VGFR2_MOUSE
ID VGFR2_MOUSE Reviewed; 1345 AA.
AC P35918; C5H7S5; Q8VCD0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Vascular endothelial growth factor receptor 2 {ECO:0000305};
DE Short=VEGFR-2;
DE EC=2.7.10.1 {ECO:0000269|PubMed:12881528};
DE AltName: Full=Fetal liver kinase 1;
DE Short=FLK-1;
DE AltName: Full=Kinase NYK;
DE AltName: Full=Protein-tyrosine kinase receptor flk-1;
DE AltName: CD_antigen=CD309;
DE Flags: Precursor;
GN Name=Kdr {ECO:0000312|MGI:MGI:96683}; Synonyms=Flk-1, Flk1;
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), AND INTERACTION WITH VEGFA.
RC STRAIN=BALB/cJ; TISSUE=Embryo;
RX PubMed=7681362; DOI=10.1016/0092-8674(93)90573-9;
RA Millauer B., Wizigmann-Voos S., Schnurch H., Martinez R., Mueller N.P.H.,
RA Risau W., Ullrich A.;
RT "High affinity VEGF binding and developmental expression suggest Flk-1 as a
RT major regulator of vasculogenesis and angiogenesis.";
RL Cell 72:835-846(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C3H/He; TISSUE=Fetal liver;
RX PubMed=1717995; DOI=10.1073/pnas.88.20.9026;
RA Mathews W., Jordan C.T., Gavin M., Jenkins N.A., Copeland N.G.,
RA Lemishcka I.R.;
RT "A receptor tyrosine kinase cDNA isolated from a population of enriched
RT primitive hematopoietic cells and exhibiting close genetic linkage to c-
RT kit.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9026-9030(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8423988;
RA Oelrichs R.B., Reid H.H., Bernard O., Ziemiecki A., Wilks A.F.;
RT "NYK/FLK-1: a putative receptor protein tyrosine kinase isolated from E10
RT embryonic neuroepithelium is expressed in endothelial cells of the
RT developing embryo.";
RL Oncogene 8:11-18(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH VEGFC, FUNCTION IN
RP INHIBITING VEGFC SIGNALING, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J;
RX PubMed=19668192; DOI=10.1038/nm.2018;
RA Albuquerque R.J., Hayashi T., Cho W.G., Kleinman M.E., Dridi S., Takeda A.,
RA Baffi J.Z., Yamada K., Kaneko H., Green M.G., Chappell J., Wilting J.,
RA Weich H.A., Yamagami S., Amano S., Mizuki N., Alexander J.S.,
RA Peterson M.L., Brekken R.A., Hirashima M., Capoor S., Usui T., Ambati B.K.,
RA Ambati J.;
RT "Alternatively spliced vascular endothelial growth factor receptor-2 is an
RT essential endogenous inhibitor of lymphatic vessel growth.";
RL Nat. Med. 15:1023-1030(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RX PubMed=7559454; DOI=10.1074/jbc.270.39.23111;
RA Patterson C., Perrella M.A., Hsieh C.-M., Yoshizumi M., Lee M.-E.,
RA Harber E.;
RT "Cloning and functional analysis of the promoter for KDR/flk-1, a receptor
RT for vascular endothelial growth factor.";
RL J. Biol. Chem. 270:23111-23118(1995).
RN [8]
RP FUNCTION, INTERACTION WITH VEGFA, AUTOPHOSPHORYLATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8356051; DOI=10.1073/pnas.90.16.7533;
RA Quinn T.P., Peters K.G., de Vries C., Ferrara N., Williams L.T.;
RT "Fetal liver kinase 1 is a receptor for vascular endothelial growth factor
RT and is selectively expressed in vascular endothelium.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7533-7537(1993).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=7596435; DOI=10.1038/376062a0;
RA Shalaby F., Rossant J., Yamaguchi T.P., Gertsenstein M., Wu X.F.,
RA Breitman M.L., Schuh A.C.;
RT "Failure of blood-island formation and vasculogenesis in Flk-1-deficient
RT mice.";
RL Nature 376:62-66(1995).
RN [10]
RP DEVELOPMENTAL STAGE.
