BIG5_ARATH
ID BIG5_ARATH Reviewed; 1739 AA.
AC F4IXW2; F4IXW1; Q0WM86; Q9LXK4;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Brefeldin A-inhibited guanine nucleotide-exchange protein 5 {ECO:0000303|PubMed:19230664};
DE Short=BIG5 {ECO:0000303|PubMed:19230664};
DE AltName: Full=ARF guanine-nucleotide exchange factor BIG5 {ECO:0000303|PubMed:19230664};
DE AltName: Full=Protein BFA-VISUALIZED ENDOCYTIC TRAFFICKING DEFECTIVE 1 {ECO:0000303|PubMed:19230664, ECO:0000303|PubMed:23737757};
DE Short=Protein BEN1 {ECO:0000303|PubMed:19230664, ECO:0000303|PubMed:23737757};
DE AltName: Full=Protein HOPM INTERACTOR 7 {ECO:0000303|PubMed:16840699, ECO:0000303|PubMed:21670267};
DE Short=AtMIN7 {ECO:0000303|PubMed:16840699, ECO:0000303|PubMed:21670267};
GN Name=BIG5 {ECO:0000303|PubMed:19230664};
GN Synonyms=BEN1 {ECO:0000303|PubMed:19230664, ECO:0000303|PubMed:23737757},
GN MIN7 {ECO:0000303|PubMed:16840699, ECO:0000303|PubMed:21670267};
GN OrderedLocusNames=At3g43300 {ECO:0000312|Araport:AT3G43300};
GN ORFNames=F7K15_150 {ECO:0000312|EMBL:CAB89051.1};
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 [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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1580-1739.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH HOPM1, UBIQUITINATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16840699; DOI=10.1126/science.1129523;
RA Nomura K., DebRoy S., Lee Y.H., Pumplin N., Jones J., He S.Y.;
RT "A bacterial virulence protein suppresses host innate immunity to cause
RT plant disease.";
RL Science 313:220-223(2006).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=19230664; DOI=10.1016/j.cub.2009.01.057;
RA Tanaka H., Kitakura S., De Rycke R., De Groodt R., Friml J.;
RT "Fluorescence imaging-based screen identifies ARF GEF component of early
RT endosomal trafficking.";
RL Curr. Biol. 19:391-397(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=21670267; DOI=10.1073/pnas.1103338108;
RA Nomura K., Mecey C., Lee Y.N., Imboden L.A., Chang J.H., He S.Y.;
RT "Effector-triggered immunity blocks pathogen degradation of an immunity-
RT associated vesicle traffic regulator in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10774-10779(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=23737757; DOI=10.1371/journal.pgen.1003540;
RA Tanaka H., Kitakura S., Rakusova H., Uemura T., Feraru M.I., De Rycke R.,
RA Robert S., Kakimoto T., Friml J.;
RT "Cell polarity and patterning by PIN trafficking through early endosomal
RT compartments in Arabidopsis thaliana.";
RL PLoS Genet. 9:e1003540-e1003540(2013).
RN [10]
RP INTERACTION WITH HLB1.
RX PubMed=26941089; DOI=10.1105/tpc.15.00794;
RA Sparks J.A., Kwon T., Renna L., Liao F., Brandizzi F., Blancaflor E.B.;
RT "HLB1 is a tetratricopeptide repeat domain-containing protein that operates
RT at the intersection of the exocytic and endocytic pathways at the TGN/EE in
RT Arabidopsis.";
RL Plant Cell 28:746-769(2016).
CC -!- FUNCTION: Activates the ARF proteins by exchanging bound GDP for free
CC GTP. Plays a role in vesicular protein sorting. Acts as the major
CC regulator of early endosomal vesicle trafficking, particularly at the
CC trans-Golgi-network/early endosome (TGN/EE), but is also involved in
CC the endocytosis process (PubMed:23737757). Together with VPS45/BEN2
CC required for polar PIN-FORMED (PIN) proteins localization, for their
CC dynamic repolarization, and consequently for auxin activity gradient
CC formation and auxin-related developmental processes (e.g. embryonic
CC patterning, organogenesis and vasculature venation patterning)
CC (PubMed:23737757). Target of hopM1, a conserved Pseudomonas syringae
CC virulence protein that directs the protein to its own proteasome-
CC mediated degradation. Plays a broad role in PAMP-triggered immunity
CC (PTI), effector-triggered immunity (ETI), and salicylic acid (SA)-
CC regulated immunity. {ECO:0000269|PubMed:19230664,
CC ECO:0000269|PubMed:21670267, ECO:0000269|PubMed:23737757}.
