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VEA_GIBM7
ID   VEA_GIBM7               Reviewed;         531 AA.
AC   W7MRI4; A0MAR2;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Developmental and secondary metabolism regulator VE1 {ECO:0000305};
DE   AltName: Full=Velvet complex subunit 1 {ECO:0000305};
GN   Name=VE1 {ECO:0000303|PubMed:17054442};
GN   Synonyms=veA {ECO:0000303|PubMed:22247572}; ORFNames=FVEG_09521;
OS   Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS   fungus) (Fusarium verticillioides).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=334819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=M3125 / FGSC 7600;
RX   PubMed=17054442; DOI=10.1111/j.1365-2958.2006.05447.x;
RA   Li S., Myung K., Guse D., Donkin B., Proctor R.H., Grayburn W.S.,
RA   Calvo A.M.;
RT   "FvVE1 regulates filamentous growth, the ratio of microconidia to
RT   macroconidia and cell wall formation in Fusarium verticillioides.";
RL   Mol. Microbiol. 62:1418-1432(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=M3125 / FGSC 7600;
RX   PubMed=22247572; DOI=10.1111/j.1365-3059.2011.02504.x;
RA   Myung K., Zitomer N.C., Duvall M., Glenn A.E., Riley R.T., Calvo A.M.;
RT   "The conserved global regulator VeA is necessary for symptom production and
RT   mycotoxin synthesis in maize seedlings by Fusarium verticillioides.";
RL   Plant Pathol. 61:152-160(2012).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M3125 / FGSC 7600;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19382792; DOI=10.1021/jf900783u;
RA   Myung K., Li S., Butchko R.A., Busman M., Proctor R.H., Abbas H.K.,
RA   Calvo A.M.;
RT   "FvVE1 regulates biosynthesis of the mycotoxins fumonisins and fusarins in
RT   Fusarium verticillioides.";
RL   J. Agric. Food Chem. 57:5089-5094(2009).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH VELB AND VELC.
RX   PubMed=24792348; DOI=10.1128/ec.00022-14;
RA   Lan N., Zhang H., Hu C., Wang W., Calvo A.M., Harris S.D., Chen S., Li S.;
RT   "Coordinated and distinct functions of velvet proteins in Fusarium
RT   verticillioides.";
RL   Eukaryot. Cell 13:909-918(2014).
CC   -!- FUNCTION: Component of the velvet transcription factor complex that
CC       controls sexual/asexual developmental ratio in response to light,
CC       promoting sexual development in the darkness while stimulating asexual
CC       sporulation under illumination (By similarity). The velvet complex hat
CC       acts as a global regulator for secondary metabolite gene expression
CC       (PubMed:22247572). Controls the expression of the cycotoxins fumonisins
CC       and fusarins gene cluster (PubMed:22247572, PubMed:19382792,
CC       PubMed:24792348). Involved in cell wall integrity, cell surface
CC       hydrophobicity, hyphal polarity and conidiation pattern
CC       (PubMed:17054442, PubMed:24792348). Required for pathogenicity against
CC       maize seedlings (PubMed:22247572). Involved in oxidative stress
CC       resistance by positively regulating the transcription of the catalase-
CC       encoding gene CAT2 (PubMed:24792348). {ECO:0000250|UniProtKB:C8VTV4,
CC       ECO:0000269|PubMed:17054442, ECO:0000269|PubMed:19382792,
CC       ECO:0000269|PubMed:22247572}.
CC   -!- SUBUNIT: Component of the heterotrimeric velvet complex composed of
CC       LAE1, VE1 and VELB; VE1 acting as a bridging protein between LAE1 and
CC       VELB (By similarity). Interacts with VELB and VELC (PubMed:24792348).
CC       {ECO:0000250|UniProtKB:C8VTV4, ECO:0000269|PubMed:24792348}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VTV4}. Cytoplasm
CC       {ECO:0000250|UniProtKB:C8VTV4}. Note=Enriched in the nucleus in the
CC       dark (By similarity). {ECO:0000250|UniProtKB:C8VTV4}.
