REN1_ARATH
ID REN1_ARATH Reviewed; 920 AA.
AC F4JQZ3; Q9SB53;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Rho GTPase-activating protein REN1;
DE AltName: Full=Protein ROP1 ENHANCER 1;
DE AltName: Full=Rho-type GTPase-activating protein REN1;
GN Name=REN1; OrderedLocusNames=At4g24580; ORFNames=F22K18.2200;
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 FUNCTION, INTERACTION WITH ARAC11/ROP1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-244.
RX PubMed=19108776; DOI=10.1016/j.cub.2008.11.057;
RA Hwang J.U., Vernoud V., Szumlanski A., Nielsen E., Yang Z.;
RT "A tip-localized RhoGAP controls cell polarity by globally inhibiting Rho
RT GTPase at the cell apex.";
RL Curr. Biol. 18:1907-1916(2008).
CC -!- FUNCTION: Acts as a GTPase activator for the Rac-type GTPase by
CC converting it to an inactive GDP-bound state. Maintains the global
CC inactivation of ARAC11/ROP1 at the apex in pollen tubes in order to
CC regulate the polar cell growth. {ECO:0000269|PubMed:19108776}.
CC -!- SUBUNIT: Interacts with ARAC11/ROP1. {ECO:0000269|PubMed:19108776}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19108776};
CC Peripheral membrane protein {ECO:0000305|PubMed:19108776}.
CC Note=Localizes to the apical plasma membrane and accumulates in the
CC clear zone of growing pollen tubes.
CC -!- TISSUE SPECIFICITY: Expressed in pollen and pollen tubes.
CC {ECO:0000269|PubMed:19108776}.
CC -!- DISRUPTION PHENOTYPE: Male gametophyte defect characterized by sterile
CC pollen grains developing balloon-like tubes.
CC {ECO:0000269|PubMed:19108776}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23005.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79368.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035356; CAA23005.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161561; CAB79368.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84928.2; -; Genomic_DNA.
DR EMBL; CP002687; ANM68131.1; -; Genomic_DNA.
DR PIR; T05576; T05576.
DR RefSeq; NP_001320057.1; NM_001341680.1.
DR RefSeq; NP_001329908.1; NM_001341681.1.
DR AlphaFoldDB; F4JQZ3; -.
DR SMR; F4JQZ3; -.
DR STRING; 3702.AT4G24580.1; -.
DR iPTMnet; F4JQZ3; -.
DR PaxDb; F4JQZ3; -.
DR PRIDE; F4JQZ3; -.
DR ProteomicsDB; 236257; -.
DR EnsemblPlants; AT4G24580.1; AT4G24580.1; AT4G24580.
DR EnsemblPlants; AT4G24580.2; AT4G24580.2; AT4G24580.
DR GeneID; 828560; -.
DR Gramene; AT4G24580.1; AT4G24580.1; AT4G24580.
DR Gramene; AT4G24580.2; AT4G24580.2; AT4G24580.
DR KEGG; ath:AT4G24580; -.
DR Araport; AT4G24580; -.
DR TAIR; locus:2121865; AT4G24580.
DR eggNOG; KOG4271; Eukaryota.
DR HOGENOM; CLU_011283_1_0_1; -.
DR InParanoid; F4JQZ3; -.
DR OMA; DTPHDHK; -.
DR OrthoDB; 209269at2759; -.
DR PRO; PR:F4JQZ3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JQZ3; baseline and differential.
DR Genevisible; F4JQZ3; AT.
DR GO; GO:0045177; C:apical part of cell; IDA:TAIR.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IDA:TAIR.
DR GO; GO:0070382; C:exocytic vesicle; IDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:TAIR.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:TAIR.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0009865; P:pollen tube adhesion; IMP:TAIR.
DR GO; GO:0048868; P:pollen tube development; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR025757; MIP1_Leuzipper.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF14389; Lzipper-MIP1; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Growth regulation; GTPase activation; Membrane;
KW Reference proteome.
FT CHAIN 1..920
FT /note="Rho GTPase-activating protein REN1"
FT /id="PRO_0000422723"
FT DOMAIN 60..167
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 213..412
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 598..728
FT /evidence="ECO:0000255"
FT COMPBIAS 430..465
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 244
FT /note="R->L: Loss of function as activator."
FT /evidence="ECO:0000269|PubMed:19108776"
SQ 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