RX PubMed=10878616;
RX DOI=10.1002/1097-0177(200007)218:3<507::aid-dvdy1012>3.0.co;2-5;
RA Pepper M.S., Baetens D., Mandriota S.J., Di Sanza C., Oikemus S.,
RA Lane T.F., Soriano J.V., Montesano R., Iruela-Arispe M.L.;
RT "Regulation of VEGF and VEGF receptor expression in the rodent mammary
RT gland during pregnancy, lactation, and involution.";
RL Dev. Dyn. 218:507-524(2000).
RN [11]
RP FUNCTION, PHOSPHORYLATION AT TYR-1212, AND MUTAGENESIS OF TYR-1212.
RX PubMed=12023952; DOI=10.1074/jbc.m110544200;
RA Meyer R.D., Dayanir V., Majnoun F., Rahimi N.;
RT "The presence of a single tyrosine residue at the carboxyl domain of
RT vascular endothelial growth factor receptor-2/FLK-1 regulates its
RT autophosphorylation and activation of signaling molecules.";
RL J. Biol. Chem. 277:27081-27087(2002).
RN [12]
RP INTERACTION WITH FLT4, AND CATALYTIC ACTIVITY.
RX PubMed=12881528; DOI=10.1074/jbc.m304499200;
RA Dixelius J., Makinen T., Wirzenius M., Karkkainen M.J., Wernstedt C.,
RA Alitalo K., Claesson-Welsh L.;
RT "Ligand-induced vascular endothelial growth factor receptor-3 (VEGFR-3)
RT heterodimerization with VEGFR-2 in primary lymphatic endothelial cells
RT regulates tyrosine phosphorylation sites.";
RL J. Biol. Chem. 278:40973-40979(2003).
RN [13]
RP INTERACTION WITH FLT1.
RX PubMed=12796773; DOI=10.1038/nm884;
RA Autiero M., Waltenberger J., Communi D., Kranz A., Moons L., Lambrechts D.,
RA Kroll J., Plaisance S., De Mol M., Bono F., Kliche S., Fellbrich G.,
RA Ballmer-Hofer K., Maglione D., Mayr-Beyrle U., Dewerchin M., Dombrowski S.,
RA Stanimirovic D., Van Hummelen P., Dehio C., Hicklin D.J., Persico G.,
RA Herbert J.M., Communi D., Shibuya M., Collen D., Conway E.M., Carmeliet P.;
RT "Role of PlGF in the intra- and intermolecular cross talk between the VEGF
RT receptors Flt1 and Flk1.";
RL Nat. Med. 9:936-943(2003).
RN [14]
RP INTERACTION WITH SHB, AND MUTAGENESIS OF TYR-1173.
RX PubMed=15026417; DOI=10.1074/jbc.m312729200;
RA Holmqvist K., Cross M.J., Rolny C., Haegerkvist R., Rahimi N.,
RA Matsumoto T., Claesson-Welsh L., Welsh M.;
RT "The adaptor protein shb binds to tyrosine 1175 in vascular endothelial
RT growth factor (VEGF) receptor-2 and regulates VEGF-dependent cellular
RT migration.";
RL J. Biol. Chem. 279:22267-22275(2004).
RN [15]
RP FUNCTION, INTERACTION WITH CBL, UBIQUITINATION, PHOSPHORYLATION AT TYR-1052
RP AND TYR-1057, MUTAGENESIS OF LYS-866; SER-1188 AND SER-1191, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15673613; DOI=10.1091/mbc.e04-08-0749;
RA Singh A.J., Meyer R.D., Band H., Rahimi N.;
RT "The carboxyl terminus of VEGFR-2 is required for PKC-mediated down-
RT regulation.";
RL Mol. Biol. Cell 16:2106-2118(2005).
RN [16]
RP INTERACTION WITH MYOF.
RX PubMed=17702744; DOI=10.1074/jbc.m704798200;
RA Bernatchez P.N., Acevedo L., Fernandez-Hernando C., Murata T., Chalouni C.,
RA Kim J., Erdjument-Bromage H., Shah V., Gratton J.-P., McNally E.M.,
RA Tempst P., Sessa W.C.;
RT "Myoferlin regulates vascular endothelial growth factor receptor-2
RT stability and function.";
RL J. Biol. Chem. 282:30745-30753(2007).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=19635461; DOI=10.1016/j.bbrc.2009.07.108;
RA Kanemura H., Satoh T., Bilasy S.E., Ueda S., Hirashima M., Kataoka T.;
RT "Impaired vascular development in the yolk sac and allantois in mice
RT lacking RA-GEF-1.";
RL Biochem. Biophys. Res. Commun. 387:754-759(2009).
