VGFR2_DANRE
ID VGFR2_DANRE Reviewed; 1357 AA.
AC Q5GIT4; B3DJQ0; Q1ANK7; Q5MD88; Q5RIP2; Q5TZ34;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Vascular endothelial growth factor receptor 2 {ECO:0000250|UniProtKB:P35968};
DE Short=VEGFR-2;
DE EC=2.7.10.1 {ECO:0000250|UniProtKB:P35968};
DE AltName: Full=Fetal liver kinase 1b;
DE Short=FLK-1b;
DE AltName: Full=Kinase insert domain receptor;
DE AltName: Full=Kinase insert domain receptor-B;
DE AltName: Full=Protein-tyrosine kinase receptor flk-1b;
DE AltName: Full=Vascular endothelial growth factor receptor 2 homolog B;
DE Short=VEGFR-2 homolog B;
DE Flags: Precursor;
GN Name=kdr {ECO:0000250|UniProtKB:P35968}; Synonyms=flk1b, kdrb;
GN ORFNames=si:busm1-205d10.1, si:ch211-254j6.1;
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].
RA Habeck H., Langhoff J., Vogel A.M., Trowe T., Koblizek T.I.,
RA Schulte-Merker S.;
RT "Synergistic signaling of vegf receptors is required for vasculogenesis in
RT zebrafish.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH VEGFAA AND VEGFAB,
RP TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=17698971; DOI=10.1182/blood-2006-04-016378;
RA Bahary N., Goishi K., Stuckenholz C., Weber G., Leblanc J., Schafer C.A.,
RA Berman S.S., Klagsbrun M., Zon L.I.;
RT "Duplicate VegfA genes and orthologues of the KDR receptor tyrosine kinase
RT family mediate vascular development in the zebrafish.";
RL Blood 110:3627-3636(2007).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 687-1144, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16617120; DOI=10.1073/pnas.0506886103;
RA Covassin L.D., Villefranc J.A., Kacergis M.C., Weinstein B.M., Lawson N.D.;
RT "Distinct genetic interactions between multiple Vegf receptors are required
RT for development of different blood vessel types in zebrafish.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6554-6559(2006).
RN [6]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND ORTHOLOGY.
RX PubMed=17722983; DOI=10.1371/journal.pgen.0030140;
RA Bussmann J., Bakkers J., Schulte-Merker S.;
RT "Early endocardial morphogenesis requires Scl/Tal1.";
RL PLoS Genet. 3:1425-1437(2007).
RN [7]
RP NOMENCLATURE AND ORTHOLOGY.
RX PubMed=18516225; DOI=10.1371/journal.pgen.1000064;
RA Bussmann J., Lawson N., Zon L., Schulte-Merker S.;
RT "Zebrafish VEGF receptors: a guideline to nomenclature.";
RL PLoS Genet. 4:E1000064-E1000064(2008).
CC -!- FUNCTION: Receptor for VEGF or VEGFC. Has a tyrosine-protein kinase
CC activity. Combinations of multiple VEGF receptors are required for
CC development of different blood vessel types in the embryo. Involved in
CC angiogenesis, specifically in VEGF-induced sprouting of new blood
CC vessels. Particularly involved in artery formation. Does not appear to
CC be required for hematopoiesis. {ECO:0000269|PubMed:16617120,
CC ECO:0000269|PubMed:17698971}.
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: Interacts with isoform VEGF165 of vegfaa and, to a lesser
CC extent, with isoform VEGF171 of vegfab (PubMed:17698971). Interacts
CC (via juxtamembrane region) with chaperone pdcl3 (via thioredoxin fold
CC region); the interaction leads to increased vegfr2 abundance through
CC inhibition of its ubiquitination and degradation (By similarity).
CC {ECO:0000250|UniProtKB:P35968, ECO:0000269|PubMed:17698971}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Early endosome
CC {ECO:0000250}. Cell junction {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P35968}.
CC -!- TISSUE SPECIFICITY: First expressed in embryos between 5- and 7-somites
CC in the bilateral stripes that contain the developing angioblasts, and
CC then localized to the intermediate cell mass (ICM) and the developing
CC vasculature. By 30 hpf, expressed in the major trunk, head and
CC intersomitic vessels, persisting through 4 dpf when expression is seen
CC in developing subintestinal veins and in the remaining vasculature.
