NTRK2_CHICK
ID NTRK2_CHICK Reviewed; 818 AA.
AC Q91987; Q91010;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=BDNF/NT-3 growth factors receptor;
DE EC=2.7.10.1 {ECO:0000269|PubMed:8670834};
DE AltName: Full=Neurotrophic tyrosine kinase receptor type 2;
DE AltName: Full=TrkB tyrosine kinase;
DE Short=Trk-B;
DE Flags: Precursor;
GN Name=NTRK2; Synonyms=TRKB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10).
RC TISSUE=Brain;
RX PubMed=7959025; DOI=10.1016/0378-1119(94)90184-8;
RA Vinh N., Erdmann K., Heumann R.;
RT "Cloning and sequence analysis of a cDNA encoding a novel truncated form of
RT the chicken TrkB receptor.";
RL Gene 149:383-384(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=8287802; DOI=10.1242/dev.119.2.545;
RA Dechant G., Biffo S., Okazawa H., Kolbeck R., Pottgiesser J., Barde Y.-A.;
RT "Expression and binding characteristics of the BDNF receptor chick trkB.";
RL Development 119:545-558(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL NUCLEOTIDE SEQUENCE
RP (ISOFORMS 2; 3; 4; 5; 6; 7; 8; 9; 10; 11 AND 12).
RX PubMed=8774442; DOI=10.1523/jneurosci.16-05-01740.1996;
RA Garner A.S., Menegay H.J., Boeshore K.L., Xie X.Y., Voci J.M.,
RA Johnson J.E., Large T.H.;
RT "Expression of TrkB receptor isoforms in the developing avian visual
RT system.";
RL J. Neurosci. 16:1740-1752(1996).
RN [4]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 9), LIGAND-BINDING, FUNCTION,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8670834; DOI=10.1002/j.1460-2075.1996.tb00698.x;
RA Strohmaier C., Carter B.D., Urfer R., Barde Y.A., Dechant G.;
RT "A splice variant of the neurotrophin receptor trkB with increased
RT specificity for brain-derived neurotrophic factor.";
RL EMBO J. 15:3332-3337(1996).
CC -!- FUNCTION: Receptor tyrosine kinase involved in the development and the
CC maturation of the central and the peripheral nervous systems through
CC regulation of neuron survival, proliferation, migration,
CC differentiation, and synapse formation and plasticity. Receptor for
CC BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4
CC (PubMed:8287802, PubMed:8670834). Alternatively can also bind
CC NTF3/neurotrophin-3 which is less efficient in activating the receptor
CC but regulates neuron survival through NTRK2. Upon ligand-binding,
CC undergoes homodimerization, autophosphorylation and activation
CC (PubMed:8670834). Recruits, phosphorylates and/or activates several
CC downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that
CC regulate distinct overlapping signaling cascades. Through SHC1, FRS2,
CC SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for
CC instance neuronal differentiation including neurite outgrowth. Through
CC the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade
CC that mainly regulates growth and survival. Through PLCG1 and the
CC downstream protein kinase C-regulated pathways controls synaptic
CC plasticity. Thereby, plays a role in learning and memory by regulating
CC both short term synaptic function and long-term potentiation. PLCG1
CC also leads to NF-Kappa-B activation and the transcription of genes
CC involved in cell survival. Hence, it is able to suppress anoikis, the
CC apoptosis resulting from loss of cell-matrix interactions. May also
CC play a role in neutrophin-dependent calcium signaling in glial cells
CC and mediate communication between neurons and glia (By similarity).
CC {ECO:0000250|UniProtKB:P15209, ECO:0000269|PubMed:8287802,
CC ECO:0000269|PubMed:8670834}.
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 ECO:0000269|PubMed:8670834};
CC -!- ACTIVITY REGULATION: The neuronal activity and the influx of calcium
CC positively regulate the kinase activity and the internalization of the
CC receptor which are both important for active signaling. Regulated by
CC NGFR that may control the internalization of the receptor. NGFR may
CC also stimulate the activation by BDNF compared to NTF3 and NTF4. The
CC formation of active receptors dimers able to fully transduce the
CC ligand-mediated signal, may be negatively regulated by the formation of
CC inactive heterodimers with the non-catalytic isoforms (By similarity).
CC {ECO:0000250|UniProtKB:P15209, ECO:0000250|UniProtKB:Q63604}.
