ID   NTRK3_MOUSE             Reviewed;         825 AA.
AC   Q6VNS1; A4QPD0; Q9Z2P9; Q9Z2Q0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 167.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/cJ;
RX   PubMed=14614136; DOI=10.1073/pnas.2336152100;
RA   Yamauchi J., Chan J.R., Shooter E.M.;
RT   "Neurotrophin 3 activation of TrkC induces Schwann cell migration through
RT   the c-Jun N-terminal kinase pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:14421-14426(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=9802700;
RX   DOI=10.1002/(sici)1096-9861(19981109)401:1<47::aid-cne4>3.0.co;2-c;
RA   Menn B., Timsit S., Calothy G., Lamballe F.;
RT   "Differential expression of TrkC catalytic and noncatalytic isoforms
RT   suggests that they act independently or in association.";
RL   J. Comp. Neurol. 401:47-64(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-516, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Brown adipose tissue;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   INDUCTION.
RX   PubMed=23785138; DOI=10.1523/jneurosci.2757-12.2013;
RA   Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F.,
RA   Sassone-Corsi P., Ptacek L.J., Akassoglou K.;
RT   "p75 neurotrophin receptor is a clock gene that regulates oscillatory
RT   components of circadian and metabolic networks.";
RL   J. Neurosci. 33:10221-10234(2013).
RN   [7]
RP   INTERACTION WITH PTPRS.
RX   PubMed=25385546; DOI=10.1038/ncomms6209;
RA   Coles C.H., Mitakidis N., Zhang P., Elegheert J., Lu W., Stoker A.W.,
RA   Nakagawa T., Craig A.M., Jones E.Y., Aricescu A.R.;
RT   "Structural basis for extracellular cis and trans RPTPsigma signal
RT   competition in synaptogenesis.";
RL   Nat. Commun. 5:5209-5209(2014).
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.
CC       {ECO:0000250|UniProtKB:Q16288}.
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. Interacts with SQSTM1 and KIDINS220 (By similarity). Interacts
CC       with PTPRS (PubMed:25385546).Interacts with MAPK8IP3/JIP3 (By
CC       similarity). {ECO:0000250|UniProtKB:P04629,
CC       ECO:0000250|UniProtKB:Q03351, ECO:0000269|PubMed:25385546}.
CC   -!- INTERACTION:
CC       Q6VNS1; Q2MHE5: Dok6; NbExp=3; IntAct=EBI-16744951, EBI-20585476;
CC       Q6VNS1; P16056: Met; NbExp=5; IntAct=EBI-16744951, EBI-1798780;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6VNS1-1; Sequence=Displayed;
CC       Name=2; Synonyms=TrkC NC1;
CC         IsoId=Q6VNS1-2; Sequence=VSP_021596, VSP_021597;
CC       Name=3; Synonyms=TrkC NC2;
CC         IsoId=Q6VNS1-3; Sequence=VSP_021598, VSP_021599;
CC   -!- TISSUE SPECIFICITY: Isoform 2 expression is restricted to specific
CC       areas in adult brain. Isoform 3 transcripts are readily detected early
CC       during embryogenesis and are expressed predominantly in adult brain and
CC       gonads. {ECO:0000269|PubMed:9802700}.
CC   -!- INDUCTION: Expression oscillates in a circadian manner in the liver.
CC       {ECO:0000269|PubMed:23785138}.
CC   -!- PTM: Ligand-mediated auto-phosphorylation. {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Non-catalytic. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 3]: Non-catalytic. {ECO:0000305}.
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; AY336094; AAP94280.1; -; mRNA.
DR   EMBL; AF035399; AAC72289.1; -; mRNA.
DR   EMBL; AF035400; AAC72290.1; -; mRNA.
DR   EMBL; BC139764; AAI39765.1; -; mRNA.
DR   CCDS; CCDS21371.1; -. [Q6VNS1-1]
DR   CCDS; CCDS21372.1; -. [Q6VNS1-3]
DR   RefSeq; NP_032772.3; NM_008746.5. [Q6VNS1-1]
DR   RefSeq; NP_877961.1; NM_182809.2. [Q6VNS1-3]
DR   AlphaFoldDB; Q6VNS1; -.
DR   SMR; Q6VNS1; -.
DR   BioGRID; 201870; 2.
DR   IntAct; Q6VNS1; 3.
DR   MINT; Q6VNS1; -.
DR   STRING; 10090.ENSMUSP00000037909; -.
DR   ChEMBL; CHEMBL2791; -.
DR   GlyConnect; 2805; 5 N-Linked glycans (3 sites).
DR   GlyCosmos; Q6VNS1; 14 sites, 5 glycans.
DR   GlyGen; Q6VNS1; 15 sites, 5 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q6VNS1; -.
DR   PhosphoSitePlus; Q6VNS1; -.
DR   MaxQB; Q6VNS1; -.
DR   PaxDb; 10090-ENSMUSP00000037909; -.
DR   PeptideAtlas; Q6VNS1; -.
