ID ARFB_ARATH Reviewed; 859 AA. AC Q94JM3; O23671; Q56YL7; Q56YP4; Q56YR7; Q9C5W5; Q9FIT6; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 13-APR-2004, sequence version 2. DT 24-JAN-2024, entry version 158. DE RecName: Full=Auxin response factor 2; DE AltName: Full=ARF1-binding protein; DE Short=ARF1-BP; DE AltName: Full=Protein MEGAINTEGUMENTA; GN Name=ARF2; Synonyms=MNT; OrderedLocusNames=At5g62000; ORFNames=MTG10.3; 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]. RC STRAIN=cv. Columbia; RX PubMed=15659631; DOI=10.1105/tpc.104.028316; RA Okushima Y., Overvoorde P.J., Arima K., Alonso J.M., Chan A., Chang C., RA Ecker J.R., Hughes B., Lui A., Nguyen D., Onodera C., Quach H., Smith A., RA Yu G., Theologis A.; RT "Functional genomic analysis of the AUXIN RESPONSE FACTOR gene family RT members in Arabidopsis thaliana: unique and overlapping functions of ARF7 RT and ARF19."; RL Plant Cell 17:444-463(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=9872454; DOI=10.1093/dnares/5.5.297; RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence RT features of the regions of 1,013,767 bp covered by sixteen physically RT assigned P1 and TAC clones."; RL DNA Res. 5:297-308(1998). 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 394-859. RC STRAIN=cv. Columbia; RX PubMed=9188533; DOI=10.1126/science.276.5320.1865; RA Ulmasov T., Hagen G., Guilfoyle T.J.; RT "ARF1, a transcription factor that binds to auxin response elements."; RL Science 276:1865-1868(1997). RN [7] RP NUCLEOTIDE SEQUENCE OF 406-859. RC STRAIN=cv. Columbia; RA Sessa G., Carabelli M., Ciarbelli A.R., Ruzza V., Steindler C., Ruberti I.; RT "Nucleotide sequence of the Arabidopsis IAA30."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [8] RP DIMERIZATION, AND TISSUE SPECIFICITY. RX PubMed=10476078; DOI=10.1046/j.1365-313x.1999.00538.x; RA Ulmasov T., Hagen G., Guilfoyle T.J.; RT "Dimerization and DNA binding of auxin response factors."; RL Plant J. 19:309-319(1999). RN [9] RP GENE FAMILY, NOMENCLATURE, AND FUNCTION. RX PubMed=12036261; DOI=10.1023/a:1015207114117; RA Hagen G., Guilfoyle T.J.; RT "Auxin-responsive gene expression: genes, promoters and regulatory RT factors."; RL Plant Mol. Biol. 49:373-385(2002). RN [10] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=16176952; DOI=10.1242/dev.02012; RA Ellis C.M., Nagpal P., Young J.C., Hagen G., Guilfoyle T.J., Reed J.W.; RT "AUXIN RESPONSE FACTOR1 and AUXIN RESPONSE FACTOR2 regulate senescence and RT floral organ abscission in Arabidopsis thaliana."; RL Development 132:4563-4574(2005). RN [11] RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION RP PHENOTYPE. RX PubMed=15960614; DOI=10.1111/j.1365-313x.2005.02426.x; RA Okushima Y., Mitina I., Quach H.L., Theologis A.; RT "AUXIN RESPONSE FACTOR 2 (ARF2): a pleiotropic developmental regulator."; RL Plant J. 43:29-46(2005). RN [12] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=16339187; DOI=10.1242/dev.02194; RA Schruff M.C., Spielman M., Tiwari S., Adams S., Fenby N., Scott R.J.; RT "The AUXIN RESPONSE FACTOR 2 gene of Arabidopsis links auxin signalling, RT cell division, and the size of seeds and other organs."; RL Development 133:251-261(2006). RN [13] RP GENE FAMILY. RX PubMed=18986826; DOI=10.1016/j.tplants.2008.09.006; RA Swaminathan K., Peterson K., Jack T.; RT "The plant B3 superfamily."; RL Trends Plant Sci. 13:647-655(2008). CC -!