RN [18]
RP FUNCTION.
RX PubMed=19652084; DOI=10.1161/hypertensionaha.109.129973;
RA Facemire C.S., Nixon A.B., Griffiths R., Hurwitz H., Coffman T.M.;
RT "Vascular endothelial growth factor receptor 2 controls blood pressure by
RT regulating nitric oxide synthase expression.";
RL Hypertension 54:652-658(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1229; SER-1233 AND THR-1236,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Lung;
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 [20]
RP FUNCTION.
RX PubMed=20705758; DOI=10.1182/blood-2010-02-267427;
RA Nakao S., Zandi S., Hata Y., Kawahara S., Arita R., Schering A., Sun D.,
RA Melhorn M.I., Ito Y., Lara-Castillo N., Ishibashi T., Hafezi-Moghadam A.;
RT "Blood vessel endothelial VEGFR-2 delays lymphangiogenesis: an endogenous
RT trapping mechanism links lymph- and angiogenesis.";
RL Blood 117:1081-1090(2011).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor
CC for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation
CC of angiogenesis, vascular development, vascular permeability, and
CC embryonic hematopoiesis. Promotes proliferation, survival, migration
CC and differentiation of endothelial cells. Promotes reorganization of
CC the actin cytoskeleton. Isoforms lacking a transmembrane domain, such
CC as isoform 2, may function as decoy receptors for VEGFA, VEGFC and/or
CC VEGFD. Isoform 2 plays an important role as a negative regulator of
CC VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of
CC free VEGFA and/or VEGFC and by preventing their binding to FLT4.
CC Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of
CC vascular growth factors to isoform 1 leads to the activation of several
CC signaling cascades. Activation of PLCG1 leads to the production of the
CC cellular signaling molecules diacylglycerol and inositol 1,4,5-
CC trisphosphate and the activation of protein kinase C. Mediates
CC activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling
CC pathway, as well as of the AKT1 signaling pathway. Mediates
CC phosphorylation of PIK3R1, the regulatory subunit of
CC phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton
CC and activation of PTK2/FAK1. Required for VEGFA-mediated induction of
CC NOS2 and NOS3, leading to the production of the signaling molecule
CC nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes
CC phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC.
CC {ECO:0000269|PubMed:12023952, ECO:0000269|PubMed:15673613,
CC ECO:0000269|PubMed:19635461, ECO:0000269|PubMed:19652084,
CC ECO:0000269|PubMed:19668192, ECO:0000269|PubMed:20705758,
CC ECO:0000269|PubMed:7596435, ECO:0000269|PubMed:8356051}.
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:12881528};
CC -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
CC of bound ligand. Binding of VEGFA, VEGFC or VEGFD leads to dimerization
CC and activation by autophosphorylation on tyrosine residues. May be
CC regulated by hydrogen sulfide (H(2)S) levels via a sensitive
CC intracellular disulfide bond (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer in the presence of bound dimeric VEGFA, VEGFC or
CC VEGFD ligands; monomeric in the absence of bound ligands. Can also form
CC heterodimers with FLT1/VEGFR1 and KDR/VEGFR2. Interacts (tyrosine
CC phosphorylated) with LFYN, NCK1, PLCG1. Interacts (tyrosine-
CC phosphorylated active form preferentially) with DAB2IP (via C2 domain
CC and active form preferentially); the interaction occurs at the late
CC phase of VEGFA response and inhibits KDR/VEGFR2 activity. Interacts
CC with SHBSH2D2A/TSAD, GRB2, MYOF, CBL and PDCD6 (PubMed:12796773,
CC PubMed:12881528, PubMed:15026417, PubMed:15673613, PubMed:17702744,
CC PubMed:19668192, PubMed:7681362, PubMed:8356051). Interacts (via C-
CC terminus domain) with ERN1 (via kinase domain); the interaction is
CC facilitated in a XBP1 isoform 1- and vascular endothelial growth factor
CC (VEGF)-dependent manner in endothelial cells (By similarity). Interacts
CC (via juxtamembrane region) with chaperone PDCL3 (via thioredoxin fold
CC region); the interaction leads to increased KDR/VEGFR2 abundance
CC through inhibition of its ubiquitination and degradation (By
CC similarity). Interacts (tyrosine phosphorylated) with CCDC88A/GIV (via
CC SH2-like region); binding requires autophosphorylation of the
CC KDR/VEGFR2 C-terminal region (By similarity). Interacts with isoform 2
CC of BSG (By similarity). {ECO:0000250|UniProtKB:P35968,
CC ECO:0000269|PubMed:12796773, ECO:0000269|PubMed:12881528,
CC ECO:0000269|PubMed:15026417, ECO:0000269|PubMed:15673613,
CC ECO:0000269|PubMed:17702744, ECO:0000269|PubMed:19668192,
CC ECO:0000269|PubMed:7681362, ECO:0000269|PubMed:8356051}.
