FGR1A_DANRE
ID FGR1A_DANRE Reviewed; 810 AA.
AC Q90Z00; A2BEU6; A2BEU7; A4JYD6; B3DGB8; Q1LY25; Q800Y8; Q800Y9; Q800Z0;
AC Q800Z1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Fibroblast growth factor receptor 1-A;
DE Short=FGFR-1-A;
DE Short=bFGF-R-1-A;
DE EC=2.7.10.1;
DE AltName: Full=Basic fibroblast growth factor receptor 1-A;
DE Flags: Precursor;
GN Name=fgfr1a; Synonyms=fgfr1; ORFNames=si:ch211-198o12.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 10-378 (ISOFORM 5), AND TISSUE SPECIFICITY.
RX PubMed=15221377; DOI=10.1007/s00427-004-0409-1;
RA Scholpp S., Groth C., Lohs C., Lardelli M., Brand M.;
RT "Zebrafish fgfr1 is a member of the fgf8 synexpression group and is
RT required for fgf8 signalling at the midbrain-hindbrain boundary.";
RL Dev. Genes Evol. 214:285-295(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-478 (ISOFORM 1).
RX PubMed=18296487; DOI=10.1101/gr.7187808;
RA Bushell K.M., Soellner C., Schuster-Boeckler B., Bateman A., Wright G.J.;
RT "Large-scale screening for novel low-affinity extracellular protein
RT interactions.";
RL Genome Res. 18:622-630(2008).
RN [5]
RP INTERACTION WITH CNPY1.
RX PubMed=16488878; DOI=10.1016/j.cub.2006.01.055;
RA Hirate Y., Okamoto H.;
RT "Canopy1, a novel regulator of FGF signaling around the midbrain-hindbrain
RT boundary in zebrafish.";
RL Curr. Biol. 16:421-427(2006).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
CC for fibroblast growth factors and plays an essential role in the
CC regulation of embryonic development, cell proliferation,
CC differentiation and migration. Required for normal mesoderm patterning
CC and normal skeletogenesis. Phosphorylates PLCG1, FRS2, GAB1 and SHB.
CC Ligand binding leads to the activation of several signaling cascades.
CC Activation of PLCG1 leads to the production of the cellular signaling
CC molecules diacylglycerol and inositol-1,4,5-trisphosphate.
CC Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and
CC SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the
CC MAP kinase signaling pathway, as well as of the AKT1 signaling pathway.
CC Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the
CC nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the
CC regulation of transcription. FGFR1 signaling is down-regulated by
CC ubiquitination, internalization and degradation (By similarity).
CC {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
CC of bound ligand. Ligand binding leads to dimerization and activation by
CC sequential autophosphorylation on tyrosine residues (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Homodimer after ligand binding (By similarity).
CC Interacts with cnpy1. {ECO:0000250, ECO:0000269|PubMed:16488878}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm,
CC cytosol {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=After
CC ligand binding, both receptor and ligand are rapidly internalized. Can
CC translocate to the nucleus after internalization, or by translocation
CC from the endoplasmic reticulum or Golgi apparatus to the cytosol, and
CC from there to the nucleus (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q90Z00-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q90Z00-2; Sequence=VSP_037677;
CC Name=3;
CC IsoId=Q90Z00-3; Sequence=VSP_037675, VSP_037677;
CC Name=4;
CC IsoId=Q90Z00-4; Sequence=VSP_037674;
CC Name=5;
CC IsoId=Q90Z00-5; Sequence=VSP_037676, VSP_037677;
CC -!- TISSUE SPECIFICITY: Initially expressed in adaxial mesoderm with
CC transcripts distinctly localized to the anterior portion of each half-
CC somite. Hereupon, also strongly expressed in the otic vesicles,
CC branchial arches and the brain, especially at the midbrain-hindbrain
CC boundary (MHB). {ECO:0000269|PubMed:15221377}.
CC -!- DOMAIN: The second and third Ig-like domains directly interact with
CC fibroblast growth factors (FGF) and heparan sulfate proteoglycans.
CC Isoforms lacking the first Ig-like domain have higher affinity for
CC fibroblast growth factors (FGF) and heparan sulfate proteoglycans than
CC isoforms with all three Ig-like domains (By similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated. Binding of FGF family members together with
CC heparan sulfate proteoglycan or heparin promotes receptor dimerization
CC and autophosphorylation on tyrosine residues. Autophosphorylation
CC occurs in trans between the two FGFR molecules present in the dimer and
CC proceeds in a highly ordered manner. Phosphotyrosine residues provide
CC docking sites for interacting proteins and so are crucial for FGFR1
CC function and its regulation (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated. FGFR1 is rapidly ubiquitinated after
CC autophosphorylation, leading to internalization and degradation (By
CC similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan chains
CC undergo further maturation to an Endo H-resistant form in the Golgi
CC apparatus (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fibroblast growth factor receptor subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI62342.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK64494.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAO45658.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAO45659.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAO45660.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF389400; AAK64494.1; ALT_INIT; mRNA.
