ABP1_ARATH
ID ABP1_ARATH Reviewed; 198 AA.
AC P33487; Q8LBB3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Auxin-binding protein 1 {ECO:0000303|PubMed:7517789};
DE Short=ABP1 {ECO:0000303|PubMed:7517789};
DE Flags: Precursor;
GN Name=ERABP1 {ECO:0000303|PubMed:7517789};
GN OrderedLocusNames=At4g02980 {ECO:0000312|Araport:AT4G02980};
GN ORFNames=T4I9.14 {ECO:0000312|EMBL:AAC79108.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=7517789;
RA Shimomura S., Liu W., Inohara N., Watanabe S., Futai M.;
RT "Structure of the gene for an auxin-binding protein and a gene for 7SL RNA
RT from Arabidopsis thaliana.";
RL Plant Cell Physiol. 34:633-637(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 34-68.
RX PubMed=1321684; DOI=10.2307/3869572;
RA Palme K., Hesse T., Campos N., Garbers C., Yanofsky M.F., Schell J.;
RT "Molecular analysis of an auxin binding protein gene located on chromosome
RT 4 of Arabidopsis.";
RL Plant Cell 4:193-201(1992).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=9804548; DOI=10.1126/science.282.5391.1114;
RA Jones A.M., Im K.H., Savka M.A., Wu M.J., DeWitt N.G., Shillito R.,
RA Binns A.N.;
RT "Auxin-dependent cell expansion mediated by overexpressed auxin-binding
RT protein 1.";
RL Science 282:1114-1117(1998).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11297513; DOI=10.1101/gad.866201;
RA Chen J.G., Ullah H., Young J.C., Sussman M.R., Jones A.M.;
RT "ABP1 is required for organized cell elongation and division in Arabidopsis
RT embryogenesis.";
RL Genes Dev. 15:902-911(2001).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SKU5.
RX PubMed=16649105; DOI=10.1007/s11103-005-5471-1;
RA Shimomura S.;
RT "Identification of a glycosylphosphatidylinositol-anchored plasma membrane
RT protein interacting with the C-terminus of auxin-binding protein 1: a
RT photoaffinity crosslinking study.";
RL Plant Mol. Biol. 60:663-677(2006).
RN [10]
RP FUNCTION.
RX PubMed=18952781; DOI=10.1105/tpc.108.059048;
RA Braun N., Wyrzykowska J., Muller P., David K., Couch D.,
RA Perrot-Rechenmann C., Fleming A.J.;
RT "Conditional repression of AUXIN BINDING PROTEIN1 reveals that it
RT coordinates cell division and cell expansion during postembryonic shoot
RT development in Arabidopsis and tobacco.";
RL Plant Cell 20:2746-2762(2008).
RN [11]
RP FUNCTION.
RX PubMed=19777056; DOI=10.1371/journal.pone.0006648;
RA Tromas A., Braun N., Muller P., Khodus T., Paponov I.A., Palme K.,
RA Ljung K., Lee J.Y., Benfey P., Murray J.A., Scheres B.,
RA Perrot-Rechenmann C.;
RT "The AUXIN BINDING PROTEIN 1 is required for differential auxin responses
RT mediating root growth.";
RL PLoS ONE 4:E6648-E6648(2009).
RN [12]
RP UBIQUITINATION BY RMA2.
RX PubMed=20152813; DOI=10.1016/j.bbrc.2010.02.032;
RA Son O., Cho S.K., Kim S.J., Kim W.T.;
RT "In vitro and in vivo interaction of AtRma2 E3 ubiquitin ligase and auxin-
RT binding protein 1.";
RL Biochem. Biophys. Res. Commun. 393:492-497(2010).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF HIS-92.
RX PubMed=20887895; DOI=10.1016/j.cell.2010.09.003;
RA Xu T., Wen M., Nagawa S., Fu Y., Chen J.G., Wu M.J., Perrot-Rechenmann C.,
RA Friml J., Jones A.M., Yang Z.;
RT "Cell surface- and rho GTPase-based auxin signaling controls cellular
RT interdigitation in Arabidopsis.";
RL Cell 143:99-110(2010).
RN [14]
RP FUNCTION.
