MOB1A_ARATH
ID MOB1A_ARATH Reviewed; 215 AA.
AC Q9FHI1; Q56W53;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=MOB kinase activator-like 1A {ECO:0000303|PubMed:19468312};
DE AltName: Full=Mob1 homolog 1A {ECO:0000303|PubMed:19468312};
DE AltName: Full=Mps one binder kinase activator-like 1A {ECO:0000303|PubMed:19468312};
GN Name=MOB1A {ECO:0000303|PubMed:19468312};
GN OrderedLocusNames=At5g45550 {ECO:0000312|Araport:AT5G45550};
GN ORFNames=MFC19.22 {ECO:0000312|EMBL:BAB09183.1};
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-215.
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15469496; DOI=10.1111/j.1365-313x.2004.02222.x;
RA Van Damme D., Bouget F.-Y., Van Poucke K., Inze D., Geelen D.;
RT "Molecular dissection of plant cytokinesis and phragmoplast structure: a
RT survey of GFP-tagged proteins.";
RL Plant J. 40:386-398(2004).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19468312;
RA Vitulo N., Vezzi A., Galla G., Citterio S., Marino G., Ruperti B.,
RA Zermiani M., Albertini E., Valle G., Barcaccia G.;
RT "Characterization and evolution of the cell cycle-associated mob domain-
RT containing proteins in eukaryotes.";
RL Evol. Bioinform. Online 3:121-158(2007).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21641974; DOI=10.1016/j.gene.2011.05.009;
RA Galla G., Zenoni S., Marconi G., Marino G., Botton A., Pinosa F.,
RA Citterio S., Ruperti B., Palme K., Albertini E., Pezzotti M., Mau M.,
RA Sharbel T.F., De Storme N., Geelen D., Barcaccia G.;
RT "Sporophytic and gametophytic functions of the cell cycle-associated Mob1
RT gene in Arabidopsis thaliana L.";
RL Gene 484:1-12(2011).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24201137; DOI=10.1093/aob/mct235;
RA Pinosa F., Begheldo M., Pasternak T., Zermiani M., Paponov I.A.,
RA Dovzhenko A., Barcaccia G., Ruperti B., Palme K.;
RT "The Arabidopsis thaliana Mob1A gene is required for organ growth and
RT correct tissue patterning of the root tip.";
RL Ann. Bot. 112:1803-1814(2013).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SIK1, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=26685188; DOI=10.1093/jxb/erv538;
RA Xiong J., Cui X., Yuan X., Yu X., Sun J., Gong Q.;
RT "The Hippo/STE20 homolog SIK1 interacts with MOB1 to regulate cell
RT proliferation and cell expansion in Arabidopsis.";
RL J. Exp. Bot. 67:1461-1475(2016).
CC -!- FUNCTION: Plays a key role in regulation of cell expansion and cell
CC division (PubMed:26685188). Required for proper plant development, the
CC correct patterning of the root meristem and the control of root growth
CC (PubMed:24201137). Involved in both sporogenesis and gametogenesis
CC (PubMed:21641974). {ECO:0000269|PubMed:21641974,
CC ECO:0000269|PubMed:24201137, ECO:0000269|PubMed:26685188}.
CC -!- SUBUNIT: Interacts with SIK1 at the plasma membrane and in the nucleus.
CC {ECO:0000269|PubMed:26685188}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15469496,
CC ECO:0000269|PubMed:21641974, ECO:0000269|PubMed:26685188}. Cell
CC membrane {ECO:0000269|PubMed:26685188}. Vacuole membrane
CC {ECO:0000269|PubMed:26685188}. Note=Observed at the plasma membrane and
CC in the nucleus when associated with SIK1.
CC {ECO:0000269|PubMed:26685188}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed (PubMed:21641974). In
CC 3- to 4-day-old seedlings, expression is high in the shoot apical
CC meristem and along the vasculature in cotyledons, hypocotyls and roots.
CC At the root tip, expression is detected in columella and lateral root
CC cap cells as well as in the stem cell niche around the quiescent center
CC (QC). The levels of expression decrease progressively in the
CC meristematic zone from the root tip towards the base of the root,
CC becoming stronger again in the elongation zone. In flowers, expression
CC appears localized in ovules and pollen (PubMed:24201137).
CC {ECO:0000269|PubMed:21641974, ECO:0000269|PubMed:24201137}.
