BIG3_ARATH
ID BIG3_ARATH Reviewed; 1750 AA.
AC Q9LPC5;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Brefeldin A-inhibited guanine nucleotide-exchange protein 3;
DE Short=BIG3;
DE AltName: Full=ARF guanine-nucleotide exchange factor BIG3;
DE AltName: Full=Protein EMBRYO SAC DEVELOPMENT ARREST 10;
GN Name=BIG3; Synonyms=EDA10; OrderedLocusNames=At1g01960; ORFNames=F22M8.9;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 GENE FAMILY.
RX PubMed=12553910; DOI=10.1016/s0092-8674(03)00003-5;
RA Geldner N., Anders N., Wolters H., Keicher J., Kornberger W., Muller P.,
RA Delbarre A., Ueda T., Nakano A., Juergens G.;
RT "The Arabidopsis GNOM ARF-GEF mediates endosomal recycling, auxin
RT transport, and auxin-dependent plant growth.";
RL Cell 112:219-230(2003).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14742722; DOI=10.1091/mbc.e03-06-0443;
RA Cox R., Mason-Gamer R.J., Jackson C.L., Segev N.;
RT "Phylogenetic analysis of Sec7-domain-containing Arf nucleotide
RT exchangers.";
RL Mol. Biol. Cell 15:1487-1505(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
RN [6]
RP GENE FAMILY.
RX PubMed=17653190; DOI=10.1038/nature05967;
RA Richter S., Geldner N., Schrader J., Wolters H., Stierhof Y.D., Rios G.,
RA Koncz C., Robinson D.G., Juergens G.;
RT "Functional diversification of closely related ARF-GEFs in protein
RT secretion and recycling.";
RL Nature 448:488-492(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586, AND IDENTIFICATION BY
RP 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 [10]
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).
CC -!- FUNCTION: Activates the ARF proteins by exchanging bound GDP for free
CC GTP. Plays a role in vesicular protein sorting (By similarity).
CC Involved both in the nuclear division phase and in the nuclear fusion
CC phase. {ECO:0000250, ECO:0000269|PubMed:15634699}.
CC -!- ACTIVITY REGULATION: Inhibited by brefeldin A. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Soluble and partially membrane-bound.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Abnormal nuclear numbers and positions. No embryo
CC sac. {ECO:0000269|PubMed:15634699}.
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DR EMBL; AC020622; AAF76474.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27360.1; -; Genomic_DNA.
DR PIR; E86151; E86151.
DR RefSeq; NP_171698.1; NM_100076.3.
DR AlphaFoldDB; Q9LPC5; -.
DR SMR; Q9LPC5; -.
DR BioGRID; 24536; 1.
DR STRING; 3702.AT1G01960.1; -.
DR iPTMnet; Q9LPC5; -.
DR PaxDb; Q9LPC5; -.
DR PRIDE; Q9LPC5; -.
DR ProMEX; Q9LPC5; -.
DR ProteomicsDB; 240428; -.
DR EnsemblPlants; AT1G01960.1; AT1G01960.1; AT1G01960.
DR GeneID; 839301; -.
DR Gramene; AT1G01960.1; AT1G01960.1; AT1G01960.
DR KEGG; ath:AT1G01960; -.
DR Araport; AT1G01960; -.
DR TAIR; locus:2025502; AT1G01960.
DR eggNOG; KOG0929; Eukaryota.
DR HOGENOM; CLU_000691_0_2_1; -.
DR InParanoid; Q9LPC5; -.
DR OMA; QESWLYE; -.
DR OrthoDB; 815698at2759; -.
DR PhylomeDB; Q9LPC5; -.
DR PRO; PR:Q9LPC5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPC5; baseline and differential.
DR Genevisible; Q9LPC5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:TAIR.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0009561; P:megagametogenesis; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:TAIR.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032629; DCB_dom.
DR InterPro; IPR032817; Mon2_C.
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; PF16206; Mon2_C; 1.
DR Pfam; PF01369; Sec7; 1.