RX PubMed=20887896; DOI=10.1016/j.cell.2010.09.027;
RA Robert S., Kleine-Vehn J., Barbez E., Sauer M., Paciorek T., Baster P.,
RA Vanneste S., Zhang J., Simon S., Covanova M., Hayashi K., Dhonukshe P.,
RA Yang Z., Bednarek S.Y., Jones A.M., Luschnig C., Aniento F., Zazimalova E.,
RA Friml J.;
RT "ABP1 mediates auxin inhibition of clathrin-dependent endocytosis in
RT Arabidopsis.";
RL Cell 143:111-121(2010).
RN [15]
RP FUNCTION, AND INDUCTION BY AUXIN.
RX PubMed=21223392; DOI=10.1111/j.1365-313x.2010.04420.x;
RA Effendi Y., Rietz S., Fischer U., Scherer G.F.;
RT "The heterozygous abp1/ABP1 insertional mutant has defects in functions
RT requiring polar auxin transport and in regulation of early auxin-regulated
RT genes.";
RL Plant J. 65:282-294(2011).
RN [16]
RP REVIEW.
RX PubMed=21822062; DOI=10.4161/psb.6.8.16403;
RA Effendi Y., Scherer G.F.;
RT "Auxin binding-protein1 (ABP1), a receptor to regulate auxin transport and
RT early auxin genes in an interlocking system with PIN proteins and the
RT receptor TIR1.";
RL Plant Signal. Behav. 6:1101-1103(2011).
RN [17]
RP FUNCTION.
RX PubMed=22683261; DOI=10.1016/j.cub.2012.05.020;
RA Chen X., Naramoto S., Robert S., Tejos R., Loefke C., Lin D., Yang Z.,
RA Friml J.;
RT "ABP1 and ROP6 GTPase signaling regulate clathrin-mediated endocytosis in
RT Arabidopsis roots.";
RL Curr. Biol. 22:1326-1332(2012).
RN [18]
RP FUNCTION.
RX PubMed=24052532; DOI=10.1093/jxb/ert294;
RA Effendi Y., Jones A.M., Scherer G.F.;
RT "AUXIN-BINDING-PROTEIN1 (ABP1) in phytochrome-B-controlled responses.";
RL J. Exp. Bot. 64:5065-5074(2013).
RN [19]
RP FUNCTION.
RX PubMed=24051655; DOI=10.1038/ncomms3496;
RA Tromas A., Paque S., Stierle V., Quettier A.L., Muller P., Lechner E.,
RA Genschik P., Perrot-Rechenmann C.;
RT "Auxin-binding protein 1 is a negative regulator of the SCF(TIR1/AFB)
RT pathway.";
RL Nat. Commun. 4:2496-2496(2013).
RN [20]
RP FUNCTION.
RX PubMed=25409144; DOI=10.1038/nature13889;
RA Chen X., Grandont L., Li H., Hauschild R., Paque S., Abuzeineh A.,
RA Rakusova H., Benkova E., Perrot-Rechenmann C., Friml J.;
RT "Inhibition of cell expansion by rapid ABP1-mediated auxin effect on
RT microtubules.";
RL Nature 516:90-93(2014).
RN [21]
RP FUNCTION.
RX PubMed=24424095; DOI=10.1105/tpc.113.120048;
RA Paque S., Mouille G., Grandont L., Alabadi D., Gaertner C., Goyallon A.,
RA Muller P., Primard-Brisset C., Sormani R., Blazquez M.A.,
RA Perrot-Rechenmann C.;
RT "AUXIN BINDING PROTEIN1 links cell wall remodeling, auxin signaling, and
RT cell expansion in arabidopsis.";
RL Plant Cell 26:280-295(2014).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TMK1, AND MUTAGENESIS OF
RP HIS-92.
RX PubMed=24578577; DOI=10.1126/science.1245125;
RA Xu T., Dai N., Chen J., Nagawa S., Cao M., Li H., Zhou Z., Chen X.,
RA De Rycke R., Rakusova H., Wang W., Jones A.M., Friml J., Patterson S.E.,
RA Bleecker A.B., Yang Z.;
RT "Cell surface ABP1-TMK auxin-sensing complex activates ROP GTPase
RT signaling.";
RL Science 343:1025-1028(2014).
RN [23]
RP FUNCTION, AND MUTAGENESIS OF LEU-60; THR-89 AND HIS-141.