CC -!- DISRUPTION PHENOTYPE: Exhibits severe defects in the growth of
CC vegetative organs and in seed setting capacity: displays a reduction in
CC the rosette size and number of leaves, a reduction of siliques size
CC with high proportion of aborted ovules, a short root length with
CC reduction of the meristem size, of the number of cortical cells and of
CC the size of the elongation zone with root tips showing a distorted
CC cellular pattern (PubMed:24201137). Also exhibits a higher sensitivity
CC to abscissic acid (ABA) (PubMed:24201137). The double mutant sik1 mob1a
CC is arrested at the seedling stage (PubMed:26685188).
CC {ECO:0000269|PubMed:24201137, ECO:0000269|PubMed:26685188}.
CC -!- MISCELLANEOUS: RNAi plants show a reduced radial expansion of the
CC inflorescence stem, a reduced elongation zone of the primary root,
CC defects during sporogenesis and gametogenesis, and a reduced fertility.
CC {ECO:0000269|PubMed:21641974}.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
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DR EMBL; AB018113; BAB09183.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95267.1; -; Genomic_DNA.
DR EMBL; AY045864; AAK76538.1; -; mRNA.
DR EMBL; AY117158; AAM51233.1; -; mRNA.
DR EMBL; AY086730; AAM63781.1; -; mRNA.
DR EMBL; AK222194; BAD95338.1; -; mRNA.
DR RefSeq; NP_199368.1; NM_123923.6.
DR AlphaFoldDB; Q9FHI1; -.
DR SMR; Q9FHI1; -.
DR STRING; 3702.AT5G45550.1; -.
DR iPTMnet; Q9FHI1; -.
DR PaxDb; Q9FHI1; -.
DR PRIDE; Q9FHI1; -.
DR ProteomicsDB; 238260; -.
DR EnsemblPlants; AT5G45550.1; AT5G45550.1; AT5G45550.
DR GeneID; 834591; -.
DR Gramene; AT5G45550.1; AT5G45550.1; AT5G45550.
DR KEGG; ath:AT5G45550; -.
DR Araport; AT5G45550; -.
DR TAIR; locus:2163533; AT5G45550.
DR eggNOG; KOG0440; Eukaryota.
DR HOGENOM; CLU_038321_3_2_1; -.
DR InParanoid; Q9FHI1; -.
DR OMA; HYPVIVH; -.
DR OrthoDB; 1127941at2759; -.
DR PhylomeDB; Q9FHI1; -.
DR PRO; PR:Q9FHI1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHI1; baseline and differential.
DR Genevisible; Q9FHI1; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005769; C:early endosome; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IGI:TAIR.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IGI:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0048229; P:gametophyte development; IMP:UniProtKB.
DR GO; GO:0009554; P:megasporogenesis; IMP:TAIR.
DR GO; GO:0009556; P:microsporogenesis; IMP:TAIR.
DR GO; GO:0035265; P:organ growth; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0080141; P:regulation of jasmonic acid biosynthetic process; IGI:TAIR.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR GO; GO:0010449; P:root meristem growth; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.140.30; -; 1.
DR InterPro; IPR005301; MOB_kinase_act_fam.
DR InterPro; IPR036703; MOB_kinase_act_sf.
DR PANTHER; PTHR22599; PTHR22599; 1.
DR Pfam; PF03637; Mob1_phocein; 1.
DR SMART; SM01388; Mob1_phocein; 1.
DR SUPFAM; SSF101152; SSF101152; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Membrane; Metal-binding; Nucleus;
KW Reference proteome; Vacuole; Zinc.
FT CHAIN 1..215
FT /note="MOB kinase activator-like 1A"
FT /id="PRO_0000432416"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P40484"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P40484"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P40484"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P40484"
SQ SEQUENCE 215 AA; 24696 MW; D253C5E87EDB786A CRC64;
MSLFGLGRNQ KTFRPKKSAP SGSKGAQLRK HIDATLGSGN LREAVRLPPG EDANEWLAVN
TVDFFNQVNL LYGTLTEFCT PDNCPTMTAG PKYEYRWADG VQIKKPIEVS APKYVEYLMD
WIETQLDDET LFPQRLGAPF PQNFKDVVKT IFKRLFRVYA HIYHSHFQKI VSLKEEAHLN
TCFKHFILFT HEFGLIDKKE LAPLQELIES IISPY
