BIG2_ARATH
ID BIG2_ARATH Reviewed; 1793 AA.
AC Q9LZX8;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Brefeldin A-inhibited guanine nucleotide-exchange protein 2;
DE Short=BIG2;
DE AltName: Full=ARF guanine-nucleotide exchange factor BIG2;
GN Name=BIG2; OrderedLocusNames=At3g60860; ORFNames=T4C21_270;
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 1605-1793.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
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 [5]
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 [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).
CC -!- FUNCTION: Activates the ARF proteins by exchanging bound GDP for free
CC GTP. Plays a role in vesicular protein sorting (By similarity).
CC {ECO:0000250}.
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}.
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DR EMBL; AL162295; CAB82690.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80118.1; -; Genomic_DNA.
DR EMBL; BX826000; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T47897; T47897.
DR RefSeq; NP_191645.1; NM_115950.4.
DR AlphaFoldDB; Q9LZX8; -.
DR SMR; Q9LZX8; -.
DR BioGRID; 10571; 1.
DR STRING; 3702.AT3G60860.1; -.
DR iPTMnet; Q9LZX8; -.
DR PaxDb; Q9LZX8; -.
DR PRIDE; Q9LZX8; -.
DR ProteomicsDB; 240427; -.
DR EnsemblPlants; AT3G60860.1; AT3G60860.1; AT3G60860.
DR GeneID; 825257; -.
DR Gramene; AT3G60860.1; AT3G60860.1; AT3G60860.
DR KEGG; ath:AT3G60860; -.
DR Araport; AT3G60860; -.
DR TAIR; locus:2101906; AT3G60860.
DR eggNOG; KOG0929; Eukaryota.
DR HOGENOM; CLU_000691_1_1_1; -.
DR InParanoid; Q9LZX8; -.
DR OMA; LLWNMEM; -.
DR OrthoDB; 815698at2759; -.
DR PhylomeDB; Q9LZX8; -.
DR PRO; PR:Q9LZX8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZX8; baseline and differential.
DR Genevisible; Q9LZX8; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:TAIR.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
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; 2.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 2: Evidence at transcript 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:0000250|UniProtKB:Q9LPC5"
FT CHAIN 2..1793
FT /note="Brefeldin A-inhibited guanine nucleotide-exchange
FT protein 2"
FT /id="PRO_0000420951"
FT DOMAIN 610..797
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 45..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 712
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPC5"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPC5"
SQ SEQUENCE 1793 AA; 199632 MW; 2FD4A7F5449D417B CRC64;
MASSEADSRL SRVVTPALEK IVKNASWRKH SKLANECKAV IERLNSLQKS PPPSSSAATD
SESESSVPGP LNDGGSIEYS LADSELIFSP LINACGTGLA KIIEPAIDCI QKLIAHGYIR
GESDPSGGAE SLLLFKLIDS VCKCHDLGDE SIELPVLKTL LSAINSISLR IHGKCLLLVV
RTCYDIYLGS KNVVNQTTAK ASLIQILVIV FRRMEADSST VPIQPIVVAE LMEPLEKSDA
DGTMTQFVQG FITKIMQDID GVLNPTMSGS GSGSGSGGQD GAYGTTTVET TNPTDLLDST
DKDMLDAKYW EISMYKSALE GRKGELTDGD AERDDDLEVQ IENKLRRDAC LVFRALCKLS
MKAPPKESSA DPQSMRGKIL ALELLKILLE NAGAVFRTSE KFSADIKQFL CLSLLKNSAS
TLMIIFQLSC SIFISLVARF RAGLKAEIGV FFPMIVLRVV ENVAQPNFQQ KMIVLRFLDK
LCLDSQILVD IFLNYDCDVN SSNIFERMVN GLLKTAQGVP PGTATTLMPP QEAAMKLEAM
KCLVAILKSM GDWLNKQLRL PVSNSLNKSD VIEIDLGPGS PQLANGNADE SADGSDTYSE
SSGGTSDALA IEQRRAYKLE LQEGISLFNR KPTKGIEFLI NAGKVGESPE EIAGFLKDAS
GLNKTLIGDY LGEREDLALK VMHAYVDSFD FRGMEFDEAI RTFLEGFRLP GEAQKIDRIM
EKFAERYCKC NPKVFTSADS AYVLAYSVIM LNTDAHNPMV KNKMSADDFI RNNRGIDDGK
DLPADYMRSL YERITKHEIK MKEDDLRLQQ KQYANSNRML GLDGILNIVI RKQWGDSYAE
TSDDLMKHMQ EQFKEKARKS ESTYYAATDV VILRFMIEAC WAPMLAAFSV PLDQSDDLIV
INICLEGFHH AIHATSLMSM KTHRDAFVTS LAKFTSLHSP ADIKQRNIEA IKAILRLADE
EGNYLQDAWE HILTCVSRFE QLHLLGEGAP PDATFFASKQ NESEKSKQPK QYILPVLKRK
GPGKSQYAAT GVLRGSYDSM SLGGKGSKNV RQEQMSSIVS NLNLLEQVGE MNQVFSQSQK
LNSEAIIDFV KALCKVSMDE LRSPSNPRVF SLTKIVEIAH YNMNRIRLVW SSIWQVLSGF
FVTIGCSENL SIAIFAMDSL RQLSMKFLER EELANYNFQN EFMTPFVIVM RRSNDVEIRE
LIIRCVSQMV LSRVNNVKSG WKSMFMVFTT AAYDDHKNIV FLSFEIIEKI IREYFPYITE
TETTTFTDCV NCLVAFTNNR FSKDISLSSI AFLRYCATKL AEGDLNSPST NKYKGTSGKI
PQSSLHSGKS GKQENGEIVN NNHLYFWFPL LSGLSELSFD PRPEIRKSAL QIMFDTLRNH
GHLFSLPLWE KVFESVLFPI FDYVRHSIDP SGEDESADQG SSGGEVDELD HDAWLYETCT
LALQLVVDLF VKFYTTVNPL LEKVLMLLVS FIKRPHQSLA GIGIAAFVRL MSDADGLFSE
EKWLEVVSAL KEAAKTTCPD FSYFLSEEYV ARSQRSALNI QNSNAESAAP TATDGNEESQ
RTATHLYAAI SDAKCRAAVQ LLLIQAVMEI YNMYRPQLSA KNTLVLVDAL HGVALHAHGI
NSNTILRSRL QELGPMTQMQ DPPLLRLENE SYQICLTFLQ NLVADKTKKE EEEEEEEIES
LLVNICQEVL NFYIETSSSA KKLQSESSRA SEYRWRIPLG SGKRRELSAR APLIVATLQA
MCTLDEASFE KNLKCLFPLL ANLISCEHGS NEVQTALADM LGLSVGPVLL QWC