RC STRAIN=cv. Wassilewskija;
RX PubMed=25392478; DOI=10.1093/jxb/eru433;
RA Effendi Y., Ferro N., Labusch C., Geisler M., Scherer G.F.;
RT "Complementation of the embryo-lethal T-DNA insertion mutant of AUXIN-
RT BINDING-PROTEIN 1 (ABP1) with abp1 point mutated versions reveals crosstalk
RT of ABP1 and phytochromes.";
RL J. Exp. Bot. 66:403-418(2015).
RN [24]
RP DISRUPTION PHENOTYPE.
RX PubMed=25646447; DOI=10.1073/pnas.1500365112;
RA Gao Y., Zhang Y., Zhang D., Dai X., Estelle M., Zhao Y.;
RT "Auxin binding protein 1 (ABP1) is not required for either auxin signaling
RT or Arabidopsis development.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:2275-2280(2015).
RN [25]
RP REVIEW.
RX PubMed=25556248; DOI=10.1242/jcs.159418;
RA Grones P., Friml J.;
RT "Auxin transporters and binding proteins at a glance.";
RL J. Cell Sci. 128:1-7(2015).
RN [26]
RP FUNCTION, AND MUTAGENESIS OF ARG-57; LEU-60; GLN-81; THR-89; PRO-90;
RP HIS-92; HIS-94; VAL-99; PHE-125; PRO-136; PHE-181; TRP-185 AND GLN-188.
RC STRAIN=cv. Columbia;
RX PubMed=25922490; DOI=10.1093/jxb/erv177;
RA Grones P., Chen X., Simon S., Kaufmann W.A., De Rycke R., Nodzynski T.,
RA Zazimalova E., Friml J.;
RT "Auxin-binding pocket of ABP1 is crucial for its gain-of-function cellular
RT and developmental roles.";
RL J. Exp. Bot. 66:5055-5065(2015).
CC -!- FUNCTION: Auxin receptor that controls cell elongation and cell
CC division (PubMed:9804548, PubMed:11297513). Involved in embryonic
CC morphogenesis (PubMed:11297513). Acts on the cell cycle, endocycle,
CC cell plate formation, and cell expansion and contributes to the control
CC of auxin-related gene expression (PubMed:18952781). Controls root
CC meristem size and mediates auxin responsiveness (PubMed:19777056).
CC Involved in activation of ROP GTPases in response to auxin and
CC regulation of clathrin-mediated endocytosis in roots (PubMed:20887895,
CC PubMed:22683261). Acts as a positive factor in clathrin recruitment to
CC the plasma membrane, thereby promoting endocytosis (PubMed:20887896,
CC PubMed:25922490). Upon auxin binding, restricts the internalization of
CC PIN proteins by inhibiting clathrin-mediated endocytosis
CC (PubMed:20887896, PubMed:25922490). Involved in the regulation of polar
CC auxin transport (PubMed:21223392). Behaves as a negative regulator of
CC the SCF(TIR1/AFB) signaling pathway, protecting AUX/IAA repressors from
CC degradation (PubMed:24051655). Regulates the expression of cell wall
CC remodeling genes via an SCF(TIR1/AFB)-dependent pathway
CC (PubMed:24424095). Involved in the modulation of hemicellulose
CC xyloglucan structure (PubMed:24424095). Required for rapid auxin-
CC mediated re-orientation of microtubules to regulate cell elongation in
CC roots and dark-grown hypocotyls as well as asymmetric growth during
CC gravitropic responses (PubMed:25409144). Involved in the shade
CC avoidance response (PubMed:24052532). Forms with TMK1 a cell surface
CC auxin perception complex that activates ROP signaling pathways
CC (PubMed:24578577). ABP1 sensing of auxin is important for the ABP1-TMK1
CC complex formation (PubMed:24578577). Interacts functionally with
CC phytochrome to regulate growth (PubMed:25392478).
CC {ECO:0000269|PubMed:11297513, ECO:0000269|PubMed:18952781,
CC ECO:0000269|PubMed:19777056, ECO:0000269|PubMed:20887895,
CC ECO:0000269|PubMed:20887896, ECO:0000269|PubMed:21223392,
CC ECO:0000269|PubMed:22683261, ECO:0000269|PubMed:24051655,
CC ECO:0000269|PubMed:24052532, ECO:0000269|PubMed:24424095,
CC ECO:0000269|PubMed:24578577, ECO:0000269|PubMed:25392478,
CC ECO:0000269|PubMed:25409144, ECO:0000269|PubMed:25922490,
CC ECO:0000269|PubMed:9804548}.