CC -!- INTERACTION:
CC P35918; P35917: Flt4; NbExp=3; IntAct=EBI-1555005, EBI-7845747;
CC P35918; P16056: Met; NbExp=3; IntAct=EBI-1555005, EBI-1798780;
CC P35918; P08581: MET; Xeno; NbExp=3; IntAct=EBI-1555005, EBI-1039152;
CC P35918; P09619: PDGFRB; Xeno; NbExp=4; IntAct=EBI-1555005, EBI-641237;
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:15673613,
CC ECO:0000269|PubMed:19635461, ECO:0000269|PubMed:19668192}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:P35968}. Cell membrane
CC {ECO:0000250|UniProtKB:P35968}. Note=Colocalizes with ERN1 and XBP1 in
CC the endoplasmic reticulum in endothelial cells in a vascular
CC endothelial growth factor (VEGF)-dependent manner (By similarity).
CC Localized with RAP1A at cell-cell junctions.
CC {ECO:0000250|UniProtKB:P35968}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasmic vesicle {ECO:0000250}. Early endosome {ECO:0000250}.
CC Note=Detected on caveolae-enriched lipid rafts at the cell surface. Is
CC recycled from the plasma membrane to endosomes and back again.
CC Phosphorylation triggered by VEGFA binding promotes internalization and
CC subsequent degradation. VEGFA binding triggers internalization and
CC translocation to the nucleus (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=mbVegfr-2;
CC IsoId=P35918-1; Sequence=Displayed;
CC Name=2; Synonyms=sVegfr-2;
CC IsoId=P35918-2; Sequence=VSP_041986, VSP_041987;
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells (at protein level).
CC Detected in embryonic endothelial cells, as well as hematopoietic stem
CC and progenitor cells. Detected in vascular endothelium. Expressed at
CC high levels in adult heart, lung, kidney, brain and skeletal muscle,
CC but is also expressed at lower levels in most other adult tissues.
CC {ECO:0000269|PubMed:1717995, ECO:0000269|PubMed:19635461,
CC ECO:0000269|PubMed:8356051, ECO:0000269|PubMed:8423988}.
CC -!- DEVELOPMENTAL STAGE: Expressed in endothelial cells of
CC allantois/umbilical vessels at 8.5 dpc (at protein level). Increases
CC moderately during pregnancy (maximum 2.7-fold at 19 days), and
CC increases further during lactation (maximum 3.7-fold increase on day
CC 7). {ECO:0000269|PubMed:10878616, ECO:0000269|PubMed:19635461}.
CC -!- DOMAIN: The second and third Ig-like C2-type (immunoglobulin-like)
CC domains are sufficient for VEGFC binding. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Tyrosine phosphorylation of the receptor promotes
CC its poly-ubiquitination, leading to its degradation via the proteasome
CC or lysosomal proteases (By similarity). {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-949 is important for interaction with
CC SH2D2A/TSAD and VEGFA-mediated reorganization of the actin
CC cytoskeleton. Phosphorylation at Tyr-1173 is important for interaction
CC with PLCG1 and SHB. Phosphorylation at Tyr-1212 is important for
CC interaction with NCK1 and FYN. Dephosphorylated by PTPRJ at Tyr-799,
CC Tyr-949, Tyr-994, Tyr-1052, Tyr-1057, Tyr-1173 and Tyr-1212 (By
CC similarity). {ECO:0000250|UniProtKB:P35968}.
