RAGP1_ARATH
ID RAGP1_ARATH Reviewed; 535 AA.
AC Q9LE82;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=RAN GTPase-activating protein 1;
DE Short=AtRanGAP1;
DE Short=RanGAP1;
GN Name=RANGAP1; OrderedLocusNames=At3g63130; ORFNames=T20O10.230;
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=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].
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 MUTAGENESIS OF 18-TRP-PRO-19, SUBCELLULAR LOCATION, AND DOMAIN WPP.
RX PubMed=11752475; DOI=10.1073/pnas.261459698;
RA Rose A., Meier I.;
RT "A domain unique to plant RanGAP is responsible for its targeting to the
RT plant nuclear rim.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:15377-15382(2001).
RN [6]
RP INTERACTION WITH WIP1; WIP2 AND WIP3, AND SUBCELLULAR LOCATION.
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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH POK1.
RX PubMed=19011093; DOI=10.1073/pnas.0806157105;
RA Xu X.M., Zhao Q., Rodrigo-Peiris T., Brkljacic J., He C.S., Mueller S.,
RA Meier I.;
RT "RanGAP1 is a continuous marker of the Arabidopsis cell division plane.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18637-18642(2008).
RN [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=22270916; DOI=10.1083/jcb.201108098;
RA Zhou X., Graumann K., Evans D.E., Meier I.;
RT "Novel plant SUN-KASH bridges are involved in RanGAP anchoring and nuclear
RT shape determination.";
RL J. Cell Biol. 196:203-211(2012).
CC -!- FUNCTION: GTPase activator for the nuclear Ras-related regulatory
CC protein Ran, converting it to the putatively inactive GDP-bound state.
CC Plays a role in spatial signaling during cell division.
CC {ECO:0000269|PubMed:12061901, ECO:0000269|PubMed:19011093}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with WIP1 through its WPP
CC domain. Component of Ran complexes at least composed of WIT1 or WIT2,
CC RANGAP1 or RANGAP2, and WIP1 or WIP2 or WIP3. Interacts directly with
CC WIT1, WIP2 and WIP3. Interacts with POK1. {ECO:0000250,
CC ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:18591351,
CC ECO:0000269|PubMed:19011093}.
CC -!- INTERACTION:
CC Q9LE82; Q27IK7: KIN12C; NbExp=2; IntAct=EBI-1779351, EBI-6881384;
CC Q9LE82; Q8GXA4: WIP1; NbExp=6; IntAct=EBI-1779351, EBI-1779367;
CC Q9LE82; Q8L7E5: WIT1; NbExp=5; IntAct=EBI-1779351, EBI-1796628;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus envelope
CC {ECO:0000269|PubMed:22270916}. 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 (NE) of interphase cells. Concentrates at the
CC preprophase band (PPB) and remains associated with the cortical
CC division site (CDS) during mitosis and cytokinesis. During mitosis,
CC associates with mitotic spindles at the anaphase. Associated to the
CC microtubular phragmoplast and the surface of the daughter nuclei at the
CC telophase.
CC -!- DOMAIN: The WPP domain is required for the nuclear envelope
CC localization. {ECO:0000269|PubMed:11752475}.
CC -!- SIMILARITY: Belongs to the RNA1 family. {ECO:0000305}.
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DR EMBL; AF214559; AAF25947.1; -; mRNA.
DR EMBL; AL163816; CAB87758.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80438.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80439.1; -; Genomic_DNA.
DR EMBL; AY034918; AAK59425.1; -; mRNA.
DR EMBL; AY150448; AAN12889.1; -; mRNA.
DR PIR; T48102; T48102.
DR RefSeq; NP_001190166.1; NM_001203237.1.
DR RefSeq; NP_191872.1; NM_116178.3.
DR AlphaFoldDB; Q9LE82; -.
DR SMR; Q9LE82; -.
DR BioGRID; 10802; 4.
DR DIP; DIP-46423N; -.
DR IntAct; Q9LE82; 7.
DR STRING; 3702.AT3G63130.2; -.
DR iPTMnet; Q9LE82; -.
DR PaxDb; Q9LE82; -.
DR PRIDE; Q9LE82; -.
DR ProteomicsDB; 234992; -.
DR EnsemblPlants; AT3G63130.1; AT3G63130.1; AT3G63130.
DR EnsemblPlants; AT3G63130.2; AT3G63130.2; AT3G63130.
DR GeneID; 825488; -.
DR Gramene; AT3G63130.1; AT3G63130.1; AT3G63130.
DR Gramene; AT3G63130.2; AT3G63130.2; AT3G63130.
DR KEGG; ath:AT3G63130; -.
DR Araport; AT3G63130; -.
DR TAIR; locus:2099207; AT3G63130.
DR eggNOG; KOG1909; Eukaryota.
DR HOGENOM; CLU_020837_0_0_1; -.
DR InParanoid; Q9LE82; -.
DR OMA; ANQHFDK; -.
DR OrthoDB; 1357476at2759; -.
DR PhylomeDB; Q9LE82; -.
DR PRO; PR:Q9LE82; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LE82; baseline and differential.
DR Genevisible; Q9LE82; AT.
DR GO; GO:0032153; C:cell division site; IDA:TAIR.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR GO; GO:0006606; P:protein import into nucleus; TAS:TAIR.
DR Gene3D; 1.10.246.200; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
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; 4.
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..535
FT /note="RAN GTPase-activating protein 1"
FT /id="PRO_0000347214"
FT REPEAT 208..231
FT /note="LRR 1"
FT REPEAT 236..259
FT /note="LRR 2"
FT REPEAT 264..287
FT /note="LRR 3"
FT REPEAT 320..343
FT /note="LRR 4"
FT REPEAT 353..376
FT /note="LRR 5"
FT REPEAT 377..400
FT /note="LRR 6"
FT REPEAT 405..428
FT /note="LRR 7"
FT REPEAT 433..456
FT /note="LRR 8"
FT REPEAT 461..488
FT /note="LRR 9"
FT REGION 1..115
FT /note="WPP"
FT REGION 493..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..519
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 18..19
FT /note="WP->AA: Loss of nuclear envelope localization."
FT /evidence="ECO:0000269|PubMed:11752475"
SQ SEQUENCE 535 AA; 58827 MW; 06CA71980A007BEB CRC64;
MDHSAKTTQN RVLSVKMWPP SKSTRLMLVE RMTKNITTPS IFSRKYGLLS VEEAEQDAKR
IEDLAFATAN KHFQNEPDGD GTSAVHVYAK ESSKLMLDVI KRGPQEESEV EVSKDGDVFF
DISGGSRAFI EEEEARDLLR PLADPRNSYT KIRFSNRSFG SEAAKFAASV LSSIKDQLTE
VDLSDFVAGR PEAEALEVMN MFSSALEGSK LRYLNLSDNA LGEKGIRAFA SLINSQHDLE
ELYLMNDGIS EDAARAVREL LPSTDKIRVL QFHNNMTGDE GATAIAEIVR ECPSLEDFRC
SSTRIGSEGG VALAEALEHC SHLKKLDLRD NMFGVEGGIA LAKTLSVLTH LTEIYMSYLN
LEDEGTEALS EALLKSAPSL EVLELAGNDI TVKSTGNLAA CIASKQSLAK LNLSENELKD
EGTILIAKAV EGHDQLVEVD LSTNMIRRAG ARALAQTVVK KNTFKLLNIN GNFISEEGID
EVNDMFKDCL DKLVPLDDND PEGEDFEDED EEEEGEDGNE LESKLGSLKI KQGEE
