P35739 (NTRK1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
High affinity nerve growth factor receptor
EC=2.7.10.1

Alternative name(s):
Neurotrophic tyrosine kinase receptor type 1
Slow nerve growth factor receptor
p140-TrkA
Short name=Trk-A

Gene names

Name:	Ntrk1
Synonyms:	Trk, Trka

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	799 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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, it 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. Ref.13
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
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. Ref.10
Subunit structure	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. 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. Interacts with RAB7A. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Subcellular location	Cell membrane; Single-pass type I membrane protein By similarity. Early endosome membrane; Single-pass type I membrane protein. Note: Internalized to endosomes upon binding of NGF or NTF3 and further transported to the cell body via a retrograde axonal transport. Ref.7
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. Ref.7 Ref.8 Ref.9 The extracellular domain mediates interaction with NGFR. Ref.7 Ref.8 Ref.9
Post-translational modification	Ligand-mediated autophosphorylation. Interaction with SQSTM1 is phosphotyrosine-dependent. Autophosphorylation at Tyr-499 mediates interaction and phosphorylation of SHC1. N-glycosylated By similarity. Ubiquitinated. Undergoes polyubiquitination upon activation; regulated by NGFR. Ubiquitination regulates the internalization of the receptor By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. Contains 2 Ig-like C2-type (immunoglobulin-like) domains. Contains 2 LRR (leucine-rich) repeats. Contains 1 LRRCT domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis
Cellular component	Cell membrane Endosome Membrane
Coding sequence diversity	Alternative splicing
Domain	Immunoglobulin domain Leucine-rich repeat Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Inferred from electronic annotation. Source: Compara Sertoli cell development Inferred from mutant phenotype PubMed 18660385. Source: RGD aging Inferred from expression pattern PubMed 21059364. Source: RGD axon guidance Inferred from mutant phenotype PubMed 18344912. Source: RGD axonogenesis involved in innervation Inferred from sequence or structural similarity. Source: UniProtKB cellular response to growth factor stimulus Inferred from direct assay PubMed 19029245. Source: MGI cellular response to nicotine Inferred from direct assay PubMed 16280603. Source: RGD detection of mechanical stimulus involved in sensory perception of pain Inferred from mutant phenotype PubMed 20351485. Source: RGD detection of temperature stimulus involved in sensory perception of pain Inferred from mutant phenotype PubMed 20351485. Source: RGD developmental programmed cell death Inferred from direct assay Ref.13. Source: UniProtKB learning or memory Inferred from mutant phenotype PubMed 18440710. Source: RGD mechanoreceptor differentiation Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of neuron apoptotic process Inferred from mutant phenotype PubMed 19146958. Source: RGD olfactory nerve development Inferred from expression pattern PubMed 8778281. Source: RGD positive regulation of ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of Ras GTPase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of Ras protein signal transduction Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of angiogenesis Inferred from electronic annotation. Source: Compara positive regulation of neuron projection development Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of programmed cell death Inferred from direct assay Ref.13. Source: UniProtKB positive regulation of synaptic transmission, glutamatergic Inferred from mutant phenotype PubMed 21550171. Source: RGD protein autophosphorylation Inferred from direct assay PubMed 19029245. Source: MGI response to activity Inferred from direct assay PubMed 19800940. Source: RGD response to axon injury Inferred from expression pattern PubMed 21456016. Source: RGD response to drug Inferred from direct assay PubMed 20059802. Source: RGD response to electrical stimulus Inferred from direct assay PubMed 19596387. Source: RGD response to ethanol Inferred from expression pattern PubMed 17316397. Source: RGD response to hydrostatic pressure Inferred from expression pattern PubMed 18817846. Source: RGD response to nutrient levels Inferred from direct assay PubMed 17582385. Source: RGD response to radiation Inferred from expression pattern PubMed 21431457. Source: RGD sympathetic nervous system development Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome axon Inferred from direct assay PubMed 11134589. Source: RGD cell surface Inferred from direct assay PubMed 19029245. Source: MGI cytoplasmic vesicle Inferred from direct assay PubMed 17625349. Source: RGD dendrite Inferred from direct assay PubMed 11134589. Source: RGD early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB neuronal cell body Inferred from direct assay PubMed 18395621. Source: RGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nerve growth factor binding Inferred from sequence or structural similarity. Source: UniProtKB nerve growth factor receptor activity Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB transmembrane receptor protein tyrosine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Both isoforms have similar biological properties.