CC -!- SUBUNIT: Exists in a dynamic equilibrium between monomeric (low
CC affinity) and dimeric (high affinity) structures. Interacts
CC (phosphorylated upon activation by BDNF) with SHC1; mediates SHC1
CC phosphorylation and activation. Interacts (phosphorylated upon
CC activation by BDNF) with PLCG1 and/or PLCG2; mediates PLCG1
CC phosphorylation and activation. Interacts with SH2B1 and SH2B2.
CC Interacts with NGFR; may regulate the ligand specificity of the
CC receptor (By similarity). Interacts with SORCS2; this interaction is
CC important for normal targeting to post-synaptic densities in response
CC to high-frequency stimulation (By similarity). Interacts
CC (phosphorylated upon ligand-binding) with SH2D1A; regulates NTRK2.
CC Interacts with SQSTM1 and KIDINS220 (By similarity). Interacts
CC (phosphorylated upon ligand-binding) with FRS2; activates the MAPK
CC signaling pathway (By similarity). Interacts with APPL1 (By
CC similarity). Interacts with MAPK8IP3/JIP3 and KLC1; interaction with
CC KLC1 is mediated by MAPK8IP3/JIP3 (By similarity).
CC {ECO:0000250|UniProtKB:P04629, ECO:0000250|UniProtKB:P15209,
CC ECO:0000250|UniProtKB:Q63604}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8287802,
CC ECO:0000269|PubMed:8670834}; Single-pass type I membrane protein
CC {ECO:0000305}. Endosome membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q63604}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q63604}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q63604}. Postsynaptic density
CC {ECO:0000250|UniProtKB:P15209}. Note=Internalized to endosomes upon
CC ligand-binding. {ECO:0000250|UniProtKB:P15209}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Alpha-FL, cTrkB-L;
CC IsoId=Q91987-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta-FL;
CC IsoId=Q91987-2; Sequence=VSP_002914;
CC Name=3; Synonyms=ED;
CC IsoId=Q91987-3; Sequence=VSP_002915;
CC Name=4; Synonyms=JD;
CC IsoId=Q91987-4; Sequence=VSP_002923;
CC Name=5; Synonyms=J1;
CC IsoId=Q91987-5; Sequence=VSP_002920;
CC Name=6; Synonyms=Alpha-T1;
CC IsoId=Q91987-6; Sequence=VSP_002918, VSP_002919;
CC Name=7; Synonyms=J1+T1;
CC IsoId=Q91987-7; Sequence=VSP_002920, VSP_002918, VSP_002919;
CC Name=8; Synonyms=J2+T1;
CC IsoId=Q91987-8; Sequence=VSP_002921, VSP_002918, VSP_002919;
CC Name=9; Synonyms=ED J2+T1, cTrkB-S;
CC IsoId=Q91987-9; Sequence=VSP_002915, VSP_002921, VSP_002918,
CC VSP_002919;
CC Name=10; Synonyms=J1+J2+T1;
CC IsoId=Q91987-10; Sequence=VSP_002922, VSP_002918, VSP_002919;
CC Name=11; Synonyms=T3;
CC IsoId=Q91987-11; Sequence=VSP_002916, VSP_002917;
CC Name=12; Synonyms=ED J1+J2+T1;
CC IsoId=Q91987-12; Sequence=VSP_002915, VSP_002922, VSP_002918,
CC VSP_002919;
CC -!- TISSUE SPECIFICITY: Detected in embryonic brain and orsal root ganglia.
CC {ECO:0000269|PubMed:8287802, ECO:0000269|PubMed:8670834}.
CC -!- PTM: Ligand-mediated auto-phosphorylation.
CC {ECO:0000269|PubMed:8670834}.
CC -!- MISCELLANEOUS: [Isoform 2]: It is unsure whether Leu-144 or Met-188 is
CC the initiator of isoform 2. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 9]: Specifically activated by BDNF but not NTF3
CC and NTF4. {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; X77251; CAA54468.1; -; mRNA.
DR EMBL; X77252; CAA54469.1; -; mRNA.
DR EMBL; X74109; CAA52210.1; -; mRNA.
DR PIR; S59938; S44099.
DR PIR; S59939; S44098.
