MOB2A_ARATH
ID MOB2A_ARATH Reviewed; 216 AA.
AC F4K495;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=MOB kinase activator-like 2A;
DE AltName: Full=Mob1 homolog 2A;
DE AltName: Full=Mps one binder kinase activator-like 2A;
GN Name=MOB2A {ECO:0000303|PubMed:19468312};
GN OrderedLocusNames=At5g20440 {ECO:0000312|Araport:AT5G20440};
GN ORFNames=F7C8.30 {ECO:0000312|EMBL:AF296833};
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] OF 2-216.
RA Wrobel R.L., Kimball T.L., Steffen E., Thao S., Aceti D.J., Blommel P.G.,
RA Newman C.S., Zhao Q., Fox B.G., Phillips G.N. Jr., Markley J.L.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15469496}.
CC -!- SIMILARITY: Belongs to the MOB1/phocein 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; AF296833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92843.1; -; Genomic_DNA.
DR EMBL; BT012010; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_197544.3; NM_122051.5.
DR AlphaFoldDB; F4K495; -.
DR SMR; F4K495; -.
DR STRING; 3702.AT5G20440.1; -.
DR PaxDb; F4K495; -.
DR PRIDE; F4K495; -.
DR DNASU; 832166; -.
DR EnsemblPlants; AT5G20440.1; AT5G20440.1; AT5G20440.
DR GeneID; 832166; -.
DR Gramene; AT5G20440.1; AT5G20440.1; AT5G20440.
DR KEGG; ath:AT5G20440; -.
DR Araport; AT5G20440; -.
DR TAIR; locus:2149882; AT5G20440.
DR eggNOG; KOG0440; Eukaryota.
DR HOGENOM; CLU_038321_3_2_1; -.
DR InParanoid; F4K495; -.
DR OMA; NAGRYEY; -.
DR OrthoDB; 1127941at2759; -.
DR PhylomeDB; F4K495; -.
DR PRO; PR:F4K495; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K495; baseline and differential.
DR Genevisible; F4K495; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA: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:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Metal-binding; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..216
FT /note="MOB kinase activator-like 2A"
FT /id="PRO_0000432419"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P40484"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P40484"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P40484"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P40484"
SQ SEQUENCE 216 AA; 25235 MW; E5BDCAE8549E6AAB CRC64;
MGGFLVLNSS NNVVRTVPSK KRKHPEYKSK IRELISGIRS DNLREAVRLP QGVDINEWFA
MNTVDFFNQI SLLYATLEEF CTQTTCPVMN AGRYEYRWAD GTTITKPKTV SAPKYVEYLI
DWVETEIDNE AIFPKNPGEP FPPNFEDFVK RILRKLFRVY AHIYYSHFHE IVALNEQAHL
NTCFKHFLLF VSEFQLVDKE KEMAPIKSLV ETMLDQ