VGFR1_MOUSE
ID VGFR1_MOUSE Reviewed; 1333 AA.
AC P35969; O55094; Q61517;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Vascular endothelial growth factor receptor 1;
DE Short=VEGFR-1;
DE EC=2.7.10.1;
DE AltName: Full=Embryonic receptor kinase 2;
DE AltName: Full=Fms-like tyrosine kinase 1;
DE Short=FLT-1;
DE AltName: Full=Tyrosine-protein kinase receptor FLT;
DE Flags: Precursor;
GN Name=Flt1; Synonyms=Emrk2, Flt, Vegfr1;
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].
RC STRAIN=BALB/cJ; TISSUE=Neonatal brain, and Placenta;
RX PubMed=8393164;
RA Finnerty H., Kelleher K., Morris G.E., Bean K., Merberg D.M., Kriz R.,
RA Morris J.C., Sookdeo H., Turner K.J., Wood C.R.;
RT "Molecular cloning of murine FLT and FLT4.";
RL Oncogene 8:2293-2298(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8134130;
RA Choi K., Wall C., Hanratty R., Keller G.;
RT "Isolation of a gene encoding a novel receptor tyrosine kinase from
RT differentiated embryonic stem cells.";
RL Oncogene 9:1261-1266(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=9524283; DOI=10.1016/s0378-1119(98)00006-7;
RA Kondo K., Hiratsuka S., Subbalakshmi E., Matsushime H., Shibuya M.;
RT "Genomic organization of the flt-1 gene encoding for vascular endothelial
RT growth factor (VEGF) receptor-1 suggests an intimate evolutionary
RT relationship between the 7-Ig and the 5-Ig tyrosine kinase receptors.";
RL Gene 208:297-305(1998).
RN [4]
RP PROTEIN SEQUENCE OF 110-119 AND 185-191, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN BLOOD VESSEL DEVELOPMENT DURING
RP EMBRYOGENESIS.
RX PubMed=7596436; DOI=10.1038/376066a0;
RA Fong G.H., Rossant J., Gertsenstein M., Breitman M.L.;
RT "Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of
RT vascular endothelium.";
RL Nature 376:66-70(1995).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN MACROPHAGE MIGRATION.
RX PubMed=9689083; DOI=10.1073/pnas.95.16.9349;
RA Hiratsuka S., Minowa O., Kuno J., Noda T., Shibuya M.;
RT "Flt-1 lacking the tyrosine kinase domain is sufficient for normal
RT development and angiogenesis in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9349-9354(1998).
RN [7]
RP FUNCTION IN ANGIOGENESIS.
RX PubMed=11221852;
RA Hiratsuka S., Maru Y., Okada A., Seiki M., Noda T., Shibuya M.;
RT "Involvement of Flt-1 tyrosine kinase (vascular endothelial growth factor
RT receptor-1) in pathological angiogenesis.";
RL Cancer Res. 61:1207-1213(2001).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=14982871; DOI=10.1182/blood-2003-07-2315;
RA Kearney J.B., Kappas N.C., Ellerstrom C., DiPaola F.W., Bautch V.L.;
RT "The VEGF receptor flt-1 (VEGFR-1) is a positive modulator of vascular
RT sprout formation and branching morphogenesis.";
RL Blood 103:4527-4535(2004).
RN [9]
RP FUNCTION IN ANGIOGENESIS.
RX PubMed=18583712; DOI=10.1161/circresaha.108.174128;
RA Nishi J., Minamino T., Miyauchi H., Nojima A., Tateno K., Okada S.,
RA Orimo M., Moriya J., Fong G.H., Sunagawa K., Shibuya M., Komuro I.;
RT "Vascular endothelial growth factor receptor-1 regulates postnatal
RT angiogenesis through inhibition of the excessive activation of Akt.";
RL Circ. Res. 103:261-268(2008).
RN [10]
RP FUNCTION.
