VEGFB_MOUSE
ID VEGFB_MOUSE Reviewed; 207 AA.
AC P49766; Q3UG04; Q5D0B1; Q64290;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Vascular endothelial growth factor B;
DE Short=VEGF-B;
DE AltName: Full=VEGF-related factor;
DE Short=VRF;
DE Flags: Precursor;
GN Name=Vegfb; Synonyms=Vrf;
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] (ISOFORMS VEGF-B186 AND VEGF-B167).
RC TISSUE=Brain;
RX PubMed=8607868; DOI=10.1006/bbrc.1996.0507;
RA Townson S., Lagercrantz J., Grimmond S., Silins G., Nordenskjoeld M.,
RA Weber G., Hayward N.K.;
RT "Characterization of the murine VEGF-related factor gene.";
RL Biochem. Biophys. Res. Commun. 220:922-928(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF-B186).
RC TISSUE=Heart;
RX PubMed=8702615; DOI=10.1074/jbc.271.32.19310;
RA Olofsson B., Pajusola K., von Euler G., Chilov D., Alitalo K., Eriksson U.;
RT "Genomic organization of the mouse and human genes for vascular endothelial
RT growth factor B (VEGF-B) and characterization of a second splice isoform.";
RL J. Biol. Chem. 271:19310-19317(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF-B167).
RC TISSUE=Heart;
RX PubMed=8637916; DOI=10.1073/pnas.93.6.2576;
RA Olofsson B., Pajusola K., Kaipainen A., von Euler G., Joukov V.,
RA Saksela O., Orpana A., Pettersson R.F., Alitalo K., Eriksson U.;
RT "Vascular endothelial growth factor B, a novel growth factor for
RT endothelial cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:2576-2581(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM VEGF-B186).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM VEGF-B167).
RC TISSUE=Eye;
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 [6]
RP FUNCTION.
RX PubMed=11457758; DOI=10.1161/01.cir.104.3.358;
RA Aase K., von Euler G., Li X., Ponten A., Thoren P., Cao R., Cao Y.,
RA Olofsson B., Gebre-Medhin S., Pekny M., Alitalo K., Betsholtz C.,
RA Eriksson U.;
RT "Vascular endothelial growth factor-B-deficient mice display an atrial
RT conduction defect.";
RL Circulation 104:358-364(2001).
CC -!- FUNCTION: Growth factor for endothelial cells. VEGF-B167 binds heparin
CC and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is
CC regulated by proteolysis. VEGF-B seems to be required for normal heart
CC function in adult but is not required for proper development of the
CC cardiovascular system either during development or for angiogenesis in
CC adults. {ECO:0000269|PubMed:11457758}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Can also form heterodimer with
CC VEGF.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted but remains associated to
CC cells or to the extracellular matrix unless released by heparin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=VEGF-B186;
CC IsoId=P49766-1; Sequence=Displayed;
CC Name=VEGF-B167;
CC IsoId=P49766-2; Sequence=VSP_004641;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in heart, brain, kidney and
CC skeletal muscle.
CC -!- PTM: VEGF-B186 is O-glycosylated.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; U43836; AAC52932.1; -; mRNA.
DR EMBL; U43837; AAC52553.1; -; mRNA.
DR EMBL; U52820; AAC52823.1; -; mRNA.
DR EMBL; U48800; AAB06273.1; -; mRNA.
DR EMBL; AK148188; BAE28405.1; -; mRNA.
DR EMBL; BC046303; AAH46303.1; -; mRNA.
DR CCDS; CCDS29516.1; -. [P49766-1]
DR CCDS; CCDS50373.1; -. [P49766-2]
DR PIR; JC4679; JC4679.
DR PIR; JC4680; JC4680.
DR RefSeq; NP_001172093.1; NM_001185164.1. [P49766-2]
DR RefSeq; NP_035827.1; NM_011697.3. [P49766-1]
DR AlphaFoldDB; P49766; -.
DR SMR; P49766; -.
DR BioGRID; 204513; 4.
DR IntAct; P49766; 1.
DR STRING; 10090.ENSMUSP00000025914; -.
DR PhosphoSitePlus; P49766; -.
DR PaxDb; P49766; -.
