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ROGF7_ARATH
ID   ROGF7_ARATH             Reviewed;         546 AA.
AC   Q9LZN0;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Rop guanine nucleotide exchange factor 7;
DE            Short=AtRopGEF7;
DE   AltName: Full=Rho of plants guanine nucleotide exchange factor 7;
GN   Name=ROPGEF7; OrderedLocusNames=At5g02010; ORFNames=T7H20.60;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY.
RX   PubMed=15980860; DOI=10.1038/nature03883;
RA   Berken A., Thomas C., Wittinghofer A.;
RT   "A new family of RhoGEFs activates the Rop molecular switch in plants.";
RL   Nature 436:1176-1180(2005).
RN   [6]
RP   FUNCTION, INTERACTION WITH ARAC1/ROP3; PLT1 AND PLT2, DEVELOPMENTAL STAGE,
RP   AND INDUCTION BY AUXIN.
RX   PubMed=21828289; DOI=10.1105/tpc.111.085514;
RA   Chen M., Liu H., Kong J., Yang Y., Zhang N., Li R., Yue J., Huang J.,
RA   Li C., Cheung A.Y., Tao L.Z.;
RT   "RopGEF7 regulates PLETHORA-dependent maintenance of the root stem cell
RT   niche in Arabidopsis.";
RL   Plant Cell 23:2880-2894(2011).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=22984069; DOI=10.1126/science.1222597;
RA   Oda Y., Fukuda H.;
RT   "Initiation of cell wall pattern by a Rho- and microtubule-driven symmetry
RT   breaking.";
RL   Science 337:1333-1336(2012).
CC   -!- FUNCTION: Guanine-nucleotide exchange factor (GEF) that acts as an
CC       activator of Rop (Rho of plants) GTPases by promoting the exchange of
CC       GDP for GTP. In postembryonic roots, modulates root stem cell
CC       maintenance by regulating the expression of PLT1 and PLT2, which are
CC       key transcription factors that mediate the patterning of the root stem
CC       cell niche. May connect RopGEF-regulated Rac/Rop signaling and auxin-
CC       dependent PLT-regulated root pattern formation.
CC       {ECO:0000269|PubMed:21828289}.
CC   -!- SUBUNIT: Interacts with ARAC1/ROP3, PLT1 and PLT2.
CC       {ECO:0000269|PubMed:21828289}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22984069}. Cell
CC       membrane {ECO:0000269|PubMed:22984069}. Note=Interacts with ARAC1/ROP3
CC       on plasma membrane.
CC   -!- DEVELOPMENTAL STAGE: During embryogenesis, specifically expressed in
CC       the precursor cells of the quiescent center (QC) at the heart, torpedo,
CC       bent-cotyledon, and mature embryo stages. At the seedling stage,
CC       expressed in the QC and vascular bundles of root differentiated zones
CC       and lateral root primordia. Expressed in the vasculature of hypocotyls,
CC       and meristemoids and guard cells of cotyledons.
CC       {ECO:0000269|PubMed:21828289}.
CC   -!- INDUCTION: By auxin. {ECO:0000269|PubMed:21828289}.
CC   -!- DOMAIN: The PRONE (plant-specific Rop nucleotide exchanger) domain is
CC       responsible for the GEF activity. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Plants silencing ROPGEF7 show defects in embryo
CC       patterning and maintenance of the quiescent center (QC), and
CC       postembryonic loss of root stem cell population.
CC       {ECO:0000305|PubMed:22984069}.
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DR   EMBL; AL162508; CAB82974.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90419.1; -; Genomic_DNA.
DR   EMBL; BT015831; AAU94394.1; -; mRNA.
DR   EMBL; BT020213; AAV59279.1; -; mRNA.
DR   PIR; T48222; T48222.
DR   RefSeq; NP_195821.1; NM_120279.3.
DR   AlphaFoldDB; Q9LZN0; -.
DR   SMR; Q9LZN0; -.
DR   DIP; DIP-59396N; -.
DR   IntAct; Q9LZN0; 1.
DR   STRING; 3702.AT5G02010.1; -.
DR   iPTMnet; Q9LZN0; -.
DR   PaxDb; Q9LZN0; -.
DR   PRIDE; Q9LZN0; -.
DR   ProteomicsDB; 228189; -.
DR   EnsemblPlants; AT5G02010.1; AT5G02010.1; AT5G02010.
DR   GeneID; 831858; -.
DR   Gramene; AT5G02010.1; AT5G02010.1; AT5G02010.
DR   KEGG; ath:AT5G02010; -.
DR   Araport; AT5G02010; -.
DR   TAIR; locus:2185153; AT5G02010.
DR   eggNOG; ENOG502QPIY; Eukaryota.
DR   HOGENOM; CLU_019073_2_1_1; -.
DR   InParanoid; Q9LZN0; -.
DR   OMA; TEKKEMW; -.
DR   OrthoDB; 383472at2759; -.
DR   PhylomeDB; Q9LZN0; -.
DR   PRO; PR:Q9LZN0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LZN0; baseline and differential.
DR   Genevisible; Q9LZN0; AT.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:TAIR.
DR   GO; GO:0009664; P:plant-type cell wall organization; IMP:TAIR.
DR   InterPro; IPR005512; PRONE_dom.
DR   InterPro; IPR038937; RopGEF.
DR   PANTHER; PTHR33101; PTHR33101; 1.
DR   Pfam; PF03759; PRONE; 1.
DR   PROSITE; PS51334; PRONE; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW   Reference proteome.
FT   CHAIN           1..546
FT                   /note="Rop guanine nucleotide exchange factor 7"
FT                   /id="PRO_0000423893"
FT   DOMAIN          61..440
FT                   /note="PRONE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00663"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   546 AA;  61753 MW;  FDA3B16C01DE041E CRC64;
     MDGSSENLPE VEEKGRESSC CSSETTRQEE EEQSPSCTED FTASPVSSRW SVKNIDGEKK
     KIRSDSRVSE VEMMKERFSK LLLGEDMSGS GNGVCTALAI SNAITNLCAT LFGQLWRLEP
     LPTEKKEMWR REMEWLLCVS DHIVEMTPTW QTFPDGTKLE IMTCRPRSDL YVNLPALRKL
     DNMLLEILDS FEETEFWYVD QGIMAHESAA DGSSSFRKSF QRQEDKWWLP VPRVSPGGLQ
     ENSRKQLQHK RDCTNQILKA AMAINSITLA DMEIPESYLE SLPRKGRSCL GDLIYRYISS
     DQFSPECLLD CLDLSSEHQA IEIANRVESS IYLWHKRTNS KPATNTKTSW EMVKELMVDA
     DKLELMADRA ESLLLSLKQR FPGLPQTALD MSKIQYNKDI GKSILESYSR VLESLAFNIV
     ARIDDLLFVD DLTRHSSDQI PTTLGNNGND APKSIAVPVS NYTTPSYSPS KQELRSSITV
     PPSPSRFKIP HSSSVKRVLT AYVTKNEPRL KNLPLERSSR SSSSERLSLE KCMKESLNVS
     NLDPGI
 
 
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