Isoform TrkA-II (identifier: P35739-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform TrkA-I (identifier: P35739-2)

The sequence of this isoform differs from the canonical sequence as follows:
     396-401: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 32	32	Potential
	Chain	33 – 799	767	High affinity nerve growth factor receptor		PRO_0000016725
Regions
	Topological domain	33 – 418	386	Extracellular Potential
	Transmembrane	419 – 442	24	Helical; Potential
	Topological domain	443 – 799	357	Cytoplasmic Potential
	Repeat	90 – 113	24	LRR 1
	Repeat	116 – 137	22	LRR 2
	Domain	148 – 219	72	LRRCT
	Domain	196 – 285	90	Ig-like C2-type 1
	Domain	295 – 368	74	Ig-like C2-type 2
	Domain	513 – 784	272	Protein kinase
	Nucleotide binding	519 – 527	9	ATP By similarity
	Region	472 – 493	22	Interaction with SQSTM1
Sites
	Active site	653	1	Proton acceptor By similarity
	Binding site	547	1	ATP By similarity
	Site	499	1	Interaction with SHC1 By similarity
	Site	794	1	Interaction with PLCG1 By similarity
Amino acid modifications
	Modified residue	499	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	679	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	683	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	684	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	794	1	Phosphotyrosine; by autocatalysis By similarity
	Glycosylation	67	1	N-linked (GlcNAc...) Potential
	Glycosylation	121	1	N-linked (GlcNAc...) Potential
	Glycosylation	190	1	N-linked (GlcNAc...) Potential
	Glycosylation	204	1	N-linked (GlcNAc...) Potential
	Glycosylation	255	1	N-linked (GlcNAc...) Potential
	Glycosylation	264	1	N-linked (GlcNAc...) Potential
	Glycosylation	320	1	N-linked (GlcNAc...) Potential
	Glycosylation	325	1	N-linked (GlcNAc...) Potential
	Glycosylation	341	1	N-linked (GlcNAc...) Potential
	Glycosylation	361	1	N-linked (GlcNAc...) Potential
	Glycosylation	404	1	N-linked (GlcNAc...) Potential
	Disulfide bond	154 ↔ 193		By similarity
	Disulfide bond	217 ↔ 267		By similarity
Natural variations
	Alternative sequence	396 – 401	6	Missing in isoform TrkA-I.		VSP_002900
Experimental info
	Mutagenesis	527	1	V → D: Loss of kinase activity. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform TrkA-II [UniParc]. Last modified June 1, 1994. Version 1. Checksum: D564E8801E8978F8	FASTA	799	87,868
