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   24-JAN-2024, entry version 213.
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   GlyCosmos; Q03351; 14 sites, No reported glycans.
DR   GlyGen; Q03351; 14 sites.
DR   iPTMnet; Q03351; -.
DR   PhosphoSitePlus; Q03351; -.
DR   PaxDb; 10116-ENSRNOP00000044402; -.
DR   Ensembl; ENSRNOT00000025536.6; ENSRNOP00000025536.4; ENSRNOG00000018674.9. [Q03351-7]
DR   Ensembl; ENSRNOT00000041839.4; ENSRNOP00000046059.1; ENSRNOG00000018674.9. [Q03351-2]
DR   Ensembl; ENSRNOT00000045165.4; ENSRNOP00000049463.1; ENSRNOG00000018674.9. [Q03351-3]
DR   Ensembl; ENSRNOT00000114826.1; ENSRNOP00000096233.1; ENSRNOG00000018674.9. [Q03351-8]
DR   Ensembl; ENSRNOT00055014935; ENSRNOP00055011904; ENSRNOG00055008845. [Q03351-1]
DR   Ensembl; ENSRNOT00060006109; ENSRNOP00060004523; ENSRNOG00060003667. [Q03351-1]
DR   Ensembl; ENSRNOT00065051242; ENSRNOP00065042181; ENSRNOG00065029604. [Q03351-1]
DR   GeneID; 29613; -.
DR   KEGG; rno:29613; -.
DR   UCSC; RGD:3214; rat. [Q03351-1]
DR   AGR; RGD:3214; -.
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   OrthoDB; 1614410at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; Q03351; baseline and differential.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
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:0048677; P:axon extension involved in regeneration; 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:0022011; P:myelination in peripheral nervous system; ISO:RGD.
DR   GO; GO:0048712; P:negative regulation of astrocyte differentiation; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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: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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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:0097107; P:postsynaptic density assembly; IDA:SynGO.
DR   GO; GO:2000177; P:regulation of neural precursor cell proliferation; IMP:RGD.
DR   GO; GO:0051896; P:regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central.
DR   GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
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   CDD; cd04971; IgI_TrKABC_d5; 1.
DR   CDD; cd05094; PTKc_TrkC; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR24416:SF66; NT-3 GROWTH FACTOR RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
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; Immunoglobulin; 2.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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.
DR   Genevisible; Q03351; RN.
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
//