NSN1_ARATH
ID NSN1_ARATH Reviewed; 582 AA.
AC Q9M8Z5; Q93Y17;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Guanine nucleotide-binding protein-like NSN1 {ECO:0000305};
DE Short=Nucleolar GTP-binding protein NSN1 {ECO:0000305};
DE AltName: Full=DAR GTPase 4 {ECO:0000303|PubMed:16849600};
DE AltName: Full=Protein nucleostemin-like 1 {ECO:0000303|PubMed:22357616};
GN Name=NSN1 {ECO:0000303|PubMed:22357616};
GN Synonyms=DGP4 {ECO:0000303|PubMed:16849600};
GN OrderedLocusNames=At3g07050 {ECO:0000312|Araport:AT3G07050};
GN ORFNames=F17A9.21 {ECO:0000312|EMBL:AAF27009.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION
RP PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=22357616; DOI=10.1091/mbc.e11-09-0797;
RA Wang X., Gingrich D.K., Deng Y., Hong Z.;
RT "A nucleostemin-like GTPase required for normal apical and floral meristem
RT development in Arabidopsis.";
RL Mol. Biol. Cell 23:1446-1456(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-531.
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 [5]
RP DOMAIN, AND GENE FAMILY.
RX PubMed=9573393; DOI=10.1016/s0378-1119(98)00088-2;
RA Fu G., Melville S., Brewster S., Warner J., Barker D.C.;
RT "Analysis of the genomic organisation of a small chromosome of Leishmania
RT braziliensis M2903 reveals two genes encoding GTP-binding proteins, one of
RT which belongs to a new G-protein family and is an antigen.";
RL Gene 210:325-333(1998).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16849600; DOI=10.1534/genetics.106.060657;
RA Hill T.A., Broadhvest J., Kuzoff R.K., Gasser C.S.;
RT "Arabidopsis SHORT INTEGUMENTS 2 is a mitochondrial DAR GTPase.";
RL Genetics 174:707-718(2006).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=22058024; DOI=10.1007/s11103-011-9840-7;
RA Wang X., Xie B., Zhu M., Zhang Z., Hong Z.;
RT "Nucleostemin-like 1 is required for embryogenesis and leaf development in
RT Arabidopsis.";
RL Plant Mol. Biol. 78:31-44(2012).
RN [8]
RP FUNCTION, INTERACTION WITH EBP2 AND PES, AND SUBCELLULAR LOCATION.
RX PubMed=26163696; DOI=10.1093/jxb/erv337;
RA Jeon Y., Park Y.J., Cho H.K., Jung H.J., Ahn T.K., Kang H., Pai H.S.;
RT "The nucleolar GTPase nucleostemin-like 1 plays a role in plant growth and
RT senescence by modulating ribosome biogenesis.";
RL J. Exp. Bot. 66:6297-6310(2015).
CC -!- FUNCTION: Involved in the differentiation of epidermal cells, probably
CC via the regulation of the expression of meristem-related genes (e.g.
CC CLV3, STM, KNAT1, CUC2 and AG) and of leaf polarity-related genes (e.g.
CC YAB5, FIL, AS2, PHB and PHV) (PubMed:22058024, PubMed:22357616). May
CC play a role in regulating cellular proliferation (By similarity).
CC Necessary for flower development, probably by preventing apical
CC dominance through the down-regulation of AG expression
CC (PubMed:22357616). Required for embryogenesis, leaf and cotyledon
CC development, as well as for leaf polarity establishment
CC (PubMed:22058024). Plays an important role in plant growth and
CC senescence by modulating ribosome biogenesis in nucleolus. Possesses
CC GTPAse activity in vitro. Possesses RNA binding activity in vitro.
CC Associates with ribosomes (PubMed:26163696).
CC {ECO:0000250|UniProtKB:Q8MT06, ECO:0000269|PubMed:22058024,
CC ECO:0000269|PubMed:22357616, ECO:0000269|PubMed:26163696}.
CC -!- SUBUNIT: Interacts with EBP2 and PES. {ECO:0000269|PubMed:26163696}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC Nucleus, nucleolus {ECO:0000269|PubMed:22357616,
CC ECO:0000269|PubMed:26163696}. Note=Shuttles between the nucleus and
CC nucleolus. {ECO:0000250|UniProtKB:Q811S9}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers, siliques and
CC inflorescence apex, and, to a lower extent, in stems and leaves.
CC {ECO:0000269|PubMed:22357616}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in developing embryos and in the
CC primordia of cotyledons and leaves (PubMed:22058024). Accumulates
CC mostly in the inflorescence meristem and in floral primordia. Low
CC levels in the inflorescence meristem dome, but high levels in the
CC floral primordia already in early stages. Accumulates progressively in
CC floral organ primordia to become concentrated in the primordia of
CC stamens and carpels. At the later stages of floral development,
CC expressed primarily in developing microspores in the stamens and ovules
CC in the carpels (PubMed:22357616). {ECO:0000269|PubMed:22058024,
CC ECO:0000269|PubMed:22357616}.
CC -!- DOMAIN: The basic domain (B) allows nucleolar localization in the
CC absence of GTP. The intermediate domain (I) inhibits nucleolar
CC localization by the B domain and is required for exit from the
CC nucleolus. Exit from the nucleolus to the nucleoplasm requires both the
CC I and the acidic (A) domains, and may be triggered by GTP hydrolysis.
CC {ECO:0000250|UniProtKB:Q811S9}.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern. {ECO:0000305}.
