RAGP2_ARATH
ID RAGP2_ARATH Reviewed; 545 AA.
AC Q9M651;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=RAN GTPase-activating protein 2;
DE Short=AtRanGAP2;
DE Short=RanGAP2;
GN Name=RANGAP2; OrderedLocusNames=At5g19320; ORFNames=F7K24.70;
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=12061901; DOI=10.1046/j.1365-313x.2002.01324.x;
RA Pay A., Resch K., Frohnmeyer H., Fejes E., Nagy F., Nick P.;
RT "Plant RanGAPs are localized at the nuclear envelope in interphase and
RT associated with microtubules in mitotic cells.";
RL Plant J. 30:699-709(2002).
RN [2]
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 [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 INTERACTION WITH WIP1 AND WIP2.
RX PubMed=17600715; DOI=10.1016/j.cub.2007.05.076;
RA Xu X.M., Meulia T., Meier I.;
RT "Anchorage of plant RanGAP to the nuclear envelope involves novel nuclear-
RT pore-associated proteins.";
RL Curr. Biol. 17:1157-1163(2007).
RN [5]
RP INTERACTION WITH WIT1.
RX PubMed=18591351; DOI=10.1105/tpc.108.059220;
RA Zhao Q., Brkljacic J., Meier I.;
RT "Two distinct interacting classes of nuclear envelope-associated coiled-
RT coil proteins are required for the tissue-specific nuclear envelope
RT targeting of Arabidopsis RanGAP.";
RL Plant Cell 20:1639-1651(2008).
RN [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: GTPase activator for the nuclear Ras-related regulatory
CC protein Ran, converting it to the putatively inactive GDP-bound state.
CC {ECO:0000269|PubMed:12061901}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with WIP1 and WIP2
CC through its WPP domain. Component of Ran complexes at least composed of
CC WIT1 or WIT2, RANGAP1 or RANGAP2, and WIP1 or WIP2 or WIP3. Interacts
CC with WIT1. {ECO:0000250, ECO:0000269|PubMed:17600715,
CC ECO:0000269|PubMed:18591351}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Cytoplasm,
CC cytoskeleton, phragmoplast. Note=Localized in patchy areas at the
CC nuclear envelope of interphase cells. During mitosis, associates with
CC mitotic spindles at the anaphase. Associated to the microtubular
CC phragmoplast and the surface of the daughter nuclei at the telophase.
CC -!- DOMAIN: The WPP domain is required for the nuclear envelope
CC localization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA1 family. {ECO:0000305}.
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DR EMBL; AF214560; AAF25948.1; -; mRNA.
DR EMBL; AF296837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92685.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69837.1; -; Genomic_DNA.
DR PIR; T52068; T52068.
DR RefSeq; NP_001318597.1; NM_001343596.1.
DR RefSeq; NP_197433.1; NM_121937.5.
DR AlphaFoldDB; Q9M651; -.
DR SMR; Q9M651; -.
DR BioGRID; 17328; 1.
DR IntAct; Q9M651; 3.
DR STRING; 3702.AT5G19320.1; -.
DR iPTMnet; Q9M651; -.
DR PaxDb; Q9M651; -.
DR PRIDE; Q9M651; -.
DR ProteomicsDB; 236343; -.
DR EnsemblPlants; AT5G19320.1; AT5G19320.1; AT5G19320.
DR EnsemblPlants; AT5G19320.2; AT5G19320.2; AT5G19320.
DR GeneID; 832052; -.
DR Gramene; AT5G19320.1; AT5G19320.1; AT5G19320.
DR Gramene; AT5G19320.2; AT5G19320.2; AT5G19320.
DR KEGG; ath:AT5G19320; -.
DR Araport; AT5G19320; -.
DR TAIR; locus:2150285; AT5G19320.
DR eggNOG; KOG1909; Eukaryota.
DR HOGENOM; CLU_020837_0_0_1; -.
DR InParanoid; Q9M651; -.
DR OMA; ANQQFER; -.
DR OrthoDB; 1357476at2759; -.
DR PhylomeDB; Q9M651; -.
DR PRO; PR:Q9M651; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9M651; baseline and differential.
DR Genevisible; Q9M651; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; TAS:TAIR.
DR Gene3D; 1.10.246.200; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR045203; RanGAP1/2.
DR InterPro; IPR025265; WPP_dom.
DR InterPro; IPR038214; WPP_sf.
DR PANTHER; PTHR46761; PTHR46761; 1.
DR Pfam; PF13516; LRR_6; 5.
DR Pfam; PF13943; WPP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; GTPase activation; Leucine-rich repeat; Membrane;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..545
FT /note="RAN GTPase-activating protein 2"
FT /id="PRO_0000347215"
FT REPEAT 213..236
FT /note="LRR 1"
FT REPEAT 241..264
FT /note="LRR 2"
FT REPEAT 269..296
FT /note="LRR 3"
FT REPEAT 325..348
FT /note="LRR 4"
FT REPEAT 353..380
FT /note="LRR 5"
FT REPEAT 382..405
FT /note="LRR 6"
FT REPEAT 410..433
FT /note="LRR 7"
FT REPEAT 439..462
FT /note="LRR 8"
FT REPEAT 467..494
FT /note="LRR 9"
FT REGION 1..116
FT /note="WPP"
FT REGION 496..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..527
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 438..439
FT /note="GH -> VN (in Ref. 1; AAF25948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 59652 MW; 9484A095ECCC36F9 CRC64;
MADILDSRPH AFSIKLWPPS LPTRKALIER ITNNFSSKTI FTEKYGSLTK DQATENAKRI
EDIAFSTANQ QFEREPDGDG GSAVQLYAKE CSKLILEVLK KGPVAKVAAR ELISEDSVSP
RETFFDISKG KRAFIEAEEA EELLKPLKEP GNAYTKICFS NRSFGLGAAR VAEPILASLK
DQLKEVDLSD FVAGRPELEA LEVMNIFSDA LQGSILSSLN LSDNALGEKG VRAFGALLKS
LSSLEELYLM NDGISKEAAQ AVSELIPSTE NLRVLHFHNN MTGDEGALAI AEVVKRSPLL
ENFRCSSTRV GSKGGIALSE ALEHCTHMEK LDLRDNMFGT EAGVSLSKTL SSFKHMTELY
LSYLNLEDEG AIAIVNALKE SASPIEVLEM AGNDITVEAA SAIAACVAAK QDLNKLNLSE
NELKDEGCVQ IANCIEEGHS KLQYIDMSTN YIRRAGARAL AHVVVKKEAF KLLNIDGNII
SEEGIEELKE IFKKSPELLG ALDENDPDGE EDDDDEEDEE DEENEGNGNG ELESKLKNLE
VNQED
