NTRK3_RAT
ID NTRK3_RAT Reviewed; 864 AA.
AC Q03351;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=NT-3 growth factor receptor;
DE EC=2.7.10.1;
DE AltName: Full=GP145-TrkC;
DE Short=Trk-C;
DE AltName: Full=Neurotrophic tyrosine kinase receptor type 3;
DE AltName: Full=TrkC tyrosine kinase;
DE Flags: Precursor;
GN Name=Ntrk3; Synonyms=Trkc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TRKC).
RX PubMed=1488112; DOI=10.1016/0306-4522(92)90292-a;
RA Merlio J.P., Ernfors P., Jaber M., Persson H.;
RT "Molecular cloning of rat trkC and distribution of cells expressing
RT messenger RNAs for members of the trk family in the rat central nervous
RT system.";
RL Neuroscience 51:513-532(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8494647; DOI=10.1016/0896-6273(93)90211-9;
RA Valenzuela D.M., Maisonpierre P.C., Glass D.J., Rojas E., Nunez L.,
RA Kong Y., Gies D.R., Stitt T.N., Ip N.Y., Yancopoulos G.D.;
RT "Alternative forms of rat TrkC with different functional capabilities.";
RL Neuron 10:963-974(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND FUNCTION.
RC TISSUE=Brain cortex, and Hippocampus;
RX PubMed=8494648; DOI=10.1016/0896-6273(93)90212-a;
RA Tsoulfas P., Soppet D., Escandon E., Tessarollo L., Mendoza-Ramirez J.-L.,
RA Rosenthal A., Nikolics K., Parada L.F.;
RT "The rat trkC locus encodes multiple neurogenic receptors that exhibit
RT differential response to neurotrophin-3 in PC12 cells.";
RL Neuron 10:975-990(1993).
RN [4]
RP INTERACTION WITH SH2B2.
RX PubMed=9856458; DOI=10.1016/s0896-6273(00)80620-0;
RA Qian X., Riccio A., Zhang Y., Ginty D.D.;
RT "Identification and characterization of novel substrates of Trk receptors
RT in developing neurons.";
RL Neuron 21:1017-1029(1998).
RN [5]
RP INTERACTION WITH SQSTM1.
RX PubMed=12471037; DOI=10.1074/jbc.m208468200;
RA Geetha T., Wooten M.W.;
RT "Association of the atypical protein kinase C-interacting protein p62/ZIP
RT with nerve growth factor receptor TrkA regulates receptor trafficking and
RT Erk5 signaling.";
RL J. Biol. Chem. 278:4730-4739(2003).
RN [6]
RP INTERACTION WITH KIDINS220.
RX PubMed=15167895; DOI=10.1038/sj.emboj.7600253;
RA Arevalo J.C., Yano H., Teng K.K., Chao M.V.;
RT "A unique pathway for sustained neurotrophin signaling through an ankyrin-
RT rich membrane-spanning protein.";
RL EMBO J. 23:2358-2368(2004).
RN [7]
RP INTERACTION WITH PTPRS.
RX PubMed=17967490; DOI=10.1016/j.bbamcr.2007.06.008;
RA Faux C., Hawadle M., Nixon J., Wallace A., Lee S., Murray S., Stoker A.;
RT "PTPsigma binds and dephosphorylates neurotrophin receptors and can
RT suppress NGF-dependent neurite outgrowth from sensory neurons.";
RL Biochim. Biophys. Acta 1773:1689-1700(2007).
RN [8]
RP INTERACTION WITH MAPK8IP3.
RX PubMed=21775604; DOI=10.1523/jneurosci.0436-11.2011;
RA Huang S.H., Duan S., Sun T., Wang J., Zhao L., Geng Z., Yan J., Sun H.J.,
RA Chen Z.Y.;
RT "JIP3 mediates TrkB axonal anterograde transport and enhances BDNF
RT signaling by directly bridging TrkB with kinesin-1.";
RL J. Neurosci. 31:10602-10614(2011).