RX PubMed=20924106; DOI=10.1158/0008-5472.can-10-0202;
RA Muramatsu M., Yamamoto S., Osawa T., Shibuya M.;
RT "Vascular endothelial growth factor receptor-1 signaling promotes
RT mobilization of macrophage lineage cells from bone marrow and stimulates
RT solid tumor growth.";
RL Cancer Res. 70:8211-8221(2010).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30936473; DOI=10.1038/s41556-019-0301-x;
RA Nguyen M.T., Vemaraju S., Nayak G., Odaka Y., Buhr E.D., Alonzo N.,
RA Tran U., Batie M., Upton B.A., Darvas M., Kozmik Z., Rao S., Hegde R.S.,
RA Iuvone P.M., Van Gelder R.N., Lang R.A.;
RT "An opsin 5-dopamine pathway mediates light-dependent vascular development
RT in the eye.";
RL Nat. Cell Biol. 21:420-429(2019).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor
CC for VEGFA, VEGFB and PGF, and plays an essential role in the
CC development of embryonic vasculature, the regulation of angiogenesis,
CC cell survival, cell migration, macrophage function, chemotaxis, and
CC cancer cell invasion. Acts as a positive regulator of postnatal retinal
CC hyaloid vessel regression (PubMed:30936473). May play an essential role
CC as a negative regulator of embryonic angiogenesis by inhibiting
CC excessive proliferation of endothelial cells. Can promote endothelial
CC cell proliferation, survival and angiogenesis in adulthood. Its
CC function in promoting cell proliferation seems to be cell-type
CC specific. Promotes PGF-mediated proliferation of endothelial cells, and
CC proliferation of some types of cancer cells, but does not promote
CC proliferation of normal fibroblasts. Has very high affinity for VEGFA
CC and relatively low protein kinase activity; may function as a negative
CC regulator of VEGFA signaling by limiting the amount of free VEGFA and
CC preventing its binding to KDR. Modulates KDR signaling by forming
CC heterodimers with KDR. Ligand binding leads to the activation of
CC several signaling cascades. Activation of PLCG leads to the production
CC of the cellular signaling molecules diacylglycerol and inositol 1,4,5-
CC trisphosphate and the activation of protein kinase C. Mediates
CC phosphorylation of PIK3R1, the regulatory subunit of
CC phosphatidylinositol 3-kinase, leading to the activation of
CC phosphatidylinositol kinase and the downstream signaling pathway.
CC Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase
CC signaling pathway, as well as of the AKT1 signaling pathway.
CC Phosphorylates SRC, YES1 and PLCG, and may also phosphorylate CBL.
CC Promotes phosphorylation of AKT1 and PTK2/FAK1 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P17948,
CC ECO:0000269|PubMed:11221852, ECO:0000269|PubMed:14982871,
CC ECO:0000269|PubMed:18583712, ECO:0000269|PubMed:20924106,
CC ECO:0000269|PubMed:30936473, ECO:0000269|PubMed:7596436,
CC ECO:0000269|PubMed:9689083}.
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. Binding of VEGFA, VEGFB or PGF leads to dimerization
CC and activation by autophosphorylation on tyrosine residues (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with VEGFA, VEGFB and PGF. Monomer in the absence of
CC bound VEGFA, VEGFB or PGF. Homodimer in the presence of bound VEGFA,
CC VEGFB and PGF. Can also form a heterodimer with KDR. Interacts
CC (tyrosine phosphorylated) with CBL, CRK, GRB2, NCK1, PIK3R1, PLCG,
CC PSEN1 and PTPN11. Probably interacts with PTPRB. Interacts with RACK1.
CC Identified in a complex with CBL and CD2AP (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Endosome {ECO:0000250}. Note=Autophosphorylation promotes
CC ubiquitination and endocytosis. {ECO:0000250}.
CC -!- DOMAIN: The second and third Ig-like C2-type (immunoglobulin-like)
CC domains are sufficient for VEGFA binding. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Ubiquitinated after VEGFA-mediated autophosphorylation, leading to
CC proteolytic degradation. {ECO:0000250}.
CC -!- PTM: Autophosphorylated on tyrosine residues upon ligand binding.
CC Autophosphorylation occurs in trans, i.e. one subunit of the dimeric
CC receptor phosphorylates tyrosine residues on the other subunit.
CC Phosphorylation at Tyr-1169 is important for interaction with PLCG.
CC Phosphorylation at Tyr-1213 is important for interaction with PIK3R1,
CC PTPN11, GRB2, and PLCG. Phosphorylation at Tyr-1328 is important for
CC endocytosis and for interaction with CBL, NCK1 and CRK. Is probably
CC dephosphorylated by PTPRB (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality at about 9 dpc, due to
CC defects in the formation and organization of the vascular network
CC (PubMed:7596436, PubMed:9689083). Mice display abnormal blood island
CC structures in the yolk sac, leading to defects in the organization of
CC the vascular endothelium, excess growth and disorganization of
CC embryonic and extraembryonic vasculature, including the endocardium and
CC the microvasculature (PubMed:7596436). Reduced vascular sprout
CC formation and migration (PubMed:14982871). Loss of retinal hyaloid
CC vessel regression from postnatal day 3 (P3) to P8 (PubMed:30936473).
CC Mice expressing a mutant protein that lacks the kinase domain survive
CC and have no apparent phenotype (PubMed:9689083).