DR PeptideAtlas; P49766; -.
DR PRIDE; P49766; -.
DR ProteomicsDB; 275177; -. [P49766-1]
DR ProteomicsDB; 275178; -. [P49766-2]
DR Antibodypedia; 15308; 707 antibodies from 36 providers.
DR DNASU; 22340; -.
DR Ensembl; ENSMUST00000025914; ENSMUSP00000025914; ENSMUSG00000024962. [P49766-1]
DR Ensembl; ENSMUST00000130048; ENSMUSP00000120860; ENSMUSG00000024962. [P49766-2]
DR GeneID; 22340; -.
DR KEGG; mmu:22340; -.
DR UCSC; uc008gjv.2; mouse. [P49766-1]
DR UCSC; uc008gjw.2; mouse. [P49766-2]
DR CTD; 7423; -.
DR MGI; MGI:106199; Vegfb.
DR VEuPathDB; HostDB:ENSMUSG00000024962; -.
DR eggNOG; ENOG502SU5Y; Eukaryota.
DR GeneTree; ENSGT00940000161844; -.
DR HOGENOM; CLU_042996_2_0_1; -.
DR InParanoid; P49766; -.
DR OMA; PRCTQRH; -.
DR OrthoDB; 1364454at2759; -.
DR PhylomeDB; P49766; -.
DR TreeFam; TF319554; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-194313; VEGF ligand-receptor interactions.
DR Reactome; R-MMU-195399; VEGF binds to VEGFR leading to receptor dimerization.
DR BioGRID-ORCS; 22340; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Vegfb; mouse.
DR PRO; PR:P49766; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P49766; protein.
DR Bgee; ENSMUSG00000024962; Expressed in myocardium and 266 other tissues.
DR Genevisible; P49766; MM.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0043183; F:vascular endothelial growth factor receptor 1 binding; ISO:MGI.
DR GO; GO:0005172; F:vascular endothelial growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0050930; P:induction of positive chemotaxis; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IBA:GO_Central.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0060754; P:positive regulation of mast cell chemotaxis; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0035470; P:positive regulation of vascular wound healing; ISO:MGI.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:MGI.
DR GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
DR GO; GO:0002040; P:sprouting angiogenesis; IBA:GO_Central.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; IBA:GO_Central.
DR CDD; cd00135; PDGF; 1.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR023581; PD_growth_factor_CS.
DR InterPro; IPR000072; PDGF/VEGF_dom.
DR Pfam; PF00341; PDGF; 1.
DR SMART; SM00141; PDGF; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00249; PDGF_1; 1.
DR PROSITE; PS50278; PDGF_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Angiogenesis; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Growth factor; Heparin-binding; Mitogen;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..207
FT /note="Vascular endothelial growth factor B"
FT /id="PRO_0000023399"
FT REGION 129..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 47..89
FT /evidence="ECO:0000250"
FT DISULFID 72
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 78..122
FT /evidence="ECO:0000250"
FT DISULFID 81
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 82..124
FT /evidence="ECO:0000250"
FT VAR_SEQ 137..207
FT /note="RVAIPHHRPQPRSVPGWDSTPGASSPADIIHPTPAPGSSARLAPSAVNALTP
FT GPAAAAADAAASSIAKGGA -> SPRILCPPCTQRRQRPDPRTCRCRCRRRRFLHCQGR
FT GLELNPDTCRCRKPRK (in isoform VEGF-B167)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8607868, ECO:0000303|PubMed:8637916"
FT /id="VSP_004641"
FT CONFLICT 69
FT /note="V -> A (in Ref. 4; BAE28405)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 21914 MW; 4817A5E96F6960C2 CRC64;
MSPLLRRLLL VALLQLARTQ APVSQFDGPS HQKKVVPWID VYARATCQPR EVVVPLSMEL
MGNVVKQLVP SCVTVQRCGG CCPDDGLECV PTGQHQVRMQ ILMIQYPSSQ LGEMSLEEHS
QCECRPKKKE SAVKPDRVAI PHHRPQPRSV PGWDSTPGAS SPADIIHPTP APGSSARLAP
SAVNALTPGP AAAAADAAAS SIAKGGA