DR EMBL; AY197498; AAO45658.1; ALT_INIT; mRNA.
DR EMBL; AY197499; AAO45659.1; ALT_INIT; mRNA.
DR EMBL; AY197500; AAO45660.1; ALT_INIT; mRNA.
DR EMBL; AY197501; AAO45661.1; -; mRNA.
DR EMBL; BX247873; CAK04365.2; -; Genomic_DNA.
DR EMBL; CR376860; CAK04365.2; JOINED; Genomic_DNA.
DR EMBL; BX247873; CAM13573.2; -; Genomic_DNA.
DR EMBL; CR376860; CAM13573.2; JOINED; Genomic_DNA.
DR EMBL; BX247873; CAM13574.1; -; Genomic_DNA.
DR EMBL; CR376860; CAM13574.1; JOINED; Genomic_DNA.
DR EMBL; CR376860; CAP19402.1; -; Genomic_DNA.
DR EMBL; BX247873; CAP19402.1; JOINED; Genomic_DNA.
DR EMBL; CR376860; CAP19403.1; -; Genomic_DNA.
DR EMBL; BX247873; CAP19403.1; JOINED; Genomic_DNA.
DR EMBL; CR376860; CAP19404.1; -; Genomic_DNA.
DR EMBL; BX247873; CAP19404.1; JOINED; Genomic_DNA.
DR EMBL; BC162342; AAI62342.1; ALT_INIT; mRNA.
DR EMBL; CU458752; CAM60064.1; -; mRNA.
DR RefSeq; NP_001296328.1; NM_001309399.1. [Q90Z00-2]
DR RefSeq; NP_001296329.1; NM_001309400.1. [Q90Z00-4]
DR RefSeq; NP_694494.2; NM_152962.3. [Q90Z00-1]
DR RefSeq; XP_009302579.1; XM_009304304.2. [Q90Z00-5]
DR AlphaFoldDB; Q90Z00; -.
DR SMR; Q90Z00; -.
DR IntAct; Q90Z00; 2.
DR MINT; Q90Z00; -.
DR STRING; 7955.ENSDARP00000069260; -.
DR PaxDb; Q90Z00; -.
DR Ensembl; ENSDART00000024882; ENSDARP00000013742; ENSDARG00000011027. [Q90Z00-5]
DR Ensembl; ENSDART00000135166; ENSDARP00000115638; ENSDARG00000011027. [Q90Z00-4]
DR Ensembl; ENSDART00000147742; ENSDARP00000116533; ENSDARG00000011027. [Q90Z00-2]
DR Ensembl; ENSDART00000167394; ENSDARP00000131679; ENSDARG00000011027. [Q90Z00-4]
DR GeneID; 30705; -.
DR KEGG; dre:30705; -.
DR CTD; 30705; -.
DR ZFIN; ZDB-GENE-980526-255; fgfr1a.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000155860; -.
DR HOGENOM; CLU_000288_74_3_1; -.
DR InParanoid; Q90Z00; -.
DR OMA; SIGNSHH; -.
DR PhylomeDB; Q90Z00; -.
DR TreeFam; TF316307; -.
DR Reactome; R-DRE-109704; PI3K Cascade.
DR Reactome; R-DRE-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DRE-190370; FGFR1b ligand binding and activation.
DR Reactome; R-DRE-190373; FGFR1c ligand binding and activation.
DR Reactome; R-DRE-190374; FGFR1c and Klotho ligand binding and activation.
DR Reactome; R-DRE-5654219; Phospholipase C-mediated cascade: FGFR1.
DR Reactome; R-DRE-5654687; Downstream signaling of activated FGFR1.
DR Reactome; R-DRE-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-DRE-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-DRE-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-DRE-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-DRE-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DRE-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR SignaLink; Q90Z00; -.
DR PRO; PR:Q90Z00; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000011027; Expressed in tail bud paraxial mesoderm and 108 other tissues.
DR ExpressionAtlas; Q90Z00; baseline and differential.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:ZFIN.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISS:UniProtKB.