CC -!- FUNCTION: Receptor tyrosine kinase involved in nervous system and
CC probably heart development. Upon binding of its ligand
CC NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different
CC signaling pathways, including the phosphatidylinositol 3-kinase/AKT and
CC the MAPK pathways, that control cell survival and differentiation (By
CC similarity). NTRK3 isoforms containing insertions within the kinase
CC domain can autophosphorylate in response to NTF3/neurotrophin-3, but
CC cannot mediate downstream phenotypic responses (PubMed:8494647,
CC PubMed:8494648). {ECO:0000250|UniProtKB:Q16288,
CC ECO:0000269|PubMed:8494647, ECO:0000269|PubMed:8494648}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Exists in a dynamic equilibrium between monomeric (low
CC affinity) and dimeric (high affinity) structures (By similarity). Binds
CC SH2B2 (PubMed:9856458). Interacts with SQSTM1 and KIDINS220
CC (PubMed:12471037, PubMed:15167895). Interacts with PTPRS
CC (PubMed:17967490). Interacts with MAPK8IP3/JIP3 (PubMed:21775604).
CC {ECO:0000250|UniProtKB:P04629, ECO:0000269|PubMed:12471037,
CC ECO:0000269|PubMed:15167895, ECO:0000269|PubMed:17967490,
CC ECO:0000269|PubMed:21775604, ECO:0000269|PubMed:9856458}.
CC -!- INTERACTION:
CC Q03351; Q03114: Cdk5; NbExp=2; IntAct=EBI-7365348, EBI-2008531;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=Additional isoforms seem to exist.;
CC Name=KI39; Synonyms=TRKC(KI39), TRKC-39;
CC IsoId=Q03351-1; Sequence=Displayed;
CC Name=TRKC;
CC IsoId=Q03351-2; Sequence=VSP_002936, VSP_002937;
CC Name=KI14; Synonyms=TRKC(KI14), TRKC-14;
CC IsoId=Q03351-3; Sequence=VSP_002936;
CC Name=KI25; Synonyms=TRKC-25;
CC IsoId=Q03351-4; Sequence=VSP_002937;
CC Name=IC158; Synonyms=TRKC(IC158), TRKCTK-;
CC IsoId=Q03351-5; Sequence=VSP_002934, VSP_002935;
CC Name=IC143; Synonyms=TRKC(IC143);
CC IsoId=Q03351-6; Sequence=VSP_002932, VSP_002933;
CC Name=IC113; Synonyms=TRKC(IC113);
CC IsoId=Q03351-7; Sequence=VSP_002930, VSP_002931;
CC Name=IC108; Synonyms=TRKC(IC108);
CC IsoId=Q03351-8; Sequence=VSP_002928, VSP_002929;
CC -!- TISSUE SPECIFICITY: Widely expressed, mainly in the nervous tissue.
CC -!- PTM: Ligand-mediated auto-phosphorylation.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; L03813; AAA42285.1; -; mRNA.
DR EMBL; L14445; AAA42282.1; -; mRNA.
DR EMBL; L14446; AAA42283.1; -; mRNA.
DR EMBL; L14447; AAA42284.1; -; mRNA.
DR EMBL; S60953; AAB26714.2; -; mRNA.
DR EMBL; S62924; AAB26716.2; -; mRNA.
DR EMBL; S62933; AAB26715.2; -; mRNA.
DR RefSeq; NP_001257584.1; NM_001270655.1. [Q03351-3]
DR RefSeq; NP_001257585.1; NM_001270656.1. [Q03351-1]
DR RefSeq; NP_062121.1; NM_019248.2. [Q03351-2]
DR RefSeq; XP_017444550.1; XM_017589061.1. [Q03351-4]
DR AlphaFoldDB; Q03351; -.
DR SMR; Q03351; -.
DR BioGRID; 248241; 7.
DR DIP; DIP-5718N; -.
DR IntAct; Q03351; 4.
DR MINT; Q03351; -.
DR STRING; 10116.ENSRNOP00000044402; -.
DR GlyGen; Q03351; 14 sites.
DR iPTMnet; Q03351; -.
DR PhosphoSitePlus; Q03351; -.
DR PaxDb; Q03351; -.
DR PRIDE; Q03351; -.
DR Ensembl; ENSRNOT00000025536; ENSRNOP00000025536; ENSRNOG00000018674. [Q03351-7]
DR Ensembl; ENSRNOT00000041839; ENSRNOP00000046059; ENSRNOG00000018674. [Q03351-2]
DR Ensembl; ENSRNOT00000045165; ENSRNOP00000049463; ENSRNOG00000018674. [Q03351-3]
DR Ensembl; ENSRNOT00000114826; ENSRNOP00000096233; ENSRNOG00000018674. [Q03351-8]
DR GeneID; 29613; -.
