VGFR3_RAT
ID VGFR3_RAT Reviewed; 1363 AA.
AC Q91ZT1; O35755; Q91ZT0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Vascular endothelial growth factor receptor 3;
DE Short=VEGFR-3;
DE EC=2.7.10.1;
DE AltName: Full=Fms-like tyrosine kinase 4;
DE Short=FLT-4;
DE AltName: Full=Tyrosine-protein kinase receptor FLT4;
DE Flags: Precursor;
GN Name=Flt4; Synonyms=Flt-4, Vegfr3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley;
RA Krishnan J., Sleeman J.P.;
RT "Characterization of a novel alternatively spliced form of VEGFR-3.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1053-1060, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1197-1315 (ISOFORM 1), AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
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).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor
CC for VEGFC and VEGFD, and plays an essential role in adult
CC lymphangiogenesis and in the development of the vascular network and
CC the cardiovascular system during embryonic development. Promotes
CC proliferation, survival and migration of endothelial cells, and
CC regulates angiogenic sprouting. Signaling by activated FLT4 leads to
CC enhanced production of VEGFC, and to a lesser degree VEGFA, thereby
CC creating a positive feedback loop that enhances FLT4 signaling.
CC Modulates KDR signaling by forming heterodimers. Mediates activation of
CC the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN
CC signaling pathway, and of the AKT1 signaling pathway. Phosphorylates
CC SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of
CC phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at
CC 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473' (By similarity).
CC {ECO:0000250|UniProtKB:P35916}.
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 VEGFC or VEGFD leads to dimerization and
CC activation by autophosphorylation on tyrosine residues (By similarity).
CC {ECO:0000250|UniProtKB:P35916}.
CC -!- SUBUNIT: Interacts with VEGFC and VEGFD. Monomer in the absence of
CC bound VEGFC or VEGFD. Homodimer in the presence of bound VEGFC or
CC VEGFD. Can also form a heterodimer with KDR. Interacts with PTPN14; the
CC interaction is enhanced by stimulation with VEGFC. Interacts with CRK,
CC GRB2, PTK2/FAK1, SHC1, PIK3R1 and PTPN11/SHP-2. Identified in a complex
CC with SRC and ITGB1 (By similarity). Identified in a complex with SRC
CC and ITGB1 (By similarity). {ECO:0000250|UniProtKB:P35916}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35917};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P35917}.
CC Cytoplasm {ECO:0000250|UniProtKB:P35917}. Nucleus
CC {ECO:0000250|UniProtKB:P35916}. Note=Ligand-mediated
CC autophosphorylation leads to rapid internalization.
CC {ECO:0000250|UniProtKB:P35917}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91ZT1-1; Sequence=Displayed;
CC Name=2; Synonyms=VEGFR3-kt;
CC IsoId=Q91ZT1-2; Sequence=VSP_016721, VSP_016722;
CC -!- DEVELOPMENTAL STAGE: Increases during pregnancy (2.2-fold at 4 days)
CC and lactation (1.5-fold at 21 days). Decreases in the early phases of
CC involution (33%, 21%, and 45% on days 1, 2, and 3 respectively).
CC {ECO:0000269|PubMed:10878616}.
CC -!- DOMAIN: The first and second Ig-like C2-type (immunoglobulin-like)
CC domains are sufficient for VEGFC binding. The fourth and fifth Ig-like
CC C2-type (immunoglobulin-like) domains are sufficient for
CC homodimerization. The fifth and seventh Ig-like C2-type
CC (immunoglobulin-like) domains are required for autophosphorylation and
CC further activation. {ECO:0000250|UniProtKB:P35916}.
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 in response to H(2)O(2) is mediated by a process that
CC requires SRC and PRKCD activity. Phosphorylation at Tyr-1068 is
CC required for autophosphorylation at additional tyrosine residues.