CC -!- PTM: The inhibitory disulfide bond between Cys-1022 and Cys-1043 may
CC serve as a specific molecular switch for H(2)S-induced modification
CC that regulates KDR/VEGFR2 function. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality at 8.5 to 9.5 dpc, due to
CC early defects in the development of hematopoietic and endothelial
CC cells, leading to defects in vasculogenesis and endocardium
CC development. At 7.5 dpc, there are no blood islands in the yolk sac.
CC Organized blood vessels are absent in the yolk sac and in the embryo.
CC {ECO:0000269|PubMed:7596435}.
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA42040.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA50192.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X70842; CAA50192.1; ALT_FRAME; mRNA.
DR EMBL; X59397; CAA42040.1; ALT_FRAME; mRNA.
DR EMBL; S53103; AAB25043.1; -; mRNA.
DR EMBL; EU884114; ACJ66293.1; -; mRNA.
DR EMBL; AC124615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020530; AAH20530.1; -; mRNA.
DR EMBL; AC160723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC134903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X89777; CAA61917.1; -; Genomic_DNA.
DR CCDS; CCDS39114.1; -. [P35918-1]
DR PIR; A41228; A41228.
DR RefSeq; NP_034742.2; NM_010612.2. [P35918-1]
DR AlphaFoldDB; P35918; -.
DR SMR; P35918; -.
DR CORUM; P35918; -.
DR DIP; DIP-215N; -.
DR IntAct; P35918; 13.
DR MINT; P35918; -.
DR STRING; 10090.ENSMUSP00000109144; -.
DR BindingDB; P35918; -.
DR ChEMBL; CHEMBL3337; -.
DR DrugCentral; P35918; -.
DR GuidetoPHARMACOLOGY; 1813; -.
DR GlyGen; P35918; 17 sites, 11 N-linked glycans (10 sites).
DR iPTMnet; P35918; -.
DR PhosphoSitePlus; P35918; -.
DR MaxQB; P35918; -.
DR PaxDb; P35918; -.
DR PRIDE; P35918; -.
DR ProteomicsDB; 297595; -. [P35918-1]
DR ProteomicsDB; 297596; -. [P35918-2]
DR ProteomicsDB; 336554; -.
DR ABCD; P35918; 30 sequenced antibodies.
DR Antibodypedia; 3413; 3684 antibodies from 52 providers.
DR DNASU; 16542; -.
DR Ensembl; ENSMUST00000113516; ENSMUSP00000109144; ENSMUSG00000062960. [P35918-1]
DR GeneID; 16542; -.
DR KEGG; mmu:16542; -.
DR UCSC; uc008xul.2; mouse.
DR UCSC; uc012dxk.2; mouse. [P35918-2]
DR CTD; 3791; -.
DR MGI; MGI:96683; Kdr.
DR VEuPathDB; HostDB:ENSMUSG00000062960; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000156710; -.
DR HOGENOM; CLU_000288_49_4_1; -.
DR InParanoid; P35918; -.
DR OMA; RIFWDSK; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; P35918; -.
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 Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5218921; VEGFR2 mediated cell proliferation.
DR BioGRID-ORCS; 16542; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Kdr; mouse.
DR PRO; PR:P35918; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P35918; protein.
DR Bgee; ENSMUSG00000062960; Expressed in vasculature of trunk and 288 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005769; C:early endosome; IDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0097443; C:sorting endosome; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0015026; F:coreceptor activity; IGI:ARUK-UCL.
DR GO; GO:0019838; F:growth factor binding; IPI:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; ISO:MGI.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IDA:MGI.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0060837; P:blood vessel endothelial cell differentiation; IMP:MGI.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:MGI.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IDA:MGI.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:UniProtKB.
DR GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR GO; GO:0016477; P:cell migration; IGI:MGI.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:1904881; P:cellular response to hydrogen sulfide; ISO:MGI.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:UniProtKB.
DR GO; GO:0003157; P:endocardium development; IMP:UniProtKB.