CC {ECO:0000269|PubMed:16617120, ECO:0000269|PubMed:17698971,
CC ECO:0000269|PubMed:17722983}.
CC -!- DEVELOPMENTAL STAGE: The first vegfr expressed during development.
CC {ECO:0000269|PubMed:17722983}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- CAUTION: This entry should not be confused with kdrl (AC Q8AXB3), which
CC used to be called kdr. {ECO:0000305}.
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DR EMBL; AY523999; AAS92270.1; -; mRNA.
DR EMBL; DQ026829; AAY89336.1; -; mRNA.
DR EMBL; BX088688; CAM14201.1; -; Genomic_DNA.
DR EMBL; BX511058; CAM14201.1; JOINED; Genomic_DNA.
DR EMBL; BX248242; CAI11526.1; -; Genomic_DNA.
DR EMBL; BX511058; CAH68950.2; -; Genomic_DNA.
DR EMBL; BX088688; CAH68950.2; JOINED; Genomic_DNA.
DR EMBL; BC163563; AAI63563.1; -; mRNA.
DR EMBL; AY833405; AAV93319.1; -; mRNA.
DR RefSeq; NP_001019824.2; NM_001024653.2.
DR AlphaFoldDB; Q5GIT4; -.
DR SMR; Q5GIT4; -.
DR STRING; 7955.ENSDARP00000049203; -.
DR BindingDB; Q5GIT4; -.
DR ChEMBL; CHEMBL2331049; -.
DR DrugCentral; Q5GIT4; -.
DR PaxDb; Q5GIT4; -.
DR PRIDE; Q5GIT4; -.
DR Ensembl; ENSDART00000049204; ENSDARP00000049203; ENSDARG00000017321.
DR GeneID; 554230; -.
DR KEGG; dre:554230; -.
DR CTD; 3791; -.
DR ZFIN; ZDB-GENE-041001-112; kdr.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000156710; -.
DR HOGENOM; CLU_000288_49_4_1; -.
DR InParanoid; Q5GIT4; -.
DR OMA; RIFWDSK; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; Q5GIT4; -.
DR TreeFam; TF325768; -.
DR Reactome; R-DRE-194306; Neurophilin interactions with VEGF and VEGFR.
DR Reactome; R-DRE-195399; VEGF binds to VEGFR leading to receptor dimerization.
DR Reactome; R-DRE-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-DRE-5218921; VEGFR2 mediated cell proliferation.
DR PRO; PR:Q5GIT4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000017321; Expressed in heart and 37 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IMP:ZFIN.
DR GO; GO:0001568; P:blood vessel development; IGI:ZFIN.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0045446; P:endothelial cell differentiation; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
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; ISS:UniProtKB.
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 Pfam; PF07679; I-set; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF17988; VEGFR-2_TMD; 1.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 4.
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 junction; Cell membrane; Cytoplasm;
KW Cytoplasmic vesicle; Developmental protein; Differentiation;
KW Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein;
KW Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1357
FT /note="Vascular endothelial growth factor receptor 2"
FT /id="PRO_0000249465"
FT TOPO_DOM 23..774
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 775..795
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 796..1357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..120
FT /note="Ig-like C2-type 1"
FT DOMAIN 120..222
FT /note="Ig-like C2-type 2"
FT DOMAIN 216..330
FT /note="Ig-like C2-type 3"
FT DOMAIN 335..426
FT /note="Ig-like C2-type 4"
FT DOMAIN 433..553
FT /note="Ig-like C2-type 5"
FT DOMAIN 556..667
FT /note="Ig-like C2-type 6"
FT DOMAIN 676..762
FT /note="Ig-like C2-type 7"
FT DOMAIN 843..1173
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 944..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..971
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1039
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 849..857
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 877
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1065