CC Phosphorylation at Tyr-1063 and Tyr-1337 is important for interaction
CC with CRK and subsequent activation of MAPK8. Phosphorylation at Tyr-
CC 1230, Tyr-1231 and Tyr-1337 is important for interaction with GRB2 and
CC subsequent activation of the AKT1 and MAPK1/ERK2 and/or MAPK3/ERK1
CC signaling pathways. In response to endothelial cell adhesion onto
CC collagen, can also be phosphorylated in the absence of FLT4 kinase
CC activity by SRC (By similarity). {ECO:0000250|UniProtKB:P35916}.
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; AF402785; AAL13269.1; -; mRNA.
DR EMBL; AF402786; AAL13270.1; -; mRNA.
DR EMBL; AF010131; AAB63249.1; -; mRNA.
DR RefSeq; NP_446104.1; NM_053652.1. [Q91ZT1-1]
DR AlphaFoldDB; Q91ZT1; -.
DR SMR; Q91ZT1; -.
DR IntAct; Q91ZT1; 1.
DR MINT; Q91ZT1; -.
DR STRING; 10116.ENSRNOP00000003519; -.
DR GlyGen; Q91ZT1; 12 sites.
DR iPTMnet; Q91ZT1; -.
DR PhosphoSitePlus; Q91ZT1; -.
DR jPOST; Q91ZT1; -.
DR PaxDb; Q91ZT1; -.
DR PRIDE; Q91ZT1; -.
DR GeneID; 114110; -.
DR KEGG; rno:114110; -.
DR UCSC; RGD:621737; rat. [Q91ZT1-1]
DR CTD; 2324; -.
DR RGD; 621737; Flt4.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; Q91ZT1; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; Q91ZT1; -.
DR Reactome; R-RNO-195399; VEGF binds to VEGFR leading to receptor dimerization.
DR PRO; PR:Q91ZT1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019838; F:growth factor binding; IMP:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IMP:RGD.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISS:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:RGD.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
DR GO; GO:0048286; P:lung alveolus development; ISO:RGD.
DR GO; GO:0001945; P:lymph vessel development; ISO:RGD.
DR GO; GO:0001946; P:lymphangiogenesis; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0060312; P:regulation of blood vessel remodeling; ISS:UniProtKB.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; ISO:RGD.
DR GO; GO:0003016; P:respiratory system process; ISO:RGD.
DR GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
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:RGD.
DR GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001944; P:vasculature development; 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 InterPro; IPR009137; VEGFR3_rcpt.
DR PANTHER; PTHR24416:SF562; PTHR24416:SF562; 1.
DR Pfam; PF07679; I-set; 1.
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; 5.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 6.
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 membrane; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1363
FT /note="Vascular endothelial growth factor receptor 3"
FT /id="PRO_0000045280"
FT TOPO_DOM 25..775
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 776..796
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 797..1363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 44..118
FT /note="Ig-like C2-type 1"
FT DOMAIN 151..213
FT /note="Ig-like C2-type 2"
FT DOMAIN 230..326
FT /note="Ig-like C2-type 3"
FT DOMAIN 331..415
FT /note="Ig-like C2-type 4"
FT DOMAIN 422..552
FT /note="Ig-like C2-type 5"
FT DOMAIN 555..671
FT /note="Ig-like C2-type 6"
FT DOMAIN 678..764
FT /note="Ig-like C2-type 7"
FT DOMAIN 845..1173