CC {ECO:0000269|PubMed:14982871, ECO:0000269|PubMed:30936473,
CC ECO:0000269|PubMed:7596436, ECO:0000269|PubMed:9689083}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; L07297; AAA40078.1; -; mRNA.
DR EMBL; X78568; CAA55311.1; -; mRNA.
DR EMBL; D88689; BAA24498.1; -; mRNA.
DR CCDS; CCDS19879.1; -.
DR PIR; I78875; I78875.
DR PIR; S49010; S49010.
DR RefSeq; NP_034358.2; NM_010228.3.
DR AlphaFoldDB; P35969; -.
DR SMR; P35969; -.
DR BioGRID; 199706; 16.
DR CORUM; P35969; -.
DR DIP; DIP-39359N; -.
DR IntAct; P35969; 8.
DR MINT; P35969; -.
DR STRING; 10090.ENSMUSP00000031653; -.
DR BindingDB; P35969; -.
DR ChEMBL; CHEMBL3516; -.
DR GlyGen; P35969; 12 sites.
DR iPTMnet; P35969; -.
DR PhosphoSitePlus; P35969; -.
DR MaxQB; P35969; -.
DR PaxDb; P35969; -.
DR PeptideAtlas; P35969; -.
DR PRIDE; P35969; -.
DR ProteomicsDB; 297594; -.
DR ABCD; P35969; 2 sequenced antibodies.
DR DNASU; 14254; -.
DR GeneID; 14254; -.
DR KEGG; mmu:14254; -.
DR UCSC; uc009aoh.1; mouse.
DR CTD; 2321; -.
DR MGI; MGI:95558; Flt1.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; P35969; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; P35969; -.
DR TreeFam; TF325768; -.
DR BRENDA; 2.7.10.1; 3474.
DR Reactome; R-MMU-194306; Neurophilin interactions with VEGF and VEGFR.
DR Reactome; R-MMU-195399; VEGF binds to VEGFR leading to receptor dimerization.
DR BioGRID-ORCS; 14254; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Flt1; mouse.
DR PRO; PR:P35969; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P35969; protein.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0019838; F:growth factor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0036332; F:placental growth factor receptor activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IDA:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:UniProtKB.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:MGI.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
DR GO; GO:1990384; P:hyaloid vascular plexus regression; IMP:UniProtKB.
DR GO; GO:0030522; P:intracellular receptor signaling pathway; ISO:MGI.
DR GO; GO:0002548; P:monocyte chemotaxis; ISO:MGI.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISO:MGI.
DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; ISO:MGI.
DR GO; GO:1904046; P:negative regulation of vascular endothelial growth factor production; ISO:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI.
DR GO; GO:1901534; P:positive regulation of hematopoietic progenitor cell differentiation; IMP: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:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISO:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0048597; P:post-embryonic camera-type eye morphogenesis; IGI:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0036323; P:vascular endothelial growth factor receptor-1 signaling pathway; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 7.
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 InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR InterPro; IPR041348; VEGFR-2_TMD.
DR InterPro; IPR009135; VEGFR1_rcpt.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF17988; VEGFR-2_TMD; 1.
DR PRINTS; PR01833; VEGFRECEPTR1.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 6.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 7.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 5.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; ATP-binding; Cell membrane; Chemotaxis;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Disulfide bond; Endosome; Glycoprotein; Immunoglobulin domain; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1333
FT /note="Vascular endothelial growth factor receptor 1"
FT /id="PRO_0000016769"
FT TOPO_DOM 23..759
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..781
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 782..1333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..124
FT /note="Ig-like C2-type 1"
FT DOMAIN 152..215
FT /note="Ig-like C2-type 2"
FT DOMAIN 231..328
FT /note="Ig-like C2-type 3"
FT DOMAIN 334..429
FT /note="Ig-like C2-type 4"
FT DOMAIN 430..550
FT /note="Ig-like C2-type 5"
FT DOMAIN 557..656