CC -!- SUBUNIT: Homodimer (By similarity). May interact with the GPI-anchored
CC plasma membrane protein SKU5 and its family members (PubMed:16649105).
CC Interacts with TMK1 (via extracellular domain) (PubMed:24578577).
CC {ECO:0000250|UniProtKB:P13689, ECO:0000269|PubMed:24578577,
CC ECO:0000303|PubMed:16649105}.
CC -!- INTERACTION:
CC P33487; P43298: TMK1; NbExp=3; IntAct=EBI-16094614, EBI-2023970;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:24578577, ECO:0000305|PubMed:7517789}. Cell
CC membrane {ECO:0000269|PubMed:24578577, ECO:0000303|PubMed:16649105};
CC Peripheral membrane protein {ECO:0000303|PubMed:16649105}. Note=In
CC plasmolyzed cells, observed in strands connecting the apoplast and the
CC plasma membrane. {ECO:0000269|PubMed:24578577}.
CC -!- INDUCTION: Up-regulated by auxin. {ECO:0000269|PubMed:21223392}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P13689}.
CC -!- PTM: Ubiquitinated by RMA2, leading to proteasomal degradation.
CC {ECO:0000269|PubMed:20152813}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality, when homozygous
CC (PubMed:11297513). No visible phenotype was found for other null
CC mutants (PubMed:25646447). {ECO:0000269|PubMed:11297513,
CC ECO:0000269|PubMed:25646447}.
CC -!- CAUTION: Analysis of new null mutants leads to the conclusion that
CC plants do not need ABP1 for auxin signaling and for their growth and
CC development under normal growth conditions.
CC {ECO:0000269|PubMed:25646447}.
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DR EMBL; X55111; CAA38909.1; -; Genomic_DNA.
DR EMBL; X69901; CAA49526.1; -; Genomic_DNA.
DR EMBL; S40550; AAB22612.1; -; mRNA.
DR EMBL; AF069442; AAC79108.1; -; Genomic_DNA.
DR EMBL; AL161495; CAB77783.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82256.1; -; Genomic_DNA.
DR EMBL; AF389278; AAK63851.1; -; mRNA.
DR EMBL; AY093754; AAM10378.1; -; mRNA.
DR EMBL; AY087315; AAM64865.1; -; mRNA.
DR PIR; S31584; S31584.
DR RefSeq; NP_192207.1; NM_116532.3.
DR AlphaFoldDB; P33487; -.
DR SMR; P33487; -.
DR BioGRID; 13409; 1.
DR DIP; DIP-61369N; -.
DR IntAct; P33487; 1.
DR STRING; 3702.AT4G02980.1; -.
DR PaxDb; P33487; -.
DR PRIDE; P33487; -.
DR ProteomicsDB; 244521; -.
DR EnsemblPlants; AT4G02980.1; AT4G02980.1; AT4G02980.
DR GeneID; 828120; -.
DR Gramene; AT4G02980.1; AT4G02980.1; AT4G02980.
DR KEGG; ath:AT4G02980; -.
DR Araport; AT4G02980; -.
DR TAIR; locus:2005491; AT4G02980.
DR eggNOG; ENOG502RXJU; Eukaryota.
DR HOGENOM; CLU_092214_1_0_1; -.
DR InParanoid; P33487; -.
DR OMA; VFIYEDW; -.
DR OrthoDB; 1374533at2759; -.
DR PhylomeDB; P33487; -.
DR PRO; PR:P33487; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P33487; baseline and differential.
DR Genevisible; P33487; AT.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010011; F:auxin binding; IMP:TAIR.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:TAIR.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:TAIR.
DR GO; GO:0032877; P:positive regulation of DNA endoreduplication; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR000526; Auxin-bd.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR37236; PTHR37236; 1.
DR Pfam; PF02041; Auxin_BP; 1.
DR PRINTS; PR00655; AUXINBINDNGP.