DR RefSeq; NP_990562.1; NM_205231.1. [Q91987-1]
DR RefSeq; XP_015135735.1; XM_015280249.1. [Q91987-5]
DR RefSeq; XP_015135738.1; XM_015280252.1. [Q91987-3]
DR RefSeq; XP_015135740.1; XM_015280254.1. [Q91987-10]
DR RefSeq; XP_015135741.1; XM_015280255.1. [Q91987-7]
DR RefSeq; XP_015135742.1; XM_015280256.1. [Q91987-8]
DR RefSeq; XP_015135743.1; XM_015280257.1. [Q91987-6]
DR AlphaFoldDB; Q91987; -.
DR SMR; Q91987; -.
DR STRING; 9031.ENSGALP00000020539; -.
DR PaxDb; Q91987; -.
DR Ensembl; ENSGALT00000020568; ENSGALP00000020539; ENSGALG00000012594. [Q91987-1]
DR Ensembl; ENSGALT00000086171; ENSGALP00000062213; ENSGALG00000012594. [Q91987-10]
DR Ensembl; ENSGALT00000090958; ENSGALP00000069579; ENSGALG00000012594. [Q91987-3]
DR Ensembl; ENSGALT00000093345; ENSGALP00000069010; ENSGALG00000012594. [Q91987-5]
DR Ensembl; ENSGALT00000094214; ENSGALP00000066233; ENSGALG00000012594. [Q91987-11]
DR Ensembl; ENSGALT00000097438; ENSGALP00000067848; ENSGALG00000012594. [Q91987-7]
DR Ensembl; ENSGALT00000106533; ENSGALP00000072387; ENSGALG00000012594. [Q91987-8]
DR GeneID; 396157; -.
DR KEGG; gga:396157; -.
DR CTD; 4915; -.
DR VEuPathDB; HostDB:geneid_396157; -.
DR eggNOG; KOG1026; Eukaryota.
DR GeneTree; ENSGT00940000155181; -.
DR HOGENOM; CLU_000288_74_1_1; -.
DR InParanoid; Q91987; -.
DR OMA; TCSCEIM; -.
DR OrthoDB; 295510at2759; -.
DR PhylomeDB; Q91987; -.
DR BRENDA; 2.7.10.1; 1306.
DR Reactome; R-GGA-9026527; Activated NTRK2 signals through PLCG1.
DR Reactome; R-GGA-9028731; Activated NTRK2 signals through FRS2 and FRS3.
DR Reactome; R-GGA-9032759; NTRK2 activates RAC1.
DR PRO; PR:Q91987; -.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000012594; Expressed in brain and 9 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0043679; C:axon terminus; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0048403; F:brain-derived neurotrophic factor binding; ISS:UniProtKB.
DR GO; GO:0060175; F:brain-derived neurotrophic factor receptor activity; ISS:UniProtKB.
DR GO; GO:0005004; F:GPI-linked ephrin receptor activity; IDA:BHF-UCL.
DR GO; GO:0043121; F:neurotrophin binding; ISS:UniProtKB.
DR GO; GO:0005030; F:neurotrophin receptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IDA:AgBase.
DR GO; GO:0031547; P:brain-derived neurotrophic factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IBA:GO_Central.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IBA:GO_Central.
DR GO; GO:0021954; P:central nervous system neuron development; ISS:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:0048668; P:collateral sprouting; IMP:BHF-UCL.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0048672; P:positive regulation of collateral sprouting; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:1903859; P:regulation of dendrite extension; IDA:AgBase.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IBA:GO_Central.
DR GO; GO:0099551; P:trans-synaptic signaling by neuropeptide, modulating synaptic transmission; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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; IPR003598; Ig_sub2.
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; IPR020455; NTRK2.
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; 2.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF16920; LRRCT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR01939; NTKRECEPTOR.