CC   -!- DOMAIN: The C-terminal PEST domain is a region rich in proline,
CC       glutamic acid, serine and threonine residues that is required for the
CC       light-dependent regulation of development and secondary metabolism (By
CC       similarity). {ECO:0000250|UniProtKB:C8VTV4}.
CC   -!- DISRUPTION PHENOTYPE: Suppresses aerial hyphal growth,reduced colony
CC       surface hydrophobicity on solid media, and increases the ratio of
CC       macroconidia to microconidia (PubMed:17054442, PubMed:24792348).
CC       Impairs production of fumonisins and fusarins, and reduces
CC       pathogenicity against maize seedlings (PubMed:22247572,
CC       PubMed:19382792, PubMed:24792348). {ECO:0000269|PubMed:17054442,
CC       ECO:0000269|PubMed:19382792, ECO:0000269|PubMed:22247572,
CC       ECO:0000269|PubMed:24792348}.
CC   -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
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DR   EMBL; DQ274059; ABC02879.1; -; Genomic_DNA.
DR   EMBL; DS022254; EWG50245.1; -; Genomic_DNA.
DR   RefSeq; XP_018756436.1; XM_018898529.1.
DR   AlphaFoldDB; W7MRI4; -.
DR   SMR; W7MRI4; -.
DR   PRIDE; W7MRI4; -.
DR   EnsemblFungi; FVEG_09521T0; FVEG_09521T0; FVEG_09521.
DR   GeneID; 30067169; -.
DR   KEGG; fvr:FVEG_09521; -.
DR   VEuPathDB; FungiDB:FVEG_09521; -.
DR   eggNOG; ENOG502S0HV; Eukaryota.
DR   HOGENOM; CLU_022491_2_0_1; -.
DR   OMA; NFFLYAT; -.
DR   OrthoDB; 1171722at2759; -.
DR   PHI-base; PHI:2858; -.
DR   Proteomes; UP000009096; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.3960; -; 1.
DR   InterPro; IPR021740; Velvet.
DR   InterPro; IPR037525; Velvet_dom.
DR   InterPro; IPR038491; Velvet_dom_sf.
DR   PANTHER; PTHR33572; PTHR33572; 1.
DR   Pfam; PF11754; Velvet; 2.
DR   PROSITE; PS51821; VELVET; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Reference proteome; Sporulation; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..531
FT                   /note="Developmental and secondary metabolism regulator
FT                   VE1"
FT                   /id="PRO_0000435764"
FT   DOMAIN          26..220
FT                   /note="Velvet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT   REGION          206..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..461
FT                   /note="PEST"
FT                   /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT   REGION          447..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           40..45
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT   COMPBIAS        215..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..308
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..463
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        192
FT                   /note="Y -> N (in Ref. 1; ABC02879)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="P -> R (in Ref. 1; ABC02879)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   531 AA;  58960 MW;  D57949BFF806739D CRC64;
     MATPSSIPAE PKRDVVNRIH RVTRGNRSLW YQMTVLQQPE RARACGSGSK ANSDRRPVDP
     PPVVELRIIE GPSVEEGKDI TFDYNANFFL YASLEHARPL ARGRVNTPAA GNPPILTGVP
     ASGMAYLDRP TEAGYFIFPD LSVRHEGLYI LTFSLFETTK EERDFDLEPA DGDLPPGVDY
     RMEIKTDPFS VYSAKKFPGL MESTQLSKTV ADQGCPVRIR RDVRMRKRES KPGAGNSNSG
     GNGFERREED FGRRRTITPA SEDPHSIRNR SHSNSSEQRT PYTDASRRPS MVDAYPPPPP
     PPPSYEPAPS ASRHLDFGDS SAAQYPTPRQ YAHQPGLQIT PGPPSASYAP TSQSPYSKTD
     APYGYVNRNI PPSCPSPAPS LKHELYDRRQ STSTYVPPSP SVYSTEGHHR RDSRPSYPPT
     PVAAPRPRPM HSQTSLPALK IDQLVSPVSP LPPIEPQTGP APELPPINVG GKRKHESVFA
     QSTRPLHNGQ RQVDPHYGRS HRGYSPDHDQ GWYSRADGQI SSVQFNRYYD E
 
 
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