DR GO; GO:0003416; P:endochondral bone growth; ISO:MGI.
DR GO; GO:0045446; P:endothelial cell differentiation; IDA:MGI.
DR GO; GO:0061154; P:endothelial tube morphogenesis; ISO:MGI.
DR GO; GO:0003158; P:endothelium development; IMP:UniProtKB.
DR GO; GO:0002070; P:epithelial cell maturation; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0001945; P:lymph vessel development; IGI:MGI.
DR GO; GO:0008584; P:male gonad development; ISO:MGI.
DR GO; GO:0010463; P:mesenchymal cell proliferation; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:ARUK-UCL.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; ISO:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:MGI.
DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:BHF-UCL.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:DFLAT.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IDA:DFLAT.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISO:MGI.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISO:MGI.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISO:MGI.
DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; TAS:DFLAT.
DR GO; GO:2001214; P:positive regulation of vasculogenesis; IMP:UniProtKB.
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:0043491; P:protein kinase B signaling; ISO:MGI.
DR GO; GO:1903010; P:regulation of bone development; IMP:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0001936; P:regulation of endothelial cell proliferation; TAS:DFLAT.
DR GO; GO:1901532; P:regulation of hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IGI:ARUK-UCL.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0043129; P:surfactant homeostasis; 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; IDA:MGI.
DR GO; GO:0036324; P:vascular endothelial growth factor receptor-2 signaling pathway; ISO:MGI.
DR GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; ISO:MGI.
DR GO; GO:0061042; P:vascular wound healing; ISO:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:UniProtKB.
DR GO; GO:0042311; P:vasodilation; 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; IPR009136; VEGFR2_rcpt.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF17988; VEGFR-2_TMD; 1.
DR PRINTS; PR01834; VEGFRECEPTR2.
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 Alternative splicing; Angiogenesis; ATP-binding; Cell junction;
KW Cell membrane; Cytoplasm; Cytoplasmic vesicle; Developmental protein;
KW Differentiation; Disulfide bond; Endoplasmic reticulum; Endosome;
KW Glycoprotein; Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1345
FT /note="Vascular endothelial growth factor receptor 2"
FT /id="PRO_0000016772"
FT TOPO_DOM 20..762
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 763..783
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 784..1345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..111
FT /note="Ig-like C2-type 1"
FT DOMAIN 143..209
FT /note="Ig-like C2-type 2"
FT DOMAIN 226..325
FT /note="Ig-like C2-type 3"
FT DOMAIN 330..416
FT /note="Ig-like C2-type 4"
FT DOMAIN 423..542
FT /note="Ig-like C2-type 5"
FT DOMAIN 549..656
FT /note="Ig-like C2-type 6"
FT DOMAIN 665..751
FT /note="Ig-like C2-type 7"
FT DOMAIN 832..1160
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1272..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1026
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 838..846
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 866
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 1173
FT /note="Interaction with SHB"
FT MOD_RES 799
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35968"
FT MOD_RES 949
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35968"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35968"
FT MOD_RES 982
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35968"
FT MOD_RES 994
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35968"
FT MOD_RES 1052
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15673613"
FT MOD_RES 1057
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15673613"
FT MOD_RES 1173
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35968"
FT MOD_RES 1212
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12023952"
FT MOD_RES 1229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1236
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1303
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35968"
FT MOD_RES 1307
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35968"
FT MOD_RES 1317
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35968"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
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 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 248..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 447..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 569..640
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 686..735
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1022..1043
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 661..673
FT /note="ERMAPMITGNLEN -> GMEASLGDRIAMP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19668192"
FT /id="VSP_041986"
FT VAR_SEQ 674..1345
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19668192"
FT /id="VSP_041987"
FT MUTAGEN 866
FT /note="K->R: Loss of enzyme activity. Abolishes
FT ubiquitination in response to VEGFA binding."
FT /evidence="ECO:0000269|PubMed:15673613"
FT MUTAGEN 1173
FT /note="Y->F: Loss of interaction with SHB."
FT /evidence="ECO:0000269|PubMed:15026417"
FT MUTAGEN 1188
FT /note="S->A: Strongly reduces internalization and down-
FT regulation of the activated receptor; when associated with
FT A-1191."