DR SUPFAM; SSF51182; SSF51182; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Auxin signaling pathway; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Metal-binding; Receptor; Reference proteome; Signal; Ubl conjugation; Zinc.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:1321684"
FT CHAIN 34..198
FT /note="Auxin-binding protein 1"
FT /id="PRO_0000020613"
FT MOTIF 195..198
FT /note="Prevents secretion from ER"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P13689"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P13689"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P13689"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P13689"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P13689"
FT DISULFID 36..189
FT /evidence="ECO:0000250|UniProtKB:P13689"
FT MUTAGEN 57
FT /note="R->K: Slight reduction of activation by auxin.
FT Slight reduction of activation by auxin; when associated
FT with V-60."
FT /evidence="ECO:0000269|PubMed:25922490"
FT MUTAGEN 60
FT /note="L->V: Slight reduction of activation by auxin.
FT Slight reduction of activation by auxin; when associated
FT with K-57."
FT /evidence="ECO:0000269|PubMed:25922490"
FT MUTAGEN 60
FT /note="L->Y: In abp1-9; lower auxin sensitivity and altered
FT responses to continuous light and shade."
FT /evidence="ECO:0000269|PubMed:25392478"
FT MUTAGEN 81
FT /note="Q->D: Slight reduction of activation by auxin."
FT /evidence="ECO:0000269|PubMed:25922490"
FT MUTAGEN 89
FT /note="T->I: In abp1-8; lower auxin sensitivity and altered
FT responses to continuous light and shade."
FT /evidence="ECO:0000269|PubMed:25392478"
FT MUTAGEN 89
FT /note="T->V: Slight reduction of activation by auxin.
FT Slight reduction of activation by auxin; when associated
FT with L-90."
FT /evidence="ECO:0000269|PubMed:25922490"
FT MUTAGEN 90
FT /note="P->L: Slight reduction of activation by auxin.
FT Slight reduction of activation by auxin; when associated
FT with V-89."
FT /evidence="ECO:0000269|PubMed:25922490"
FT MUTAGEN 92
FT /note="H->A: In ABP-M1X; Strong reduction of activation by
FT auxin. In ABP-M2X; strong reduction of activation by auxin;
FT when associated with A-94."
FT /evidence="ECO:0000269|PubMed:25922490"
FT MUTAGEN 92
FT /note="H->Y: In abp1-5; defects in pavement cells
FT interdigitation and decreased interaction with TMK1."
FT /evidence="ECO:0000269|PubMed:20887895,
FT ECO:0000269|PubMed:24578577"
FT MUTAGEN 94
FT /note="H->A: In ABP-M2X; strong reduction of activation by
FT auxin; when associated with A-92."
FT /evidence="ECO:0000269|PubMed:25922490"
FT MUTAGEN 99
FT /note="V->A: No effect on activation by auxin."
FT /evidence="ECO:0000269|PubMed:25922490"
FT MUTAGEN 125
FT /note="F->L: No effect on activation by auxin."
FT /evidence="ECO:0000269|PubMed:25922490"
FT MUTAGEN 136
FT /note="P->L: No effect on activation by auxin."
FT /evidence="ECO:0000269|PubMed:25922490"
FT MUTAGEN 141
FT /note="H->N: In abp1-10; lower auxin sensitivity and
FT altered responses to continuous light and shade."
FT /evidence="ECO:0000269|PubMed:25392478"
FT MUTAGEN 181
FT /note="F->L: Slight reduction of activation by auxin.
FT Slight reduction of activation by auxin; when associated
FT with Y-185."
FT /evidence="ECO:0000269|PubMed:25922490"
FT MUTAGEN 185
FT /note="W->Y: Slight reduction of activation by auxin.
FT Slight reduction of activation by auxin; when associated
FT with L-181."
FT /evidence="ECO:0000269|PubMed:25922490"
FT MUTAGEN 188
FT /note="Q->D: No effect on activation by auxin."
FT /evidence="ECO:0000269|PubMed:25922490"
FT CONFLICT 102
FT /note="V -> L (in Ref. 6; AAM64865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 22044 MW; 43440CFDCE9EFD67 CRC64;
MIVLSVGSAS SSPIVVVFSV ALLLFYFSET SLGAPCPING LPIVRNISDL PQDNYGRPGL
SHMTVAGSVL HGMKEVEIWL QTFAPGSETP IHRHSCEEVF VVLKGSGTLY LAETHGNFPG
KPIEFPIFAN STIHIPINDA HQVKNTGHED LQVLVIISRP PIKIFIYEDW FMPHTAARLK
FPYYWDEQCI QESQKDEL