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1289..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1037
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 851..859
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 879
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 830
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P35916"
FT MOD_RES 833
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P35916"
FT MOD_RES 1063
FT /note="Phosphotyrosine; by autocatalysis and SRC"
FT /evidence="ECO:0000250|UniProtKB:P35916"
FT MOD_RES 1068
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35916"
FT MOD_RES 1230
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35916"
FT MOD_RES 1231
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35916"
FT MOD_RES 1265
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35916"
FT MOD_RES 1333
FT /note="Phosphotyrosine; by autocatalysis and SRC"
FT /evidence="ECO:0000250|UniProtKB:P35916"
FT MOD_RES 1337
FT /note="Phosphotyrosine; by autocatalysis and SRC"
FT /evidence="ECO:0000250|UniProtKB:P35916"
FT MOD_RES 1363
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35916"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 158..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 252..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 445..534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 466..486
FT /evidence="ECO:0000250|UniProtKB:P35916"
FT DISULFID 578..653
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 699..751
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1079..1092
FT /note="KWMAPESIFDKVYT -> HTLGYRSMRNSASG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_016721"
FT VAR_SEQ 1093..1363
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_016722"
SQ SEQUENCE 1363 AA; 153317 MW; 203E79172C614D6C CRC64;
MQPGAALNRR LWLCLGLLQG LANGYSMTPP TLNITEDSYV IDTGDSLSIS CRGQHPLEWT
WRGAQEVLTT GGKDSEDTQV VQDCEGTEAR PYCKVLSLAQ THANNTGSYY CYYKYIKARI
EGTTAASTYV FVRDFEQPFI NKPDTLLVNR KDSMWVPCLV SIPGLNITLR SQSSVLHPDG
QEVLWDDRRG MRVPTLLLRD ALYLQCETTW GDQDFLSNPF LVHITGNELY DIQLYPKKSL
ELLVGEKLVL NCTVWAEFDS GVTFDWDYPG KQAERAKWVP ERRSQQTHTE LSSILTIHNV
SQHDLGPYVC EANNGIQQFR ESTEVIVHEK PFISVEWLKG PVLEATAGDE MVKLPVKLAA
YPPPEFQWYK DRKAVTGRHN PHALVLKEVT EASAGVYTLA LWNSAAGLRQ NISLELVVNV
PPHIHEKEAS SPSIYSRHSR QTLTCTTYGV PQPLSVQWHW RPWTPCKTFA QRSLRRRQPR
DGMPQCRDWK EVTTQDAVNP IESLDTWTES VEGKNKTVSK LVIQDANVSA MYKCVVFNKV
GQDERLIYFY VTTIPDGFSI ESEPSEDPLE GQSVRLSCRA DNYTYEHLRW YRLNLSTLHD
AQGNPLLLDC KNVHLFATPL EANLEEAEPG ARHATLSLNI PRVAPEDEGD YVCEVQDRRS
QDKHCHKKYL SVQALEAPRL TQNLTDLLVN VRTSLEMRCP VAGAHVPSIV WYKDERLLEK
ESGIDLADSN QRLSIQRVRE EDAGRYLCSV CNAKGCVNSS ASVAVEGSED KGSMEIVILI
GTGVIAVFFW VLLLLIFCNM KRPAHADIKT GYLSIIMDPG EVPLEEQCEY LSYDVSQWEF
PRERLHLGRV LGHGAFGKVV EASAFGINKG SSCDTVAVKM LKEGATASEH RALMSELKIL
IHIGNHLNVV NLLGACTKPN GPLMVIVEFC KYGNLSNFLR VKRETFDPYA EKSPEQRRRF
RAMVEGAKAD RRRLGSTDRA LFTRFLMGKG SARRAPFVQE AEDLWLSPLT MEDLVCYSFQ
VARGMEFLAS RKCIHRDLAA RNILLSESDI VKICDFGLAR DIYKDPDYVR KGSARLPLKW
MAPESIFDKV YTTQSDVWSF GVLLWEIFSL GASPYPGVQI NEEFCQRLKD GTRMRAPELA
TPAIRHIMQS CWSGDPKARP AFSDLVEILG DLLQGGGWQE EEEECMALHS SQSSEEDGFM
QASTTALHIT EADAESSPPS MHCHSLAARY YNCVSFPGRL VRGTKAPGSS RMKTFEELPM
TPTTYKASVD NQTDSGMVLA SEEFEQIESR HRQEGSFSRK DPGQHMDISR GHPDLQGRRR
RPTQGAQGGK VFYNNEYGEV SQPCTEGDCC PSAGSTFFAD SNY