DR GO; GO:0005007; F:fibroblast growth factor receptor activity; IDA:ZFIN.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0060249; P:anatomical structure homeostasis; IMP:ZFIN.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:ZFIN.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:ZFIN.
DR GO; GO:0031101; P:fin regeneration; IMP:ZFIN.
DR GO; GO:0001889; P:liver development; IMP:ZFIN.
DR GO; GO:0042664; P:negative regulation of endodermal cell fate specification; IGI:ZFIN.
DR GO; GO:0021628; P:olfactory nerve formation; IMP:ZFIN.
DR GO; GO:0071699; P:olfactory placode morphogenesis; IMP:ZFIN.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IGI:ZFIN.
DR GO; GO:0048916; P:posterior lateral line development; IMP:ZFIN.
DR GO; GO:0045471; P:response to ethanol; IDA:ZFIN.
DR GO; GO:0043589; P:skin morphogenesis; IMP:ZFIN.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd05098; PTKc_FGFR1; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR028174; FGF_rcpt_1.
DR InterPro; IPR016248; FGF_rcpt_fam.
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; 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 Pfam; PF07679; I-set; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000628; FGFR; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasm;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..810
FT /note="Fibroblast growth factor receptor 1-A"
FT /id="PRO_0000249202"
FT TOPO_DOM 27..363
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..810
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..115
FT /note="Ig-like C2-type 1"
FT DOMAIN 147..235
FT /note="Ig-like C2-type 2"
FT DOMAIN 244..346
FT /note="Ig-like C2-type 3"
FT DOMAIN 465..754
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 787..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 610
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 471..477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 549..551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 450
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 570
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 572
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 640
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 641
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 717
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 753
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
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 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 167..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 266..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 302..415
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15221377"
FT /id="VSP_037674"
FT VAR_SEQ 302..349
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15221377"
FT /id="VSP_037675"
FT VAR_SEQ 302..349
FT /note="TAGVNTTDKEMEVLQIRNVSLEDAGEYTCLAGNSIGHSHHSAWLTVYK ->
FT NSGVNSSDTQVLTLYNVTEEQSGEYICKVSNYIGQANQSAWLTVVKHLQ (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15221377"
FT /id="VSP_037676"
FT VAR_SEQ 414..415
FT /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15221377"
FT /id="VSP_037677"
FT CONFLICT 92
FT /note="T -> A (in Ref. 1; AAK64494/AAO45658/AAO45659/
FT AAO45660, 3; AAI62342 and 4; CAM60064)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="V -> I (in Ref. 4; CAM60064)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 810 AA; 91041 MW; 20D0C8B8022893CD CRC64;
MKMMMIMKTT LLLISVLLTQ ALQSQGRPAI QDEAPAEPTS YTLDSGEKLE LSCKAKEDTQ
KVTWTKDLVP LVDGEHTRLR NDQMEIEKVE PTDSGLYACF AQGLNSNHTE YFNISVTDEE
DEVDSSSEEA KLSNDQNLPM APVWAQPDKM EKKLHAVPAS KTVKFRCQAN GNPTPTLKWL
KNGKEFKRDQ RIGGFKVREH MWTIIMESVV PSDRGNYTCL VENRHGSINH TYQLDVVERS
PHRPILQAGL PANRTAVVGS DVEFECKVFS DPQPHIQWLK HIEVNGSRYG PDGLPYVRAL
KTAGVNTTDK EMEVLQIRNV SLEDAGEYTC LAGNSIGHSH HSAWLTVYKA VPPTQLPNQT
YLEVLIYCVG FFLICVMVGT AVLAKMHSSA KKSDFNSQLA VHKLAKSIPL RRQVTVSVDS
SSSMHSGGML VRPSRLSSSG SPMLSGVSEY ELPQDPRWEV QRDRLVLGKP LGEGCFGQVM
MAEAMGMDKE KPNRITKVAV KMLKSDATEK DLSDLISEME MMKIIGKHKN IINLLGACTQ
DGPLYVIVEF AAKGNLREYL RVRRPPGMEY CYNPDQVPVE NMSIKDLVSC AYQVARGMEY
LASKKCIHRD LAARNVLVTE DNVMKIADFG LARDIHHIDY YKKTTNGRLP VKWMAPEALF
DRIYTHQSDV WSFGVLLWEI FTLGGSPYPG VPVEELFKLL KEGHRMDRPS TCTHELYMMM
RDCWHAVPSQ RPTFKQLVED LDRTLSMTSN QEYLDLSVSL DQFSPNFPDT RSSTCSSGED
SVFSHDAGAD EPCLPKFPPH PNRGVAFKKR