DR Pfam; PF12783; Sec7_N; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1750
FT /note="Brefeldin A-inhibited guanine nucleotide-exchange
FT protein 3"
FT /id="PRO_0000420952"
FT DOMAIN 601..788
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 44..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 703
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 1307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
SQ SEQUENCE 1750 AA; 194943 MW; F4FCFF663ACDB019 CRC64;
MASTEVDSRL GRVVIPALDK VIKNASWRKH SKLAHECKSV IERLRSPENS SPVADSESGS
SIPGPLHDGG AAEYSLAESE IILSPLINAS STGVLKIVDP AVDCIQKLIA HGYVRGEADP
TGGPEALLLS KLIETICKCH ELDDEGLELL VLKTLLTAVT SISLRIHGDS LLQIVRTCYG
IYLGSRNVVN QATAKASLVQ MSVIVFRRME ADSSTVPIQP IVVAELMEPM DKSESDPSTT
QSVQGFITKI MQDIDGVFNS ANAKGTFGGH DGAFETSLPG TANPTDLLDS TDKDMLDAKY
WEISMYKSAL EGRKGELADG EVEKDDDSEV QIGNKLRRDA FLVFRALCKL SMKTPPKEDP
ELMRGKIVAL ELLKILLENA GAVFRTSDRF LGAIKQYLCL SLLKNSASNL MIIFQLSCSI
LLSLVSRFRA GLKAEIGVFF PMIVLRVLEN VAQPDFQQKM IVLRFLDKLC VDSQILVDIF
INYDCDVNSS NIFERMVNGL LKTAQGVPPG TVTTLLPPQE AAMKLEAMKC LVAVLRSMGD
WVNKQLRLPD PYSAKMLEIV DRNLEEGSHP VENGKGDGGH GGFERSDSQS ELSSGNSDAL
AIEQRRAYKL ELQEGISIFN QKPKKGIEFL IKANKVGDSP EEIAAFLKDA SGLNKTLIGD
YLGEREDLSL KVMHAYVDSF EFQGMEFDEA IRAFLRGFRL PGEAQKIDRI MEKFAERFCK
CNPKDFSSAD TAYVLAYSVI LLNTDAHNPM VKSKMTADGF IRNNRGIDDG KDLPEEYLRA
LYERISRNEI KMKDDGLGPQ QKQPTNSSRL LGLDTILNIV VPRRGDDMNM ETSDDLIRHM
QERFKEKARK SESVYYAASD VIILRFMVEV CWAPMLAAFS VPLDQSDDAV ITTLCLEGFH
HAIHVTSVMS LKTHRDAFVT SLAKFTSLHS PADIKQKNIE AIKAIVKLAE EEGNYLQDAW
EHILTCVSRF EHLHLLGEGA PPDATFFAFP QTESGNSPLA KPNSVPAIKE RAPGKLQYAA
SAMIRGSYDG SGVAGKASNT VTSEQMNNLI SNLNLLEQVG DMSRIFTRSQ RLNSEAIIDF
VKALCKVSMD ELRSPSDPRV FSLTKIVEIA HYNMNRIRLV WSSIWHVLSD FFVTIGCSDN
LSIAIFAMDS LRQLSMKFLE REELANYNFQ NEFMKPFVVV MRKSGAVEIR ELIIRCVSQM
VLSRVDNVKS GWKSMFMIFT TAAHDAHKNI VFLSFEMVEK IIRDYFPHIT ETETTTFTDC
VNCLVAFTNC KFEKDISLQA IAFLQYCARK LAEGYVGSSL RRNPPLSPQG GKIGKQDSGK
FLESDEHLYS WFPLLAGLSE LSFDPRAEIR KVALKVLFDT LRNHGDHFSL ALWERVFESV
LFRIFDYVRQ DVDPSEDDST DQRGYNGEVD QESWLYETCS LALQLVVDLF VNFYKTVNPL
LKKVLMLFVS LIKRPHQSLA GAGIAALVRL MRDVGHQFSN EQWLEVVSCI KEAADATSPD
FSYVTSEDLM EDVSNEDETN DNSNDALRRR NRQLHAVVTD AKSKASIQIF VIQAVTDIYD
MYRMSLTANH MLMLFDAMHG IGSNAHKINA DLLLRSKLQE LGSSLESQEA PLLRLENESF
QTCMTFLDNL ISDQPVGYNE AEIESHLISL CREVLEFYIN ISCSKEQSSR WAVPSGSGKK
KELTARAPLV VAAIQTLGNM GESLFKKNLP ELFPLIATLI SCEHGSGEVQ VALSDMLQTS
MGPVLLRSCC