FT /note="Ig-like C2-type 6"
FT DOMAIN 662..748
FT /note="Ig-like C2-type 7"
FT DOMAIN 828..1158
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 947..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1022
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 834..842
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 862
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 768..769
FT /note="Cleavage; by PSEN1"
FT /evidence="ECO:0000250"
FT MOD_RES 915
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P17948"
FT MOD_RES 1053
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 1169
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P17948"
FT MOD_RES 1213
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P17948"
FT MOD_RES 1242
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P17948"
FT MOD_RES 1322
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P17948"
FT MOD_RES 1328
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P17948"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
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 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 159..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 253..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 455..536
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 578..637
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 683..732
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 158
FT /note="Missing (in Ref. 2; CAA55311)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="Missing (in Ref. 2; CAA55311)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="H -> L (in Ref. 2; CAA55311)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="H -> N (in Ref. 2; CAA55311)"
FT /evidence="ECO:0000305"
FT CONFLICT 609..615
FT /note="KMATTQD -> NGHHSS (in Ref. 2; CAA55311)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="F -> L (in Ref. 2; CAA55311)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="A -> S (in Ref. 2; CAA55311)"
FT /evidence="ECO:0000305"
FT CONFLICT 765
FT /note="C -> Y (in Ref. 2; CAA55311)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="K -> N (in Ref. 2; CAA55311)"
FT /evidence="ECO:0000305"
FT CONFLICT 1009
FT /note="G -> R (in Ref. 2; CAA55311)"
FT /evidence="ECO:0000305"
FT CONFLICT 1181
FT /note="S -> G (in Ref. 3; BAA24498)"
FT /evidence="ECO:0000305"
FT CONFLICT 1181
FT /note="S -> N (in Ref. 2; CAA55311)"
FT /evidence="ECO:0000305"
FT CONFLICT 1193..1194
FT /note="LF -> RG (in Ref. 2; CAA55311)"
FT /evidence="ECO:0000305"
FT CONFLICT 1278..1279
FT /note="KS -> PR (in Ref. 2; CAA55311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1333 AA; 149876 MW; C06533B7ECBC404C CRC64;
MVSCWDTAVL PYALLGCLLL TGYGSGSKLK VPELSLKGTQ HVMQAGQTLF LKCRGEAAHS
WSLPTTVSQE DKRLSITPPS ACGRDNRQFC STLTLDTAQA NHTGLYTCRY LPTSTSKKKK
AESSIYIFVS DAGSPFIEMH TDIPKLVHMT EGRQLIIPCR VTSPNVTVTL KKFPFDTLTP
DGQRITWDSR RGFIIANATY KEIGLLNCEA TVNGHLYQTN YLTHRQTNTI LDVQIRPPSP
VRLLHGQTLV LNCTATTELN TRVQMSWNYP GKATKRASIR QRIDRSHSHN NVFHSVLKIN
NVESRDKGLY TCRVKSGSSF QSFNTSVHVY EKGFISVKHR KQPVQETTAG RRSYRLSMKV
KAFPSPEIVW LKDGSPATLK SARYLVHGYS LIIKDVTTED AGDYTILLGI KQSRLFKNLT
ATLIVNVKPQ IYEKSVSSLP SPPLYPLGSR QVLTCTVYGI PRPTITWLWH PCHHNHSKER
YDFCTENEES FILDPSSNLG NRIESISQRM TVIEGTNKTV STLVVADSQT PGIYSCRAFN
KIGTVERNIK FYVTDVPNGF HVSLEKMPAE GEDLKLSCVV NKFLYRDITW ILLRTVNNRT
MHHSISKQKM ATTQDYSITL NLVIKNVSLE DSGTYACRAR NIYTGEDILR KTEVLVRDSE
APHLLQNLSD YEVSISGSTT LDCQARGVPA PQITWFKNNH KIQQEPGIIL GPGNSTLFIE
RVTEEDEGVY RCRATNQKGA VESAAYLTVQ GTSDKSNLEL ITLTCTCVAA TLFWLLLTLF
IRKLKRSSSE VKTDYLSIIM DPDEVPLDEQ CERLPYDASK WEFARERLKL GKSLGRGAFG
KVVQASAFGI KKSPTCRTVA VKMLKEGATA SEYKALMTEL KILTHIGHHL NVVNLLGACT
KQGGPLMVIV EYCKYGNLSN YLKSKRDLFC LNKDAALHME LKKESLEPGL EQGQKPRLDS
VSSSSVTSSS FPEDRSVSDV EGDEDYSEIS KQPLTMEDLI SYSFQVARGM EFLSSRKCIH
RDLAARNILL SENNVVKICD FGLARDIYKN PDYVRRGDTR LPLKWMAPES IFDKVYSTKS
DVWSYGVLLW EIFSLGGSPY PGVQMDEDFC SRLKEGMRMR TPEYATPEIY QIMLDCWHKD
PKERPRFAEL VEKLGDLLQA NVQQDGKDYI PLNAILTRNS SFTYSTPTFS EDLFKDGFAD
PHFHSGSSDD VRYVNAFKFM SLERIKTFEE LSPNSTSMFE DYQLDTSTLL GSPLLKRFTW
TETKPKASMK IDLRIASKSK EAGLSDLPRP SFCFSSCGHI RPVQDDESEL GKESCCSPPP
DYNSVVLYSS PPA
