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VEGFB_RAT
ID   VEGFB_RAT               Reviewed;         207 AA.
AC   O35485; O54881; Q6DGF3;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 3.
DT   03-AUG-2022, entry version 134.
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   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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM VEGF-B167).
RC   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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 32-181 (ISOFORM VEGF-B167).
RC   TISSUE=Heart;
RA   Weil J., Eschenhagen T., Mittmann C., Scholz H.;
RT   "Isolation and characterization of rat vascular endothelial growth factor B
RT   (VEGF-B).";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 51-186 (ISOFORM VEGF-B186).
RC   STRAIN=Sprague-Dawley; TISSUE=Placenta;
RA   Mandriota S.J., Pepper M.S.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Can also form heterodimer with
CC       VEGF (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted but remains
CC       associated to cells or to the extracellular matrix unless released by
CC       heparin. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=VEGF-B186;
CC         IsoId=O35485-1; Sequence=Displayed;
CC       Name=VEGF-B167;
CC         IsoId=O35485-2; Sequence=VSP_016662;
CC   -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC       {ECO:0000305}.
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DR   EMBL; AABR03002421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC076395; AAH76395.1; -; mRNA.
DR   EMBL; AF022952; AAB95447.1; -; mRNA.
DR   EMBL; AF032925; AAB86884.1; -; mRNA.
DR   RefSeq; NP_446001.1; NM_053549.1. [O35485-2]
DR   RefSeq; XP_006230972.1; XM_006230910.3. [O35485-1]
DR   RefSeq; XP_006230973.1; XM_006230911.3. [O35485-1]
DR   AlphaFoldDB; O35485; -.
DR   SMR; O35485; -.
DR   STRING; 10116.ENSRNOP00000049757; -.
DR   iPTMnet; O35485; -.
DR   PhosphoSitePlus; O35485; -.
DR   PaxDb; O35485; -.
DR   PRIDE; O35485; -.
DR   Ensembl; ENSRNOT00000050891; ENSRNOP00000049757; ENSRNOG00000021156. [O35485-2]
DR   GeneID; 89811; -.
DR   KEGG; rno:89811; -.
DR   UCSC; RGD:619799; rat. [O35485-1]
DR   CTD; 7423; -.
DR   RGD; 619799; Vegfb.
DR   VEuPathDB; HostDB:ENSRNOG00000021156; -.
DR   eggNOG; ENOG502SU5Y; Eukaryota.
DR   GeneTree; ENSGT00940000161844; -.
DR   HOGENOM; CLU_042996_2_0_1; -.
DR   InParanoid; O35485; -.
DR   OMA; PRCTQRH; -.
DR   OrthoDB; 1364454at2759; -.
DR   PhylomeDB; O35485; -.
DR   TreeFam; TF319554; -.
DR   Reactome; R-RNO-114608; Platelet degranulation.
DR   Reactome; R-RNO-194313; VEGF ligand-receptor interactions.
DR   Reactome; R-RNO-195399; VEGF binds to VEGFR leading to receptor dimerization.
DR   PRO; PR:O35485; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000021156; Expressed in heart and 19 other tissues.
DR   GO; GO:0005576; C:extracellular region; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0042056; F:chemoattractant activity; IBA:GO_Central.
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; ISO:RGD.
DR   GO; GO:0043183; F:vascular endothelial growth factor receptor 1 binding; ISO:RGD.
DR   GO; GO:0005172; F:vascular endothelial growth factor receptor binding; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IEP:RGD.
DR   GO; GO:0060048; P:cardiac muscle contraction; ISO:RGD.
DR   GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
DR   GO; GO:0007507; P:heart development; ISO:RGD.
DR   GO; GO:0050930; P:induction of positive chemotaxis; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0060754; P:positive regulation of mast cell chemotaxis; IBA:GO_Central.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0035470; P:positive regulation of vascular wound healing; ISO:RGD.
DR   GO; GO:0006493; P:protein O-linked glycosylation; ISO:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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; Disulfide bond; Growth factor; Heparin-binding;
KW   Mitogen; 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_0000045174"
FT   REGION          140..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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="RVAIPHHRPQPRSVLSWDSAPGASSPADIIHPTPAPGPSAHAAPSAVSALIP
FT                   GPAVAAADAAASSIAKGGA -> SPRTLCPRCTQRRQRPDPRTCRCRCRRRRFLHCQGR
FT                   GLELNPDTCRSSET (in isoform VEGF-B167)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT                   /id="VSP_016662"
FT   CONFLICT        32..33
FT                   /note="QK -> KR (in Ref. 3; AAB95447)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        60
FT                   /note="L -> F (in Ref. 3; AAB95447)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="L -> F (in Ref. 3; AAB95447)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="K -> R (in Ref. 4; AAB86884)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   207 AA;  21869 MW;  1A7F7DC4F8D0C9E2 CRC64;
     MSPLLRRLLL VALLQLACTQ APVSQFDGPS HQKKVVSWID VYARATCQPR EVVVPLSMEL
     MGNVVKQLVP SCVTVQRCGG CCPDDGLECV PIGQHQVRMQ ILMIQYPSSQ LGEMSLEEHS
     QCECRPKRKE SAVKPDRVAI PHHRPQPRSV LSWDSAPGAS SPADIIHPTP APGPSAHAAP
     SAVSALIPGP AVAAADAAAS SIAKGGA
 
 
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