QQT2_ARATH
ID QQT2_ARATH Reviewed; 379 AA.
AC Q8W586; O49703; Q8L9E7; Q9SVR7;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=GPN-loop GTPase QQT2 {ECO:0000305};
DE EC=3.6.5.- {ECO:0000305};
DE AltName: Full=Protein QUATRE QUART 2 {ECO:0000303|PubMed:17419841};
GN Name=QQT2 {ECO:0000303|PubMed:17419841};
GN Synonyms=quatre-quart2 {ECO:0000312|EMBL:AEE84504.1};
GN OrderedLocusNames=At4g21800 {ECO:0000312|Araport:AT4G21800};
GN ORFNames=F17L22.260 {ECO:0000312|EMBL:CAB81287.1},
GN T8O5.10 {ECO:0000312|EMBL:CAA17147.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 FUNCTION, INTERACTION WITH QQT1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=17419841; DOI=10.1111/j.1365-313x.2007.03072.x;
RA Lahmy S., Guilleminot J., Schmit A.C., Pelletier G., Chaboute M.E.,
RA Devic M.;
RT "QQT proteins colocalize with microtubules and are essential for early
RT embryo development in Arabidopsis.";
RL Plant J. 50:615-626(2007).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Small GTPase that is essential for the correct formation of
CC the tangential divisions in early embryos. Associates with microtubule
CC during mitosis and may function in the positioning of the division
CC plane. May participate in the patterning of the early embryo at the
CC octant-dermatogen transition. {ECO:0000269|PubMed:17419841}.
CC -!- SUBUNIT: Heterodimer with QQT1. {ECO:0000269|PubMed:17419841}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17419841}. Nucleus
CC {ECO:0000269|PubMed:17419841}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:17419841}. Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:17419841}. Note=During interphase, mainly expressed
CC in the cytoplasm and weakly in the nucleus. Associated with
CC microtubules during cell division. {ECO:0000269|PubMed:17419841}.
CC -!- TISSUE SPECIFICITY: Expressed in individual cells of roots, leaves and
CC flowers. {ECO:0000269|PubMed:17419841}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, expressed in the embryo from
CC octant to heart stage. {ECO:0000269|PubMed:17419841}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality due to embryo development
CC arrest at the octant stage. {ECO:0000269|PubMed:17419841}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81287.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021890; CAA17147.1; -; Genomic_DNA.
DR EMBL; AL035527; CAB36824.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161555; CAB81287.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84504.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84505.1; -; Genomic_DNA.
DR EMBL; AF419563; AAL31895.1; -; mRNA.
DR EMBL; AY143879; AAN28818.1; -; mRNA.
DR EMBL; AY088472; AAM66008.1; -; mRNA.
DR PIR; A85249; A85249.
DR PIR; T05462; T05462.
DR RefSeq; NP_193911.1; NM_118300.3.
DR RefSeq; NP_974586.1; NM_202857.2.
DR AlphaFoldDB; Q8W586; -.
DR SMR; Q8W586; -.
DR IntAct; Q8W586; 1.
DR STRING; 3702.AT4G21800.2; -.
DR iPTMnet; Q8W586; -.
DR PaxDb; Q8W586; -.
DR PRIDE; Q8W586; -.
DR ProteomicsDB; 226143; -.
DR EnsemblPlants; AT4G21800.1; AT4G21800.1; AT4G21800.
DR EnsemblPlants; AT4G21800.2; AT4G21800.2; AT4G21800.
DR GeneID; 828268; -.
DR Gramene; AT4G21800.1; AT4G21800.1; AT4G21800.
DR Gramene; AT4G21800.2; AT4G21800.2; AT4G21800.
DR KEGG; ath:AT4G21800; -.
DR Araport; AT4G21800; -.
DR TAIR; locus:2119093; AT4G21800.
DR eggNOG; KOG1532; Eukaryota.
DR HOGENOM; CLU_037460_1_1_1; -.
DR InParanoid; Q8W586; -.
DR OMA; MIIVFNK; -.
DR OrthoDB; 1096688at2759; -.
DR PhylomeDB; Q8W586; -.
DR PRO; PR:Q8W586; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W586; baseline and differential.
DR GO; GO:0005874; C:microtubule; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231; PTHR21231; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; GTP-binding; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..379
FT /note="GPN-loop GTPase QQT2"
FT /id="PRO_0000443287"
FT REGION 303..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 288..322
FT /evidence="ECO:0000255"
FT MOTIF 108..110
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT COMPBIAS 303..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..373
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 211..214
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 267
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 110
FT /note="Stabilizes the phosphate intermediate; shared with
FT dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 379 AA; 42551 MW; BB146A3225BB9A9A CRC64;
MDPMESSSEQ DIVEESQKLV DSLDKLRVSA ASSSSNFKKK PIIIIVVGMA GSGKTSFLHR
LVCHTFDSKS HGYVVNLDPA VMSLPFGANI DIRDTVKYKE VMKQYNLGPN GGILTSLNLF
ATKFDEVVSV IEKRADQLDY VLVDTPGQIE IFTWSASGAI ITEAFASTFP TVVTYVVDTP
RSSSPITFMS NMLYACSILY KTRLPLVLAF NKTDVADHKF ALEWMEDFEV FQAAIQSDNS
YTATLANSLS LSLYEFYRNI RSVGVSAISG AGMDGFFKAI EASAEEYMET YKADLDMRKA
DKERLEEERK KHEMEKLRKD MESSQGGTVV LNTGLKDRDA TEKMMLEEDD EDFQVEDEED
SDDAIDEDDE DDETKHYYL