DR   ProteomicsDB; 287838; -. [Q6VNS1-1]
DR   ProteomicsDB; 287839; -. [Q6VNS1-2]
DR   ProteomicsDB; 287840; -. [Q6VNS1-3]
DR   Antibodypedia; 3979; 920 antibodies from 42 providers.
DR   DNASU; 18213; -.
DR   Ensembl; ENSMUST00000039431.14; ENSMUSP00000037909.8; ENSMUSG00000059146.13. [Q6VNS1-1]
DR   Ensembl; ENSMUST00000039438.9; ENSMUSP00000038324.8; ENSMUSG00000059146.13. [Q6VNS1-3]
DR   GeneID; 18213; -.
DR   KEGG; mmu:18213; -.
DR   UCSC; uc009hxf.2; mouse. [Q6VNS1-1]
DR   UCSC; uc009hxh.2; mouse. [Q6VNS1-3]
DR   UCSC; uc009hxi.2; mouse. [Q6VNS1-2]
DR   AGR; MGI:97385; -.
DR   CTD; 4916; -.
DR   MGI; MGI:97385; Ntrk3.
DR   VEuPathDB; HostDB:ENSMUSG00000059146; -.
DR   eggNOG; KOG1026; Eukaryota.
DR   GeneTree; ENSGT00940000155645; -.
DR   HOGENOM; CLU_000288_74_1_1; -.
DR   InParanoid; Q6VNS1; -.
DR   OMA; STDYYRX; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; Q6VNS1; -.
DR   TreeFam; TF106465; -.
DR   Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
DR   Reactome; R-MMU-9034013; NTF3 activates NTRK3 signaling.
DR   Reactome; R-MMU-9034793; Activated NTRK3 signals through PLCG1.
DR   Reactome; R-MMU-9603381; Activated NTRK3 signals through PI3K.
DR   BioGRID-ORCS; 18213; 1 hit in 79 CRISPR screens.
DR   ChiTaRS; Ntrk3; mouse.
DR   PRO; PR:Q6VNS1; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q6VNS1; Protein.
DR   Bgee; ENSMUSG00000059146; Expressed in ascending aorta and 245 other cell types or tissues.
DR   ExpressionAtlas; Q6VNS1; baseline and differential.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005004; F:GPI-linked ephrin receptor activity; ISO:MGI.
DR   GO; GO:0043121; F:neurotrophin binding; IBA:GO_Central.
DR   GO; GO:0005030; F:neurotrophin receptor activity; ISO:MGI.
DR   GO; GO:0002039; F:p53 binding; ISO:MGI.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0048677; P:axon extension involved in regeneration; IGI:MGI.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IBA:GO_Central.
DR   GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR   GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR   GO; GO:0070306; P:lens fiber cell differentiation; IGI:MGI.
DR   GO; GO:0042490; P:mechanoreceptor differentiation; IMP:MGI.
DR   GO; GO:0022011; P:myelination in peripheral nervous system; IGI:MGI.
DR   GO; GO:0048712; P:negative regulation of astrocyte differentiation; ISO:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0048665; P:neuron fate specification; ISO:MGI.
DR   GO; GO:0001764; P:neuron migration; ISO:MGI.
DR   GO; GO:0019227; P:neuronal action potential propagation; IGI:MGI.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR   GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; IGI:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
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:MGI.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR   GO; GO:0097107; P:postsynaptic density assembly; ISO:MGI.
DR   GO; GO:2000177; P:regulation of neural precursor cell proliferation; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:MGI.
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; 1.
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; Q6VNS1; MM.
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..825
FT                   /note="NT-3 growth factor receptor"
FT                   /id="PRO_0000260434"
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..825
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..825
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            820
FT                   /note="Interaction with PLC-gamma-1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         493
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         516
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
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   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         467..502
FT                   /note="PVAVISGEEDSASPLHHINHGITTPSSLDAGPDTVV -> KVLFFQSQEFHG
FT                   FHLLIKRYCTSICSLRKPLVTGPW (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9802700"
FT                   /id="VSP_021596"
FT   VAR_SEQ         503..825
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9802700"
FT                   /id="VSP_021597"
FT   VAR_SEQ         529..612
FT                   /note="YVQHIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLA
FT                   ARKDFQREAELLTNLQHEHIVKFYGVCGDGDP -> WVFSNIDNHGILNLKDNRDHLVP
FT                   STHYIYEEPEVQSGDVSYPRSHGFREIMLNPISLSGHSKPLNHGIYVEDVNVYFSKGRH
FT                   GF (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9802700"
FT                   /id="VSP_021598"
FT   VAR_SEQ         613..825
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9802700"
FT                   /id="VSP_021599"
FT   CONFLICT        366
FT                   /note="N -> K (in Ref. 2; AAC72289)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   825 AA;  92760 MW;  4DE08AB546CC5BD6 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 RVGGHTMLPI
     RWMPPESIMY RKFTTESDVW SFGVILWEIF TYGKQPWFQL SNTEVIECIT QGRVLERPRV
     CPKEVYDVML GCWQREPQQR LNIKEIYKIL HALGKATPIY LDILG
//