HREAELLTML QHQHIVRFFG VCTEGGPLLM VFEYMRHGDL
NRFLRSHGPD AKLLAGGEDV APGPLGLGQL LAVASQVAAG MVYLASLHFV HRDLATRNCL
VGQGLVVKIG DFGMSRDIYS TDYYRVGGRT MLPIRWMPPE SILYRKFSTE SDVWSFGVVL
WEIFTYGKQP WYQLSNTEAI ECITQGRELE RPRACPPDVY AIMRGCWQRE PQQRLSMKDV
HARLQALAQA PPSYLDVLG


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