DR KEGG; rno:29613; -.
DR UCSC; RGD:3214; rat. [Q03351-1]
DR CTD; 4916; -.
DR RGD; 3214; Ntrk3.
DR VEuPathDB; HostDB:ENSRNOG00000018674; -.
DR eggNOG; KOG1026; Eukaryota.
DR GeneTree; ENSGT00940000155645; -.
DR HOGENOM; CLU_000288_74_1_1; -.
DR InParanoid; Q03351; -.
DR OMA; RXVGGHT; -.
DR OrthoDB; 295510at2759; -.
DR PhylomeDB; Q03351; -.
DR TreeFam; TF106465; -.
DR BRENDA; 2.7.10.1; 5301.
DR Reactome; R-RNO-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-RNO-9034013; NTF3 activates NTRK3 signaling.
DR Reactome; R-RNO-9034793; Activated NTRK3 signals through PLCG1.
DR Reactome; R-RNO-9603381; Activated NTRK3 signals through PI3K.
DR PRO; PR:Q03351; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018674; Expressed in frontal cortex and 18 other tissues.
DR ExpressionAtlas; Q03351; baseline and differential.
DR Genevisible; Q03351; RN.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005004; F:GPI-linked ephrin receptor activity; IDA:BHF-UCL.
DR GO; GO:0043121; F:neurotrophin binding; IBA:GO_Central.
DR GO; GO:0005030; F:neurotrophin receptor activity; ISO:RGD.
DR GO; GO:0002039; F:p53 binding; ISO:RGD.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; TAS:Reactome.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; ISO:RGD.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISO:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IBA:GO_Central.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0090102; P:cochlea development; IEP:RGD.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0070306; P:lens fiber cell differentiation; ISO:RGD.
DR GO; GO:0042490; P:mechanoreceptor differentiation; ISO:RGD.
DR GO; GO:0019056; P:modulation by virus of host transcription; IEP:RGD.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISO:RGD.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IMP:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0048665; P:neuron fate specification; IMP:RGD.
DR GO; GO:0001764; P:neuron migration; IMP:RGD.
DR GO; GO:0019227; P:neuronal action potential propagation; ISO:RGD.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IBA:GO_Central.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR020777; NTRK.
DR InterPro; IPR020446; NTRK3.
DR InterPro; IPR031635; NTRK_LRRCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF16920; LRRCT_2; 1.
DR Pfam; PF01462; LRRNT; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR PRINTS; PR01939; NTKRECEPTOR.
DR PRINTS; PR01942; NTKRECEPTOR3.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase;
KW Leucine-rich repeat; Membrane; Neurogenesis; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..864
FT /note="NT-3 growth factor receptor"
FT /id="PRO_0000016735"
FT TOPO_DOM 32..429
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..864
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 104..125
FT /note="LRR 1"
FT REPEAT 128..149
FT /note="LRR 2"
FT DOMAIN 160..209
FT /note="LRRCT"
FT DOMAIN 210..300
FT /note="Ig-like C2-type 1"
FT DOMAIN 309..382
FT /note="Ig-like C2-type 2"
FT DOMAIN 538..853
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 679
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 544..552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 572
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 516
FT /note="Interaction with SHC1"
FT /evidence="ECO:0000250"
FT SITE 859
FT /note="Interaction with PLC-gamma-1"