FT /evidence="ECO:0000269|PubMed:15673613"
FT MUTAGEN 1191
FT /note="S->A: Strongly reduces internalization and down-
FT regulation of the activated receptor; when associated with
FT A-1188."
FT /evidence="ECO:0000269|PubMed:15673613"
FT MUTAGEN 1212
FT /note="Y->F: Strongly reduced autophosphorylation."
FT /evidence="ECO:0000269|PubMed:12023952"
FT CONFLICT 25
FT /note="P -> T (in Ref. 1; CAA50192)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="G -> D (in Ref. 3; AAB25043)"
FT /evidence="ECO:0000305"
FT CONFLICT 783..784
FT /note="VL -> LV (in Ref. 2; CAA42040 and 3; AAB25043)"
FT /evidence="ECO:0000305"
FT CONFLICT 917
FT /note="C -> S (in Ref. 2; CAA42040 and 3; AAB25043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1345 AA; 150462 MW; 11859F8A58A33A39 CRC64;
MESKALLAVA LWFCVETRAA SVGLPGDFLH PPKLSTQKDI LTILANTTLQ ITCRGQRDLD
WLWPNAQRDS EERVLVTECG GGDSIFCKTL TIPRVVGNDT GAYKCSYRDV DIASTVYVYV
RDYRSPFIAS VSDQHGIVYI TENKNKTVVI PCRGSISNLN VSLCARYPEK RFVPDGNRIS
WDSEIGFTLP SYMISYAGMV FCEAKINDET YQSIMYIVVV VGYRIYDVIL SPPHEIELSA
GEKLVLNCTA RTELNVGLDF TWHSPPSKSH HKKIVNRDVK PFPGTVAKMF LSTLTIESVT
KSDQGEYTCV ASSGRMIKRN RTFVRVHTKP FIAFGSGMKS LVEATVGSQV RIPVKYLSYP
APDIKWYRNG RPIESNYTMI VGDELTIMEV TERDAGNYTV ILTNPISMEK QSHMVSLVVN
VPPQIGEKAL ISPMDSYQYG TMQTLTCTVY ANPPLHHIQW YWQLEEACSY RPGQTSPYAC
KEWRHVEDFQ GGNKIEVTKN QYALIEGKNK TVSTLVIQAA NVSALYKCEA INKAGRGERV
ISFHVIRGPE ITVQPAAQPT EQESVSLLCT ADRNTFENLT WYKLGSQATS VHMGESLTPV
CKNLDALWKL NGTMFSNSTN DILIVAFQNA SLQDQGDYVC SAQDKKTKKR HCLVKQLIIL
ERMAPMITGN LENQTTTIGE TIEVTCPASG NPTPHITWFK DNETLVEDSG IVLRDGNRNL
TIRRVRKEDG GLYTCQACNV LGCARAETLF IIEGAQEKTN LEVIILVGTA VIAMFFWLLL
VIVLRTVKRA NEGELKTGYL SIVMDPDELP LDERCERLPY DASKWEFPRD RLKLGKPLGR
GAFGQVIEAD AFGIDKTATC KTVAVKMLKE GATHSEHRAL MSELKILIHI GHHLNVVNLL
GACTKPGGPL MVIVEFCKFG NLSTYLRGKR NEFVPYKSKG ARFRQGKDYV GELSVDLKRR
LDSITSSQSS ASSGFVEEKS LSDVEEEEAS EELYKDFLTL EHLICYSFQV AKGMEFLASR
KCIHRDLAAR NILLSEKNVV KICDFGLARD IYKDPDYVRK GDARLPLKWM APETIFDRVY
TIQSDVWSFG VLLWEIFSLG ASPYPGVKID EEFCRRLKEG TRMRAPDYTT PEMYQTMLDC
WHEDPNQRPS FSELVEHLGN LLQANAQQDG KDYIVLPMSE TLSMEEDSGL SLPTSPVSCM
EEEEVCDPKF HYDNTAGISH YLQNSKRKSR PVSVKTFEDI PLEEPEVKVI PDDSQTDSGM
VLASEELKTL EDRNKLSPSF GGMMPSKSRE SVASEGSNQT SGYQSGYHSD DTDTTVYSSD
EAGLLKMVDA AVHADSGTTL RSPPV
