MON1_ARATH
ID MON1_ARATH Reviewed; 607 AA.
AC Q9SKN1; Q680T1; Q93ZL8;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Vacuolar fusion protein MON1 homolog {ECO:0000305};
GN Name=MON1 {ECO:0000303|PubMed:24824487};
GN OrderedLocusNames=At2g28390 {ECO:0000312|Araport:AT2G28390};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=16166256; DOI=10.1104/pp.105.063743;
RA Czechowski T., Stitt M., Altmann T., Udvardi M.K., Scheible W.R.;
RT "Genome-wide identification and testing of superior reference genes for
RT transcript normalization in Arabidopsis.";
RL Plant Physiol. 139:5-17(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP INTERACTION WITH CCZ1A; CCZ1B AND RABF2B, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24824487; DOI=10.1105/tpc.114.123141;
RA Cui Y., Zhao Q., Gao C., Ding Y., Zeng Y., Ueda T., Nakano A., Jiang L.;
RT "Activation of the Rab7 GTPase by the MON1-CCZ1 complex is essential for
RT PVC-to-vacuole trafficking and plant growth in Arabidopsis.";
RL Plant Cell 26:2080-2097(2014).
CC -!- FUNCTION: Plays an important role in membrane trafficking through the
CC secretory apparatus. In complex with CCZ1, acts as a guanine exchange
CC factor (GEF) for RABG3F of the Rab7 protein family. Promotes the
CC exchange of GDP to GTP, converting RABG3F from an inactive GDP-bound
CC form into an active GTP-bound form. The RABG3F active form is involved
CC in protein trafficking from prevacuolar compartments (PVCs) to
CC vacuoles. May serve as a linker between Rab5 and Rab7 protein families
CC in PVCs and mediate PVC maturation. {ECO:0000269|PubMed:24824487}.
CC -!- SUBUNIT: Interacts with CCZ1A, CCZ1B and RABF2B.
CC {ECO:0000269|PubMed:24824487}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:24824487}.
CC Prevacuolar compartment {ECO:0000269|PubMed:24824487}.
CC -!- TISSUE SPECIFICITY: Widely expressed at stable levels.
CC {ECO:0000269|PubMed:16166256}.
CC -!- DISRUPTION PHENOTYPE: Severe plant growth defects, such as short root
CC phenotype, retarded growth and dwarf phenotype.
CC {ECO:0000269|PubMed:10617197}.
CC -!- MISCELLANEOUS: Due to the stability of its transcription during plant
CC development, this gene is proposed as a reference gene for transcript
CC normalization. {ECO:0000305|PubMed:16166256}.
CC -!- SIMILARITY: Belongs to the MON1/SAND family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC006283; AAD20687.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08115.1; -; Genomic_DNA.
DR EMBL; AY056801; AAL10492.1; -; mRNA.
DR EMBL; AY133524; AAM91354.1; -; mRNA.
DR EMBL; AK118037; BAC42668.1; -; mRNA.
DR EMBL; AK175575; BAD43338.1; -; mRNA.
DR EMBL; AK175699; BAD43462.1; -; mRNA.
DR EMBL; AK175786; BAD43549.1; -; mRNA.
DR EMBL; AK176064; BAD43827.1; -; mRNA.
DR EMBL; AK176154; BAD43917.1; -; mRNA.
DR EMBL; AK221211; BAD93763.1; -; mRNA.
DR PIR; C84684; C84684.
DR RefSeq; NP_029426.1; NM_128399.4.
DR AlphaFoldDB; Q9SKN1; -.
DR SMR; Q9SKN1; -.
DR STRING; 3702.AT2G28390.1; -.
DR iPTMnet; Q9SKN1; -.
DR PaxDb; Q9SKN1; -.
DR PRIDE; Q9SKN1; -.
DR ProteomicsDB; 250879; -.
DR EnsemblPlants; AT2G28390.1; AT2G28390.1; AT2G28390.
DR GeneID; 817387; -.
DR Gramene; AT2G28390.1; AT2G28390.1; AT2G28390.
DR KEGG; ath:AT2G28390; -.
DR Araport; AT2G28390; -.
DR TAIR; locus:2057552; AT2G28390.
DR eggNOG; KOG0997; Eukaryota.
DR HOGENOM; CLU_014574_3_1_1; -.
DR InParanoid; Q9SKN1; -.
DR OMA; TKTCAIT; -.
DR OrthoDB; 829786at2759; -.
DR PhylomeDB; Q9SKN1; -.
DR PRO; PR:Q9SKN1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKN1; baseline and differential.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:UniProtKB.
DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
DR GO; GO:0006623; P:protein targeting to vacuole; IEA:InterPro.
DR GO; GO:0007033; P:vacuole organization; IMP:UniProtKB.
DR InterPro; IPR043972; FUZ/MON1/HPS1_longin_1.
DR InterPro; IPR043971; FUZ/MON1/HPS1_longin_2.
DR InterPro; IPR043970; FUZ/MON1/HPS1_longin_3.
DR InterPro; IPR004353; Mon1.
DR PANTHER; PTHR13027; PTHR13027; 1.
DR Pfam; PF19036; Fuz_longin_1; 1.
DR Pfam; PF19037; Fuz_longin_2; 1.
DR Pfam; PF19038; Fuz_longin_3; 1.
DR PRINTS; PR01546; YEAST73DUF.
PE 1: Evidence at protein level;
KW Endosome; Guanine-nucleotide releasing factor; Reference proteome.
FT CHAIN 1..607
FT /note="Vacuolar fusion protein MON1 homolog"
FT /id="PRO_0000438479"
FT REGION 1..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 528
FT /note="A -> V (in Ref. 4; BAD43549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 66924 MW; 41ABB543CFFCC821 CRC64;
MATSDSRSSP SSSDTEFADP NPSSDPETNS ERVQSQLESM NLSQPSEVSD GSHTEFSGGG
DDNDDEVASA NGNEGGVSNG GLLREGVAGT SGGEVLLRAE NPVEMEAGEE PPSPTSSGYD
GERGSSGGAT STYKADDGSE DEIREANVDG DTASQHEAAW LPGKRHVDED DASTSWRKRK
KHFFILSNSG KPIYSRYGDE HKLAGFSATL QAIISFVENG GDRVNLVKAG NHQVVFLVKG
PIYLVCISCT DETYEYLRGQ LDLLYGQMIL ILTKSIDRCF EKNAKFDMTP LLGGTDAVFS
SLVHSFSWNP ATFLHAYTCL PLPYALRQAT GTILQEVCAS GVLFSLLMCR HKVVSLAGAQ
KASLHPDDLL LLSNFVMSSE SFRTSESFSP ICLPRYNAQA FLHAYVHFFD DDTYVILLTT
RSDAFHHLKD CRVRLEAVLL KSNILSVVQR SIAEGGMRVE DVPIDRRRRS STTNQEQDSP
GPDISVGTGG PFGLWHFMYR SIYLDQYISS EFSPPVTSHR QQKSLYRAYQ KLYASMHVKG
LGPHKTQYRR DENYTLLCWV TPDFELYAAF DPLADKAMAI KICNQVCQRV KDVENEVFLQ
GASPFSW