- FUNCTION: Auxin response factors (ARFs) are transcriptional factors CC that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the CC auxin-responsive promoter elements (AuxREs). Could act as CC transcriptional activator or repressor. Formation of heterodimers with CC Aux/IAA proteins may alter their ability to modulate early auxin CC response genes expression. Promotes flowering, stamen development, CC floral organ abscission and fruit dehiscence. Functions independently CC of ethylene and cytokinin response pathways. May act as a repressor of CC cell division and organ growth. {ECO:0000269|PubMed:12036261, CC ECO:0000269|PubMed:15960614, ECO:0000269|PubMed:16176952, CC ECO:0000269|PubMed:16339187}. CC -!- SUBUNIT: Homodimers and heterodimers. Interacts with ARF1. CC -!- INTERACTION: CC Q94JM3; Q8L7G0: ARF1; NbExp=4; IntAct=EBI-1799262, EBI-2324259; CC Q94JM3; Q39011: ASK7; NbExp=6; IntAct=EBI-1799262, EBI-1798250; CC Q94JM3; Q38828: IAA10; NbExp=6; IntAct=EBI-1799262, EBI-3946434; CC Q94JM3; P93830: IAA17; NbExp=3; IntAct=EBI-1799262, EBI-632243; CC Q94JM3; O24408: IAA18; NbExp=3; IntAct=EBI-1799262, EBI-2295525; CC Q94JM3; Q8LAL2: IAA26; NbExp=7; IntAct=EBI-1799262, EBI-3947418; CC Q94JM3; Q93WC4: IAA29; NbExp=6; IntAct=EBI-1799262, EBI-3946697; CC Q94JM3; Q8RYC6: IAA32; NbExp=6; IntAct=EBI-1799262, EBI-3946448; CC Q94JM3; Q9FKM7: IAA33; NbExp=3; IntAct=EBI-1799262, EBI-3946739; CC Q94JM3; Q9C5X0: IAA34; NbExp=6; IntAct=EBI-1799262, EBI-3946459; CC Q94JM3; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-1799262, EBI-15192297; CC Q94JM3; Q8GWF1: WRKY38; NbExp=3; IntAct=EBI-1799262, EBI-1993263; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=Q94JM3-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: Expressed in the whole plant. CC {ECO:0000269|PubMed:10476078, ECO:0000269|PubMed:15960614}. CC -!- DEVELOPMENTAL STAGE: Expressed in the sepals and carpels of young CC flower buds. At stage 10 of flower development, expression in the CC carpels becomes restricted to the style. Also expressed in anthers and CC filaments. At stage 13, expressed in the region at the top of the CC pedicel, including the abscission zone. Expressed in developing CC siliques. {ECO:0000269|PubMed:15960614, ECO:0000269|PubMed:16176952}. CC -!- DOMAIN: Interactions between auxin response factors (ARFs) and Aux/IAA CC proteins occur through their C-terminal dimerization domains III and CC IV. CC -!- DISRUPTION PHENOTYPE: Large, dark green rosette leaves, delayed CC flowering, thick and long inflorescence, abnormal flower morphology and CC sterility in early formed flowers, but fertility in late-formed CC flowers. Delayed senescence and abscission. Increased seed size and CC weight, and extra cell division and expansion in many organs. CC {ECO:0000269|PubMed:15960614, ECO:0000269|PubMed:16339187}. CC -!- SIMILARITY: Belongs to the ARF family. {ECO:0000305}. CC -!- CAUTION: Was originally erroneously termed IAA26 and IAA30 (Ref.5). CC {ECO:0000305|Ref.5}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC49752.