CC -!- ACTIVITY REGULATION: Inhibited by brefeldin A. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with hopM1
CC (PubMed:16840699). Interacts with HLB1 (PubMed:26941089). {ECO:0000250,
CC ECO:0000269|PubMed:16840699, ECO:0000269|PubMed:26941089}.
CC -!- INTERACTION:
CC F4IXW2; Q887D0: hopM1; Xeno; NbExp=3; IntAct=EBI-6395043, EBI-6394949;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:19230664,
CC ECO:0000269|PubMed:21670267}; Peripheral membrane protein; Cytoplasmic
CC side. Early endosome membrane {ECO:0000269|PubMed:19230664,
CC ECO:0000269|PubMed:21670267, ECO:0000269|PubMed:23737757}; Peripheral
CC membrane protein; Cytoplasmic side. Note=Soluble and partially
CC membrane-bound.
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=F4IXW2-1; Sequence=Displayed;
CC -!- INDUCTION: By the pathogen elicitor flagellin 22 and by
CC benzothiadiazole (BTH), a synthetic activator of the salicylic acid
CC (SA)-dependent immunity (at protein level).
CC {ECO:0000269|PubMed:21670267}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:16840699}.
CC -!- DISRUPTION PHENOTYPE: Inhibited trafficking at the trans-Golgi-
CC network/early endosome (TGN/EE) leading to an increased accumulation of
CC PIN2 in agglomerated intracellular compartments leading to an altered
CC auxin gradient and subsequent growth defects (e.g. disrupted roots
CC architecture and shoot growth) (PubMed:23737757). Increased
CC susceptibility to Pseudomonas syringae infection (PubMed:16840699).
CC Displays growth and polarity defects (PubMed:19230664).
CC {ECO:0000269|PubMed:16840699, ECO:0000269|PubMed:19230664,
CC ECO:0000269|PubMed:23737757}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE77785.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE77786.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB89051.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL353871; CAB89051.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77785.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77786.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; ANM65211.1; -; Genomic_DNA.
DR EMBL; AK229944; BAF01770.1; -; mRNA.
DR PIR; T49244; T49244.
DR RefSeq; NP_001190006.1; NM_001203077.1.
DR RefSeq; NP_001327198.1; NM_001339097.1. [F4IXW2-1]
DR RefSeq; NP_189916.4; NM_114198.4.
DR AlphaFoldDB; F4IXW2; -.
DR SMR; F4IXW2; -.
DR BioGRID; 8727; 1.
DR IntAct; F4IXW2; 1.
DR STRING; 3702.AT3G43300.1; -.
DR iPTMnet; F4IXW2; -.
DR PaxDb; F4IXW2; -.
DR PRIDE; F4IXW2; -.
DR ProMEX; F4IXW2; -.
DR ProteomicsDB; 240794; -. [F4IXW2-1]
DR EnsemblPlants; AT3G43300.3; AT3G43300.3; AT3G43300. [F4IXW2-1]
DR GeneID; 823405; -.
DR Gramene; AT3G43300.3; AT3G43300.3; AT3G43300. [F4IXW2-1]
DR KEGG; ath:AT3G43300; -.
DR Araport; AT3G43300; -.
DR TAIR; locus:2084706; AT3G43300.
DR eggNOG; KOG0929; Eukaryota.
DR HOGENOM; CLU_000691_1_1_1; -.
DR InParanoid; F4IXW2; -.
DR OrthoDB; 815698at2759; -.
DR PRO; PR:F4IXW2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4IXW2; baseline and differential.
DR Genevisible; F4IXW2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:2000012; P:regulation of auxin polar transport; IMP:UniProtKB.
DR GO; GO:2000067; P:regulation of root morphogenesis; IMP:UniProtKB.
DR GO; GO:0031338; P:regulation of vesicle fusion; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032629; DCB_dom.
DR InterPro; IPR015403; Sec7_C.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR InterPro; IPR032691; Sec7_N.
DR Pfam; PF16213; DCB; 1.
DR Pfam; PF09324; DUF1981; 1.
DR Pfam; PF01369; Sec7; 1.