	10 20 30 40 50 60 MLRGQRHGQL GWHRPAAGLG GLVTSLMLAC ACAASCRETC CPVGPSGLRC TRAGTLNTLR 70 80 90 100 110 120 GLRGAGNLTE LYVENQRDLQ RLEFEDLQGL GELRSLTIVK SGLRFVAPDA FHFTPRLSHL 130 140 150 160 170 180 NLSSNALESL SWKTVQGLSL QDLTLSGNPL HCSCALLWLQ RWEQEDLCGV YTQKLQGSGS 190 200 210 220 230 240 GDQFLPLGHN NSCGVPSVKI QMPNDSVEVG DDVFLQCQVE GQALQQADWI LTELEGTATM 250 260 270 280 290 300 KKSGDLPSLG LTLVNVTSDL NKKNVTCWAE NDVGRAEVSV QVSVSFPASV HLGKAVEQHH 310 320 330 340 350 360 WCIPFSVDGQ PAPSLRWFFN GSVLNETSFI FTQFLESALT NETMRHGCLR LNQPTHVNNG 370 380 390 400 410 420 NYTLLAANPY GQAAASIMAA FMDNPFEFNP EDPIPVSFSP VDTNSTSRDP VEKKDETPFG 430 440 450 460 470 480 VSVAVGLAVS AALFLSALLL VLNKCGQRSK FGINRPAVLA PEDGLAMSLH FMTLGGSSLS 490 500 510 520 530 540 PTEGKGSGLQ GHIMENPQYF SDTCVHHIKR QDIILKWELG EGAFGKVFLA ECYNLLNDQD 550 560 570 580 590 600 KMLVAVKALK ETSENARQDF HREAELLTML QHQHIVRFFG VCTEGGPLLM VFEYMRHGDL 610 620 630 640 650 660 NRFLRSHGPD AKLLAGGEDV APGPLGLGQL LAVASQVAAG MVYLASLHFV HRDLATRNCL 670 680 690 700 710 720 VGQGLVVKIG DFGMSRDIYS TDYYRVGGRT MLPIRWMPPE SILYRKFSTE SDVWSFGVVL 730 740 750 760 770 780 WEIFTYGKQP WYQLSNTEAI ECITQGRELE RPRACPPDVY AIMRGCWQRE PQQRLSMKDV 790 HARLQALAQA PPSYLDVLG
	Isoform TrkA-I [UniParc]. Checksum: A4A5D0B76B08655D	FASTA	793	87,252
	10 20 30 40 50 60 MLRGQRHGQL GWHRPAAGLG GLVTSLMLAC ACAASCRETC CPVGPSGLRC TRAGTLNTLR 70 80 90 100 110 120 GLRGAGNLTE LYVENQRDLQ RLEFEDLQGL GELRSLTIVK SGLRFVAPDA FHFTPRLSHL 130 140 150 160 170 180 NLSSNALESL SWKTVQGLSL QDLTLSGNPL HCSCALLWLQ RWEQEDLCGV YTQKLQGSGS 190 200 210 220 230 240 GDQFLPLGHN NSCGVPSVKI QMPNDSVEVG DDVFLQCQVE GQALQQADWI LTELEGTATM 250 260 270 280 290 300 KKSGDLPSLG LTLVNVTSDL NKKNVTCWAE NDVGRAEVSV QVSVSFPASV HLGKAVEQHH 310 320 330 340 350 360 WCIPFSVDGQ PAPSLRWFFN GSVLNETSFI FTQFLESALT NETMRHGCLR LNQPTHVNNG 370 380 390 400 410 420 NYTLLAANPY GQAAASIMAA FMDNPFEFNP EDPIPDTNST SRDPVEKKDE TPFGVSVAVG 430 440 450 460 470 480 LAVSAALFLS ALLLVLNKCG QRSKFGINRP AVLAPEDGLA MSLHFMTLGG SSLSPTEGKG 490 500 510 520 530 540 SGLQGHIMEN PQYFSDTCVH HIKRQDIILK WELGEGAFGK VFLAECYNLL NDQDKMLVAV 550 560 570 580 590 600 KALKETSENA RQDFHREAEL LTMLQHQHIV RFFGVCTEGG PLLMVFEYMR HGDLNRFLRS 610 620 630 640 650 660 HGPDAKLLAG GEDVAPGPLG LGQLLAVASQ VAAGMVYLAS LHFVHRDLAT RNCLVGQGLV 670 680 690 700 710 720 VKIGDFGMSR DIYSTDYYRV GGRTMLPIRW MPPESILYRK FSTESDVWSF GVVLWEIFTY 730 740 750 760 770 780 GKQPWYQLSN TEAIECITQG RELERPRACP PDVYAIMRGC WQREPQQRLS MKDVHARLQA 790 LAQAPPSYLD VLG