FT /evidence="ECO:0000250"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VNS1"
FT MOD_RES 516
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q16288"
FT MOD_RES 705
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 709
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 710
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 859
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..38
FT /evidence="ECO:0000250|UniProtKB:Q91044"
FT DISULFID 36..45
FT /evidence="ECO:0000250|UniProtKB:Q91044"
FT DISULFID 164..189
FT /evidence="ECO:0000250|UniProtKB:Q91044"
FT DISULFID 166..207
FT /evidence="ECO:0000250|UniProtKB:Q91044"
FT DISULFID 231..284
FT /evidence="ECO:0000250|UniProtKB:Q91044"
FT DISULFID 320..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 529..612
FT /note="YVQHIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLA
FT ARKDFQREAELLTNLQHEHIVKFYGVCGDGDP -> WVFSNIDNHGILNLKDNRDHLVP
FT STHYIYEEPEVQSGDVSYPRSHGFREIMLNPISLSGHSKPLNHGIYVEDVNVYFSKGRH
FT GF (in isoform IC158)"
FT /evidence="ECO:0000305"
FT /id="VSP_002934"
FT VAR_SEQ 529..597
FT /note="YVQHIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLA
FT ARKDFQREAELLTNLQH -> WVFSNIDNHGILNLKDNRDHLVPSTHYIYEEPEVQSGD
FT VSYPRSHGELLPLTSLYEVKPLPLPVLILKT (in isoform IC143)"
FT /evidence="ECO:0000305"
FT /id="VSP_002932"
FT VAR_SEQ 529..567
FT /note="YVQHIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKM -> CFREIMLNP
FT ISLSGHSKPLNHGIYVEDVNVYFSKGRHGF (in isoform IC113)"
FT /evidence="ECO:0000305"
FT /id="VSP_002930"
FT VAR_SEQ 529..562
FT /note="YVQHIKRRDIVLKRELGEGAFGKVFLAECYNLSP -> FGRIEGFAYGKRYV
FT VMTSVHCHPCWFRFGGLEWL (in isoform IC108)"
FT /evidence="ECO:0000305"
FT /id="VSP_002928"
FT VAR_SEQ 563..864
FT /note="Missing (in isoform IC108)"
FT /evidence="ECO:0000305"
FT /id="VSP_002929"
FT VAR_SEQ 568..864
FT /note="Missing (in isoform IC113)"
FT /evidence="ECO:0000305"
FT /id="VSP_002931"
FT VAR_SEQ 598..864
FT /note="Missing (in isoform IC143)"
FT /evidence="ECO:0000305"
FT /id="VSP_002933"
FT VAR_SEQ 613..864
FT /note="Missing (in isoform IC158)"
FT /evidence="ECO:0000305"
FT /id="VSP_002935"
FT VAR_SEQ 712..736
FT /note="Missing (in isoform KI14 and isoform TRKC)"
FT /evidence="ECO:0000303|PubMed:1488112"
FT /id="VSP_002936"
FT VAR_SEQ 737..750
FT /note="Missing (in isoform KI25 and isoform TRKC)"
FT /evidence="ECO:0000303|PubMed:1488112"
FT /id="VSP_002937"
SQ SEQUENCE 864 AA; 97064 MW; A202E993E208F636 CRC64;
MDVSLCPAKC SFWRIFLLGS VWLDYVGSVL ACPANCVCSK TEINCRRPDD GNLFPLLEGQ
DSGNSNGNAS INITDISRNI TSIHIENWRG LHTLNAVDME LYTGLQKLTI KNSGLRNIQP
RAFAKNPHLR YINLSSNRLT TLSWQLFQTL SLRELRLEQN FFNCSCDIRW MQLWQEQGEA
RLDSQSLYCI SADGSQLPLF RMNISQCDLP EISVSHVNLT VREGDNAVIT CNGSGSPLPD
VDWIVTGLQS INTHQTNLNW TNVHAINLTL VNVTSEDNGF TLTCIAENVV GMSNASVALT
VYYPPRVVSL VEPEVRLEHC IEFVVRGNPT PTLHWLYNGQ PLRESKIIHM DYYQEGEVSE
GCLLFNKPTH YNNGNYTLIA KNALGTANQT INGHFLKEPF PESTDFFDFE SDASPTPPIT
VTHKPEEDTF GVSIAVGLAA FACVLLVVLF IMINKYGRRS KFGMKGPVAV ISGEEDSASP
LHHINHGITT PSSLDAGPDT VVIGMTRIPV IENPQYFRQG HNCHKPDTYV QHIKRRDIVL
KRELGEGAFG KVFLAECYNL SPTKDKMLVA VKALKDPTLA ARKDFQREAE LLTNLQHEHI
VKFYGVCGDG DPLIMVFEYM KHGDLNKFLR AHGPDAMILV DGQPRQAKGE LGLSQMLHIA
SQIASGMVYL ASQHFVHRDL ATRNCLVGAN LLVKIGDFGM SRDVYSTDYY REGPYQKGPF
SVSWQQQRLA ASAASTLFNP SGNDFCIWCE VGGHTMLPIR WMPPESIMYR KFTTESDVWS
FGVILWEIFT YGKQPWFQLS NTEVIECITQ GRVLERPRVC PKEVYDVMLG CWQREPQQRL
NIKEIYKILH ALGKATPIYL DILG