DR Pfam; PF12783; Sec7_N; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Auxin signaling pathway; Cytoplasm;
KW Endocytosis; Endosome; Golgi apparatus;
KW Guanine-nucleotide releasing factor; Host-virus interaction; Immunity;
KW Innate immunity; Membrane; Protein transport; Reference proteome;
KW Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1739
FT /note="Brefeldin A-inhibited guanine nucleotide-exchange
FT protein 5"
FT /id="PRO_0000420954"
FT DOMAIN 572..759
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 44..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 674
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 1739 AA; 192883 MW; 0E4D8D33D84E4718 CRC64;
MAAGGFLTRA FDTMLKESGG KKFPDLQKAI QAYQDGSKVV TQAAPSSIVE SSQAEGGGEK
TGVEADEPQK VTSAEVAQQA SQSKSETINV SLANAGHTLG GAEVELVLKP LRLAFETKNL
KIFDAALDCL HKLIAYDHLE GDPGLDGGKN SAPFTDILNM VCSCVDNSSP DSTVLQVLKV
LLTAVASGKF KVHGEPLLGV IRVCYNIALN SKSPINQATS KAMLTQMISI VFRRMETDIV
SASSTVSQEE HVSGDTSSPK NEEITAADEN EKEMTLGDAL TQAKDTTLAS VEELHTLVGG
ADIKGLEAAL DKAVHLEDGK KIKRGIELES MSIGQRDALL VFRTLCKMGM KEDSDEVTTK
TRILSLELLQ GMLEGVSHSF TKNFHFIDSV KAYLSYALLR ASVSQSSVIF QYASGIFSVL
LLRFRDSLKG EIGIFFPIIV LRSLDNSECP NDQKMGVLRM LEKVCKDPQM LVDVYVNYDC
DLEAPNLFER MVTTLSKIAQ GSQSADPNPA MASQTASVKG SSLQCLVNVL KSLVDWEKIR
REAENSTRNA NEDSASTGEP IETKSREDVP SNFEKAKAHK STMEAAISEF NRNSVKGVEY
LIANKLVERN PASVAQFLRS TSSLSKVMIG DYLGQHEEFP LAVMHAYVDS MKFSEMKFHS
AIREFLKGFR LPGEAQKIDR IMEKFAERYC ADNPGLFKNA DTAYVLAYAV IMLNTDAHNP
MVWPKMSKSD FTRMNATNDP EDCAPTELLE EIYDSIVQEE IKLKDDDTMK KLSSQRPGGE
ERGGLVSILN LGLPKRISAA DAKSETEDIV RKTQEIFRKH GVKRGVFHTV EQVDIIRPMV
EAVGWPLLAA FSVTMEVGDN KPRILLCMEG FKAGIHIAYV LGMDTMRYAF LTSLVRFTFL
HAPKEMRSKN VEALRILLGL CDSEPDTLQD TWNAVLECVS RLEFIISTPG IAATVMHGSN
QISRDGVVQS LKELAGRPAE QVFVNSVKLP SESVVEFFTA LCGVSAEELK QSPARVFSLQ
KLVEISYYNI ARIRMVWARI WSVLAEHFVS AGSHHDEKIA MYAIDSLRQL GMKYLERAEL
TNFTFQNDIL KPFVIIMRNT QSQTIRSLIV DCIVQMIKSK VGSIKSGWRS VFMIFTAAAD
DEVESIVEKS FENVEQVILE HFDQVIGDCF MDCVNCLIRF ANNKASDRIS LKAIALLRIC
EDRLAEGLIP GGVLKPVDGN EDETFDVTEH YWFPMLAGLS DLTSDYRPEV RNCALEVLFD
LLNERGNKFS TPFWESIFHR ILFPIFDHVS HAGKESLISS GDVKFRETSI HSLQLLCNLF
NTFYKEVCFM LPPLLSLLLD CAKKSDQTVV SISLGALVHL IEVGGHQFSE GDWDMLLKSI
RDASYTTQPL ELLNALSFDN PKKNLVLAGD IEADASDSPR VDRNPDDIKD NGKVSAQASP
RIGTHGTSLE SGIPPKADGS EGRPSSSGRA QKDVDDVNLQ RSQTFGQRFM DNLFLRNLTS
QPKSSVAEVT VPSSPYKHED PTEPDSREEE SPALGAIRGK CITQLLLLGA INSIQQKYWS
NLKTPQKIAI MDILFSFIEF ASSYNSYSNL RTRMNHIPTE RPPLNLLRQE LEGTTIYLDV
LQKTTSGLAD DASNSEDRLE GAAEEKLVSF CEQVLKETSD LQSTLGETTN MDVHRVLELR
SPVIVKVLEG MCFMNNTIFR KHMREFYPLL TRLVCCEQME IRGALANLFK AQLKPLLQQ