CC -!- DOMAIN: The DARXP motif is also sometime designated as G6 region.
CC {ECO:0000305|PubMed:9573393}.
CC -!- DISRUPTION PHENOTYPE: Dwarf with severe defects in reproduction,
CC eventual arrest in embryo development that can occur at any stage of
CC embryogenesis, distorted cotyledons, and upward curled leaves probably
CC due to disoriented leaf polarity. Ectopic meristem-like outgrowths on
CC the surface of cotyledons and leaves (PubMed:22058024). Abnormal
CC expression of meristem-related genes and of leaf polarity-related genes
CC (PubMed:22357616, PubMed:22058024). Heterozygote plants develop
CC defective flowers and siliques on inflorescences sometimes terminated
CC by the formation of carpelloid flower, and thus leading to a highly
CC reduced self-fertility (PubMed:22357616). {ECO:0000269|PubMed:22058024,
CC ECO:0000269|PubMed:22357616}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK96878.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; JX644918; AFW99797.1; -; mRNA.
DR EMBL; AC016827; AAF27009.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74493.1; -; Genomic_DNA.
DR EMBL; AY054687; AAK96878.1; ALT_FRAME; mRNA.
DR RefSeq; NP_187361.1; NM_111585.5.
DR AlphaFoldDB; Q9M8Z5; -.
DR SMR; Q9M8Z5; -.
DR BioGRID; 5225; 1.
DR STRING; 3702.AT3G07050.1; -.
DR iPTMnet; Q9M8Z5; -.
DR PaxDb; Q9M8Z5; -.
DR PRIDE; Q9M8Z5; -.
DR ProteomicsDB; 249132; -.
DR EnsemblPlants; AT3G07050.1; AT3G07050.1; AT3G07050.
DR GeneID; 819890; -.
DR Gramene; AT3G07050.1; AT3G07050.1; AT3G07050.
DR KEGG; ath:AT3G07050; -.
DR Araport; AT3G07050; -.
DR TAIR; locus:2077587; AT3G07050.
DR eggNOG; KOG2484; Eukaryota.
DR HOGENOM; CLU_011106_5_0_1; -.
DR InParanoid; Q9M8Z5; -.
DR OMA; FKLDGLW; -.
DR OrthoDB; 1210675at2759; -.
DR PhylomeDB; Q9M8Z5; -.
DR PRO; PR:Q9M8Z5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8Z5; baseline and differential.
DR Genevisible; Q9M8Z5; AT.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0048825; P:cotyledon development; IMP:UniProtKB.
DR GO; GO:0048444; P:floral organ morphogenesis; IMP:TAIR.
DR GO; GO:0010077; P:maintenance of inflorescence meristem identity; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0045604; P:regulation of epidermal cell differentiation; IMP:UniProtKB.
DR GO; GO:2000024; P:regulation of leaf development; IMP:UniProtKB.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR014813; Gnl3_N_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF08701; GN3L_Grn1; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; GTP-binding; Nucleotide-binding;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..582
FT /note="Guanine nucleotide-binding protein-like NSN1"
FT /id="PRO_0000431376"
FT DOMAIN 127..311
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..49
FT /note="Basic"
FT /evidence="ECO:0000250|UniProtKB:Q811S9"
FT REGION 175..178
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 202..204
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 260..267
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 281..456
FT /note="Intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q811S9"
FT REGION 286..290
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 304..307
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 463..551
FT /note="Acidic"
FT /evidence="ECO:0000250|UniProtKB:Q811S9"
FT REGION 469..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..94
FT /evidence="ECO:0000255"
FT COILED 515..537
FT /evidence="ECO:0000255"
FT MOTIF 5..12
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 22..29
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 69..76
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 145..149
FT /note="DARXP motif"
FT MOTIF 522..529
FT /note="Nuclear localization signal 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..40
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 175..178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 263..268
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 304..307
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 307
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT CONFLICT 506
FT /note="T -> A (in Ref. 4; AAK96878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 65786 MW; AFD1B2607CB624CD CRC64;
MVKRSKKSKS KRVTLKQKHK VLKKVKEHHK KKAKDAKKLG LHRKPRVEKD PGIPNDWPFK
EQELKALEVR RARALEEIEQ KKEARKERAK KRKLGLVDDE DTKTEGETIE DLPKVVNVRD
NSERAFYKEL VKVIELSDVI LEVLDARDPL GTRCTDMERM VMQAGPNKHL VLLLNKIDLV
PREAAEKWLM YLREEFPAVA FKCSTQEQRS NLGWKSSKAS KPSNMLQTSD CLGADTLIKL
LKNYSRSHEL KKSITVGIIG LPNVGKSSLI NSLKRAHVVN VGATPGLTRS LQEVHLDKNV
KLLDCPGVVM LKSSGNDASI ALRNCKRIEK LDDPVSPVKE ILKLCPKDML VTLYKIPSFE
AVDDFLYKVA TVRGKLKKGG LVDIDAAARI VLHDWNEGKI PYYTMPPKRD QGGHAESKIV
TELAKDFNID EVYSGESSFI GSLKTVNEFN PVIIPSNGPL NFDETMIEDE SKTQTEEEAE
HESDDDESMG GEEEEEAGKT KEKSETGRQN VKLYAAESML NTKKQKAEKK KRKKAKKAGA
DEEDLMDGDY DFKVDYRKNK DGEDEEFQID AKIPMAGLLP EE