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAK55665.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAN46837.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAD29696.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAD30210.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY669787; AAT67071.1; -; mRNA. DR EMBL; AB016880; BAB10162.1; -; Genomic_DNA. DR EMBL; CP002688; AED97548.1; -; Genomic_DNA. DR EMBL; CP002688; AED97549.1; -; Genomic_DNA. DR EMBL; CP002688; AED97550.1; -; Genomic_DNA. DR EMBL; CP002688; ANM68885.1; -; Genomic_DNA. DR EMBL; AF336918; AAG53999.1; -; mRNA. DR EMBL; AF378862; AAK55665.1; ALT_FRAME; mRNA. DR EMBL; BT000784; AAN31923.1; -; mRNA. DR EMBL; BT001072; AAN46837.1; ALT_FRAME; mRNA. DR EMBL; AK221252; BAD93891.1; -; mRNA. DR EMBL; AK221254; BAD93897.1; -; mRNA. DR EMBL; AK221274; BAD93959.1; -; mRNA. DR EMBL; AK221277; BAD93968.1; -; mRNA. DR EMBL; AK221282; BAD93985.1; -; mRNA. DR EMBL; AK221305; BAD94058.1; -; mRNA. DR EMBL; U89771; AAC49752.1; ALT_INIT; mRNA. DR EMBL; AJ441313; CAD29696.1; ALT_INIT; mRNA. DR EMBL; AJ458328; CAD30210.1; ALT_INIT; mRNA. DR RefSeq; NP_001330603.1; NM_001345519.1. [Q94JM3-1] DR RefSeq; NP_201006.2; NM_125593.5. [Q94JM3-1] DR RefSeq; NP_851244.1; NM_180913.4. [Q94JM3-1] DR RefSeq; NP_974980.1; NM_203251.4. [Q94JM3-1] DR AlphaFoldDB; Q94JM3; -. DR SMR; Q94JM3; -. DR BioGRID; 21565; 30. DR DIP; DIP-46014N; -. DR IntAct; Q94JM3; 20. DR STRING; 3702.Q94JM3; -. DR iPTMnet; Q94JM3; -. DR PaxDb; 3702-AT5G62000-1; -. DR ProteomicsDB; 246955; -. [Q94JM3-1] DR EnsemblPlants; AT5G62000.1; AT5G62000.1; AT5G62000. [Q94JM3-1] DR EnsemblPlants; AT5G62000.2; AT5G62000.2; AT5G62000. [Q94JM3-1] DR EnsemblPlants; AT5G62000.3; AT5G62000.3; AT5G62000. [Q94JM3-1] DR EnsemblPlants; AT5G62000.5; AT5G62000.5; AT5G62000. [Q94JM3-1] DR GeneID; 836321; -. DR Gramene; AT5G62000.1; AT5G62000.1; AT5G62000. [Q94JM3-1] DR Gramene; AT5G62000.2; AT5G62000.2; AT5G62000. [Q94JM3-1] DR Gramene; AT5G62000.3; AT5G62000.3; AT5G62000. [Q94JM3-1] DR Gramene; AT5G62000.5; AT5G62000.5; AT5G62000. [Q94JM3-1] DR KEGG; ath:AT5G62000; -. DR Araport; AT5G62000; -. DR TAIR; AT5G62000; ARF2. DR eggNOG; ENOG502QRXI; Eukaryota. DR HOGENOM; CLU_002626_2_2_1; -. DR InParanoid; Q94JM3; -. DR OMA; ENWMPSG; -. DR OrthoDB; 447839at2759; -. DR PhylomeDB; Q94JM3; -. DR PRO; PR:Q94JM3; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q94JM3; baseline and differential. DR Genevisible; Q94JM3; AT. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR. DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0010227; P:floral organ abscission; IMP:TAIR. DR GO; GO:0010047; P:fruit dehiscence; IMP:TAIR. DR GO; GO:0010150; P:leaf senescence; IMP:TAIR. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:TAIR. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:TAIR. DR GO; GO:0048481; P:plant ovule development; IMP:TAIR. DR GO; GO:0009911; P:positive regulation of flower development; IMP:TAIR. DR GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; IMP:TAIR. DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR. DR CDD; cd10017; B3_DNA; 1. DR Gene3D; 2.30.30.1040; -; 1. DR Gene3D; 2.40.330.10; DNA-binding pseudobarrel domain; 1. DR InterPro; IPR010525; ARF_dom. DR InterPro; IPR044835; ARF_plant. DR InterPro; IPR033389; AUX/IAA_dom. DR InterPro; IPR003340; B3_DNA-bd. DR InterPro; IPR015300; DNA-bd_pseudobarrel_sf. DR InterPro; IPR000270; PB1_dom. DR PANTHER; PTHR31384:SF79; AUXIN RESPONSE FACTOR 2; 1. DR PANTHER; PTHR31384; AUXIN RESPONSE FACTOR 4-RELATED; 1. DR Pfam; PF02309; AUX_IAA; 1. DR Pfam; PF06507; Auxin_resp; 1. DR Pfam; PF02362; B3; 1. DR SMART; SM01019; B3; 1. DR SUPFAM; SSF54277; CAD & PB1 domains; 1. DR SUPFAM; SSF101936; DNA-binding pseudobarrel domain; 1. DR PROSITE; PS50863; B3; 1. DR PROSITE; PS51745; PB1; 1. PE 1: Evidence at protein level; KW Alternative splicing; Auxin signaling pathway; DNA-binding; Nucleus; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..859 FT /note="Auxin response factor 2" FT /id="PRO_0000111506" FT DOMAIN 733..817 FT /note="PB1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081" FT DNA_BIND 164..266 FT /note="TF-B3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00326" FT REGION 1..48 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 396..442 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 687..736 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 829..859 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..47 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 396..414 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 416..431 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 711..736 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 845..859 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 491..492 FT /note="RR -> KK (in Ref. 6; AAC49752 and 7; CAD29696/ FT CAD30210)" FT /evidence="ECO:0000305" FT CONFLICT 520 FT /note="D -> E (in Ref. 6; AAC49752 and 7; CAD29696/ FT CAD30210)" FT /evidence="ECO:0000305" FT CONFLICT 596 FT /note="V -> A (in Ref. 5; BAD93968)" FT /evidence="ECO:0000305" FT CONFLICT 675 FT /note="R -> K (in Ref. 6; AAC49752 and 7; CAD29696/ FT CAD30210)" FT /evidence="ECO:0000305" FT CONFLICT 823 FT /note="P -> Q (in Ref. 6; AAC49752 and 7; CAD29696/ FT CAD30210)" FT /evidence="ECO:0000305" FT CONFLICT 826 FT /note="L -> V (in Ref. 5; BAD93959/BAD93897/BAD93891)" FT /evidence="ECO:0000305" SQ SEQUENCE 859 AA; 95701 MW; 6B75171D7FF0E66B CRC64; MASSEVSMKG NRGGDNFSSS GFSDPKETRN VSVAGEGQKS NSTRSAAAER ALDPEAALYR ELWHACAGPL VTVPRQDDRV FYFPQGHIEQ VEASTNQAAE QQMPLYDLPS KLLCRVINVD LKAEADTDEV YAQITLLPEA NQDENAIEKE APLPPPPRFQ VHSFCKTLTA SDTSTHGGFS VLRRHADECL PPLDMSRQPP TQELVAKDLH ANEWRFRHIF RGQPRRHLLQ SGWSVFVSSK RLVAGDAFIF LRGENGELRV GVRRAMRQQG NVPSSVISSH SMHLGVLATA WHAISTGTMF TVYYKPRTSP SEFIVPFDQY MESVKNNYSI GMRFKMRFEG EEAPEQRFTG TIVGIEESDP TRWPKSKWRS LKVRWDETSS IPRPDRVSPW KVEPALAPPA LSPVPMPRPK RPRSNIAPSS PDSSMLTREG TTKANMDPLP ASGLSRVLQG QEYSTLRTKH TESVECDAPE NSVVWQSSAD DDKVDVVSGS RRYGSENWMS SARHEPTYTD LLSGFGTNID PSHGQRIPFY DHSSSPSMPA KRILSDSEGK FDYLANQWQM IHSGLSLKLH ESPKVPAATD ASLQGRCNVK YSEYPVLNGL STENAGGNWP IRPRALNYYE EVVNAQAQAQ AREQVTKQPF TIQEETAKSR EGNCRLFGIP LTNNMNGTDS TMSQRNNLND AAGLTQIASP KVQDLSDQSK GSKSTNDHRE QGRPFQTNNP HPKDAQTKTN SSRSCTKVHK QGIALGRSVD LSKFQNYEEL VAELDRLFEF NGELMAPKKD WLIVYTDEEN DMMLVGDDPW QEFCCMVRKI FIYTKEEVRK MNPGTLSCRS EEEAVVGEGS DAKDAKSASN PSLSSAGNS //