NTRK3_MOUSE
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 03-AUG-2022, entry version 158.
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 GlyGen; Q6VNS1; 14 sites, 5 N-linked glycans (3 sites).
DR iPTMnet; Q6VNS1; -.
DR PhosphoSitePlus; Q6VNS1; -.
DR MaxQB; Q6VNS1; -.
DR PaxDb; Q6VNS1; -.
DR PeptideAtlas; Q6VNS1; -.
DR PRIDE; Q6VNS1; -.
DR ProteomicsDB; 287838; -. [Q6VNS1-1]
DR ProteomicsDB; 287839; -. [Q6VNS1-2]
DR ProteomicsDB; 287840; -. [Q6VNS1-3]
DR Antibodypedia; 3979; 792 antibodies from 42 providers.
DR DNASU; 18213; -.
DR Ensembl; ENSMUST00000039431; ENSMUSP00000037909; ENSMUSG00000059146. [Q6VNS1-1]
DR Ensembl; ENSMUST00000039438; ENSMUSP00000038324; ENSMUSG00000059146. [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 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; RXVGGHT; -.
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 74 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 243 other tissues.
DR ExpressionAtlas; Q6VNS1; baseline and differential.
DR Genevisible; Q6VNS1; MM.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma 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:0090630; P:activation of GTPase activity; ISO:MGI.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISO:MGI.
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:0060548; P:negative regulation of cell death; 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:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:MGI.
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:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; 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:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; 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:0099151; P:regulation of postsynaptic density assembly; ISO:MGI.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:MGI.
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; 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; 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..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