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 1070
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 1186
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 1222
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
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 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 153..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 248..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 457..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 579..651
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 697..746
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 17
FT /note="F -> V (in Ref. 3; AAI63563)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="T -> S (in Ref. 3; AAI63563)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="L -> P (in Ref. 2; AAY89336)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="L -> R (in Ref. 2; AAY89336)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="W -> C (in Ref. 3; AAI63563)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="K -> R (in Ref. 1; AAS92270)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="E -> G (in Ref. 2; AAY89336)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="A -> G (in Ref. 2; AAY89336)"
FT /evidence="ECO:0000305"
FT CONFLICT 488..489
FT /note="TR -> PS (in Ref. 2; AAY89336 and 3; AAI63563)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="F -> S (in Ref. 1; AAS92270)"
FT /evidence="ECO:0000305"
FT CONFLICT 958
FT /note="R -> K (in Ref. 1; AAS92270)"
FT /evidence="ECO:0000305"
FT CONFLICT 996
FT /note="Y -> S (in Ref. 2; AAY89336, 3; AAI63563 and 5;
FT AAV93319)"
FT /evidence="ECO:0000305"
FT CONFLICT 997
FT /note="K -> T (in Ref. 2; AAY89336 and 3; AAI63563)"
FT /evidence="ECO:0000305"
FT CONFLICT 1100
FT /note="W -> R (in Ref. 1; AAS92270)"
FT /evidence="ECO:0000305"
FT CONFLICT 1223
FT /note="D -> G (in Ref. 2; AAY89336)"
FT /evidence="ECO:0000305"
FT CONFLICT 1234
FT /note="M -> I (in Ref. 2; AAY89336 and 3; AAI63563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1357 AA; 153042 MW; 43B97B484DBEA38F CRC64;
MAKTSYALLL LDILLTFNVA KAIELRFVPD PPTLNITEKT IKINASDTLQ ITCRGRQILE
WSTPHNRTSS ETRLTISDCS GDGLFCSTLT LSKAVANETG EYRCFYKSLP KEDGKTSVAV
YVFIQDYRTP FVRIAQDYDV VFIREGEQVV IPCLVSVEDL NVTLYTKYPV KELSTDGKEV
IWDSRRGFIL PSRVVSYAGV VYCQTTIRNE TFQSSPYIVA VVGYKIYDLT LSPQHERLTV
GERLILNCTA HTELNVGIDF QWTFPHEKRS VNGSMSTSRY KTSSNKKKLW NSLELSNTLT
VENVTLNDTG EYICTASSGQ MQKIAQASLI VYEKPFIALS DQLWQTVEAK AGDAEAKILV
KYYAYPEPAV RWYKNDQLIV LRDEYRMKFY RGVHLTIYGV TEKDAGNYTV VMTNKITKEE
QRRTFQLVVN DLPRIFEKDV SLDRDVHMYG SSPTLTCTAS GGSSPVTIKW QWMPREDCPV
RFLPKSDTRM AKCDKWREMS NNTGKNPLIS QTSVDERTLK TISTLKIQKA VDHALYRCIA
TNKMGQDQRV IVFQVTRFLN LSVLPSSSPI EGQDVIMRCV ADRLLYYNLR WYRVANVANH
DPPPAAVPCD TLTLSHLHQP NVTVSGLQGT NVTLDMPIPN ATMMDQGLYA CQVEIVGTNE
KTCLLHNLRL RALEMSRIVT NLTDQRVNVS DSTTLVCEVS GTPTPTIVWT KDNQTVMEGS
GVILKRSNRV LTIQRVKKED SGLYICTACN QQGCESSEAR ISVDGAEEKM NVELIMPIGA
VVIAMFLWLL IVFVIRNRKR PNDGDLKTGY LSIILDSDDM PMDEHCERLT YDASKWEFPR
DRLKLGEPLG RGAFGQVVEA TAYGIEKATT CTTVAVKMLK EGATSSEYRA LMSELKILIH
IGHHLNVVNL LGACTKQGGP LMVIVEYCKH GNLSSYLKSK RGEYSPYKKR TPRMPNRREV
QQDEDPREGD LGLGTSTRLD ICTGTAVCTR TGEQTYKTLQ DEQESSDWDH LTMEDLISYS
FQVAKGMEFL ASRKCIHRDL AARNILLSEN SVVKICDFGL ARDVYKDPDY VRKGDARLPL
KWMAPETIFD RVYTTQSDVW SFGVLLWEIF SLGASPYPGV CIDESFCRRL KEGTRMRAPD
YATPEIYQTM LDCWLDRPLD RPTFTQLVEH LGNLLQASAQ QDGKDYIPLT NGEMEEELVA
PHLNVTSKRS FYAGNTEAQL HYDNAPPLGF PQQMNSSGVP VNMTGFVDIP LEHTTVMDGH
VDCGVGLSRE QMKALDRQAQ RPLNFSPLLR CKSKESLASE SSNQTSGYQS GYHSDDAEAP
IYANEEMILK RDIRKKPPLP KRNDKFSAEV RYSAPPV