DR PRINTS; PR01941; NTKRECEPTOR2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SMART; SM00220; S_TKc; 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; Cell membrane; Cell projection;
KW Cytoplasm; Developmental protein; Differentiation; Disulfide bond;
KW Endosome; Glycoprotein; Immunoglobulin domain; Kinase; Leucine-rich repeat;
KW Membrane; Neurogenesis; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Synapse; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..818
FT /note="BDNF/NT-3 growth factors receptor"
FT /id="PRO_0000016730"
FT TOPO_DOM 32..426
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..818
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 71..92
FT /note="LRR 1"
FT REPEAT 95..116
FT /note="LRR 2"
FT DOMAIN 196..281
FT /note="Ig-like C2-type 1"
FT DOMAIN 295..364
FT /note="Ig-like C2-type 2"
FT DOMAIN 534..803
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 384..394
FT /note="Provides specificity for BDNF as ligand versus NTF3
FT and NTF4"
FT REGION 400..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 672
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 540..548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 568
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 512
FT /note="Interaction with SHC1"
FT /evidence="ECO:0000250"
FT SITE 702
FT /note="Interaction with SH2D1A"
FT /evidence="ECO:0000250"
FT SITE 813
FT /note="Interaction with PLCG1"
FT /evidence="ECO:0000250"
FT MOD_RES 512
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P15209"
FT MOD_RES 698
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q63604"
FT MOD_RES 702
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q63604"
FT MOD_RES 703
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q63604"
FT MOD_RES 813
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q63604"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 36..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 151..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 153..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 217..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 301..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002914"
FT VAR_SEQ 384..394
FT /note="Missing (in isoform 3, isoform 9 and isoform 12)"
FT /evidence="ECO:0000305"
FT /id="VSP_002915"
FT VAR_SEQ 462..467
FT /note="GPSSVI -> ERGRRK (in isoform 11)"
FT /evidence="ECO:0000305"
FT /id="VSP_002916"
FT VAR_SEQ 462..465
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_002923"
FT VAR_SEQ 462
FT /note="G -> VHGEVKGVGLVDQIWLSLQDCDNEEQVMVTVNSDVHNNSTASDNNRL
FT G (in isoform 10 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:7959025"
FT /id="VSP_002922"
FT VAR_SEQ 462
FT /note="G -> VHGEVKGVGLVDQIWLSLQDCDNEG (in isoform 5 and
FT isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_002920"
FT VAR_SEQ 462
FT /note="G -> EQVMVTVNSDVHNNSTASDNNRLG (in isoform 8 and
FT isoform 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_002921"
FT VAR_SEQ 463..473
FT /note="PSSVISNDDDS -> FVLFHKIPLDG (in isoform 6, isoform 7,
FT isoform 8, isoform 9, isoform 10 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:7959025"
FT /id="VSP_002918"
FT VAR_SEQ 468..818
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000305"
FT /id="VSP_002917"
FT VAR_SEQ 474..818
FT /note="Missing (in isoform 6, isoform 7, isoform 8, isoform
FT 9, isoform 10 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:7959025"
FT /id="VSP_002919"
SQ SEQUENCE 818 AA; 91737 MW; D1BA39E2092B2152 CRC64;
MVSWRRRPGP GLARLWGLCC LVLGCWRGAL GCPASCRCSS WRIWCSEPVP GITSFPVPQR
STEDDNVTEI YIANQRKLES INDNEVGFYV GLKNLTVVDS GLRFVSRQAF VKNINLQYIN
LSRNKLSSLS KKPFRHLGLS DLILVDNPFK CSCEIMWIKK FQETKFYTEA QDIYCVDDNN
KRIALMDMKV PNCDLPSANL SNYNITVVEG KSITLYCDTT GGPPPNVSWV LTNLVSNHES
DTSKNPASLT IKNVSSMDSG LWISCVAENI VGEVQTSAEL TVFFAPNITF IESPTPDHHW
CIPFTVKGNP KPTLQWFYEG AILNESEYIC TKIHVINQSE YHGCLQLDNP THLNNGAYTL
LAKNEYGEDE KRVDAHFMSV PGDGSGPIVD PDVYEYETTP NDLGDTTNNS NQITSPDVSN
KENEDSITVY VVVGIAALVC TGLVIMLIIL KFGRHSKFGM KGPSSVISND DDSASPLHHI
SNGSNTPSSS EGGPDAVIIG MTKIPVIENP QYFGITNSQL KPDTFVQHIK RHNIVLKREL
GEGAFGKVFL AECYNLCPEQ DKILVAVKTL KDASDNARKD FHREAELLTN LQHEHIVKFY
GVCVEGDPLI MVFEYMKHGD LNKFLRAHGP DAVLMAEGNR PAELTQSQML HIAQQIAAGM
VYLASQHFVH RDLATRNCLV GENLLVKIGD FGMSRDVYST DYYRVGGHTM LPIRWMPPES
IMYRKFTTES DVWSLGVVLW EIFTYGKQPW YQLSNNEVIE CITQGRVLQR PRTCPKEVYD
LMLGCWQREP HMRLNIKEIH SLLQNLAKAS PVYLDILG