References

[1]	"The rat trk protooncogene product exhibits properties characteristic of the slow nerve growth factor receptor." Meakin S.O., Suter U., Drinkwater C.C., Welcher A.A., Shooter E.M. Proc. Natl. Acad. Sci. U.S.A. 89:2374-2378(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TRKA-II).
[2]	"Tissue-specific alternative splicing generates two isoforms of the trkA receptor." Barker P.A., Lomen-Hoerth C., Gensch E.M., Meakin S.O., Glass D.J., Shooter E.M. J. Biol. Chem. 268:15150-15157(1993) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS TRKA-I AND TRKA-II).
[3]	"Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses." Stephens R.M., Loeb D.M., Copeland T.D., Pawson T., Greene L.A., Kaplan D.R. Neuron 12:691-705(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SHC1.
[4]	"Identification and characterization of novel substrates of Trk receptors in developing neurons." Qian X., Riccio A., Zhang Y., Ginty D.D. Neuron 21:1017-1029(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLCG1; SHC1; SH2B1 AND SH2B2, MUTAGENESIS OF VAL-527.
[5]	"The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor." Wooten M.W., Seibenhener M.L., Mamidipudi V., Diaz-Meco M.T., Barker P.A., Moscat J. J. Biol. Chem. 276:7709-7712(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SQSTM1.
[6]	"An evolutionarily conserved transmembrane protein that is a novel downstream target of neurotrophin and ephrin receptors." Kong H., Boulter J., Weber J.L., Lai C., Chao M.V. J. Neurosci. 21:176-185(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KIDINS220.
[7]	"Association of the atypical protein kinase C-interacting protein p62/ZIP with nerve growth factor receptor TrkA regulates receptor trafficking and Erk5 signaling." Geetha T., Wooten M.W. J. Biol. Chem. 278:4730-4739(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION, DOMAIN.
[8]	"A unique pathway for sustained neurotrophin signaling through an ankyrin-rich membrane-spanning protein." Arevalo J.C., Yano H., Teng K.K., Chao M.V. EMBO J. 23:2358-2368(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KIDINS220, DOMAIN.
[9]	"Ternary complex with Trk, p75, and an ankyrin-rich membrane spanning protein." Chang M.-S., Arevalo J.C., Chao M.V. J. Neurosci. Res. 78:186-192(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NGFR AND KIDINS220, DOMAIN.
[10]	"SLAM-associated protein as a potential negative regulator in Trk signaling." Lo K.Y., Chin W.H., Ng Y.P., Cheng A.W., Cheung Z.H., Ip N.Y. J. Biol. Chem. 280:41744-41752(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, INTERACTION WITH SH2D1A.
[11]	"The small GTPase Rab7 controls the endosomal trafficking and neuritogenic signaling of the nerve growth factor receptor TrkA." Saxena S., Bucci C., Weis J., Kruttgen A. J. Neurosci. 25:10930-10940(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB7A.
[12]	"Neurotrophin receptor homolog-2 regulates nerve growth factor signaling." Wong A.W., Willingham M., Xiao J., Kilpatrick T.J., Murray S.S. J. Neurochem. 106:1964-1976(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NRADD.
[13]	"Neurotrophin receptors TrkA and TrkC cause neuronal death whereas TrkB does not." Nikoletopoulou V., Lickert H., Frade J.M., Rencurel C., Giallonardo P., Zhang L., Bibel M., Barde Y.A. Nature 467:59-63(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL DEATH.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M85214 mRNA. Translation: AAA42286.1. L12225 Genomic DNA. No translation available.
IPI	IPI00201638. IPI00231206.
PIR	TVRTTB. A41981.
RefSeq	NP_067600.1. NM_021589.1.
UniGene	Rn.39098.
3D structure databases
ProteinModelPortal	P35739.
SMR	P35739. Positions 36-385.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5716N.
IntAct	P35739. 1 interaction.
MINT	MINT-191667.
PTM databases
PhosphoSite	P35739.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000018961; ENSRNOP00000018961; ENSRNOG00000013953. ENSRNOT00000044046; ENSRNOP00000048885; ENSRNOG00000013953.
GeneID	59109.
KEGG	rno:59109.
UCSC	RGD:620144. rat.
Organism-specific databases
CTD	4914.
RGD	620144. Ntrk1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00700000104172.
HOGENOM	HOG000264255.
HOVERGEN	HBG056735.
InParanoid	P35739.
KO	K03176.
OMA	CPDACCP.
OrthoDB	EOG4J3WGJ.
Enzyme and pathway databases
BRENDA	2.7.10.1. 5301.
Reactome	REACT_111984. Signal Transduction.
Gene expression databases
Genevestigator	P35739.
GermOnline	ENSRNOG00000013953. Rattus norvegicus.
Family and domain databases
Gene3D	2.60.40.10. 2 hits.
InterPro	IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. IPR003599. Ig_sub. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. IPR020461. Tyr_kinase_neurotrophic_rcpt_1. IPR020777. Tyr_kinase_NGF_rcpt. IPR002011. Tyr_kinase_rcpt_2_CS. [Graphical view]
Pfam	PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PRINTS	PR01939. NTKRECEPTOR. PR01940. NTKRECEPTOR1. PR00109. TYRKINASE.
SMART	SM00409. IG. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS50835. IG_LIKE. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS00239. RECEPTOR_TYR_KIN_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL4220.
NextBio	611747.

Entry information

Entry name

NTRK1_RAT

Accession

Primary (citable) accession number: P35739

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	April 3, 2013
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program