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Rho GTPase-activating protein REN1 (Protein ROP1 ENHANCER 1) (Rho-type GTPase-activating protein REN1)

 REN1_ARATH              Reviewed;         920 AA.
F4JQZ3; Q9SB53;
26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
26-JUN-2013, sequence version 2.
25-OCT-2017, entry version 48.
RecName: Full=Rho GTPase-activating protein REN1;
AltName: Full=Protein ROP1 ENHANCER 1;
AltName: Full=Rho-type GTPase-activating protein REN1;
Name=REN1; OrderedLocusNames=At4g24580; ORFNames=F22K18.2200;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, INTERACTION WITH ARAC11/ROP1, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-244.
PubMed=19108776; DOI=10.1016/j.cub.2008.11.057;
Hwang J.U., Vernoud V., Szumlanski A., Nielsen E., Yang Z.;
"A tip-localized RhoGAP controls cell polarity by globally inhibiting
Rho GTPase at the cell apex.";
Curr. Biol. 18:1907-1916(2008).
-!- FUNCTION: Acts as a GTPase activator for the Rac-type GTPase by
converting it to an inactive GDP-bound state. Maintains the global
inactivation of ARAC11/ROP1 at the apex in pollen tubes in order
to regulate the polar cell growth. {ECO:0000269|PubMed:19108776}.
-!- SUBUNIT: Interacts with ARAC11/ROP1.
{ECO:0000269|PubMed:19108776}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19108776};
Peripheral membrane protein {ECO:0000305|PubMed:19108776}.
Note=Localizes to the apical plasma membrane and accumulates in
the clear zone of growing pollen tubes.
-!- TISSUE SPECIFICITY: Expressed in pollen and pollen tubes.
{ECO:0000269|PubMed:19108776}.
-!- DISRUPTION PHENOTYPE: Male gametophyte defect characterized by
sterile pollen grains developing balloon-like tubes.
{ECO:0000269|PubMed:19108776}.
-!- SEQUENCE CAUTION:
Sequence=CAA23005.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB79368.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL035356; CAA23005.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161561; CAB79368.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE84928.2; -; Genomic_DNA.
EMBL; CP002687; ANM68131.1; -; Genomic_DNA.
PIR; T05576; T05576.
RefSeq; NP_001320057.1; NM_001341680.1.
RefSeq; NP_001329908.1; NM_001341681.1.
ProteinModelPortal; F4JQZ3; -.
SMR; F4JQZ3; -.
STRING; 3702.AT4G24580.1; -.
iPTMnet; F4JQZ3; -.
PaxDb; F4JQZ3; -.
EnsemblPlants; AT4G24580.1; AT4G24580.1; AT4G24580.
EnsemblPlants; AT4G24580.2; AT4G24580.2; AT4G24580.
GeneID; 828560; -.
Gramene; AT4G24580.1; AT4G24580.1; AT4G24580.
Gramene; AT4G24580.2; AT4G24580.2; AT4G24580.
KEGG; ath:AT4G24580; -.
Araport; AT4G24580; -.
TAIR; locus:2121865; AT4G24580.
eggNOG; KOG4271; Eukaryota.
eggNOG; ENOG410XR4E; LUCA.
InParanoid; F4JQZ3; -.
OrthoDB; EOG093608J2; -.
PRO; PR:F4JQZ3; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; F4JQZ3; baseline and differential.
Genevisible; F4JQZ3; AT.
GO; GO:0045177; C:apical part of cell; IDA:TAIR.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IDA:TAIR.
GO; GO:0070382; C:exocytic vesicle; IDA:TAIR.
GO; GO:0090406; C:pollen tube; IDA:TAIR.
GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
GO; GO:0017048; F:Rho GTPase binding; IPI:UniProtKB.
GO; GO:0090630; P:activation of GTPase activity; IDA:TAIR.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:TAIR.
GO; GO:0009846; P:pollen germination; IMP:TAIR.
GO; GO:0009865; P:pollen tube adhesion; IMP:TAIR.
GO; GO:0048868; P:pollen tube development; IMP:TAIR.
GO; GO:0009860; P:pollen tube growth; IMP:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR025757; MIP1_Leuzipper.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
Pfam; PF14389; Lzipper-MIP1; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00620; RhoGAP; 1.
SMART; SM00233; PH; 1.
SMART; SM00324; RhoGAP; 1.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50238; RHOGAP; 1.
1: Evidence at protein level;
Cell membrane; Coiled coil; Complete proteome; Growth regulation;
GTPase activation; Membrane; Reference proteome.
CHAIN 1 920 Rho GTPase-activating protein REN1.
/FTId=PRO_0000422723.
DOMAIN 60 167 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 213 412 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
COILED 598 728 {ECO:0000255}.
COMPBIAS 20 25 Poly-Gln.
COMPBIAS 442 446 Poly-Asp.
MUTAGEN 244 244 R->L: Loss of function as activator.
{ECO:0000269|PubMed:19108776}.
SEQUENCE 920 AA; 100627 MW; 05EF5B8A09387208 CRC64;
MANKNAESSS QPPPHVQPNQ QQQQQPPIAN EQEQEPHGDT CSIPPAQSGN TDSRSRGGNT
VFKSGPLSIS SKGIGWTSWK KRWFILTRTS LVFFRSDPSA VQQKGSEVNL TLGGIDLNNS
GSVVVKADKK LLTVLFPDGR DGRAFTLKAD TMEDLHEWKA ALENALTQAP SASHVMGQNG
IFRNDHADPA VGVDEKKDET PTKSTVLGRP VLLALEDVDG APSFLEKALR FVENHGVRIE
GILRQAADVD DVEHRIREYE KGKNEFSPEE DAHIIADCLK YFLRELPSSP VPASCCNALL
EACRTDRGNR VNAMRAAICE SFPEPNRRLL QRILMMMQTV ASNKTVNRMN TNAVAACMAP
LLLRPLLAGD CEIENDFDVG GDGSMQLLQA AAAANHAQAI VITLLEEYES IFGEGSLSPG
LYSDSEESGS GTEEGSDDEE YDDDDDGSQG SEDYTDEEED LENESNGSYS ESAASEDKYA
DSIDPDDHKI NDNLSTESKS PKRSKEPKKL LSGSRRSSLP RHDDGKKDED IVVKGVNNTE
VKAVVEVSTS EDKNSSTSDV ASDTQKPSKL SDAPGGSKRH WGRTPGKKNL SMESIDFSVE
VDEDNADIER LESTKLELQS RITEEVKSNA VLQASLERRK KALYGRRQAL EQDVGRLQEQ
LQQERDRKLA LETGLNMSKG NQPIPETIDE NLKKDLQEVA QAEADIAKLE HKVDDLENRL
GHHDGKASGS THSASKESRK LPEHNAKMKE KQKDTEAAST HISERSTSKD GQGAARENET
EKQQDSRSKS SQQETSRGSS KLVGLSKRSG TKGEGSTTTT SALSKLTMRL NFLKERRSQI
ANELQNMDKG KTLGQPSPTS GQNRVSEETE KGSGSNQDPD SSKLQSPHIL DRGRSENGGD
RGRGSSGGNH PNTTPRTFSR


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