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BIG1_ARATH
ID   BIG1_ARATH              Reviewed;        1687 AA.
AC   F4JSZ5; Q0WUF1; Q9SZM0;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Brefeldin A-inhibited guanine nucleotide-exchange protein 1;
DE            Short=BIG1;
DE   AltName: Full=ARF guanine-nucleotide exchange factor BIG1;
GN   Name=BIG1; OrderedLocusNames=At4g38200; ORFNames=F20D10.320;
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=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   [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 897-1687.
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   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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB37560.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80485.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL035538; CAB37560.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161593; CAB80485.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86892.1; -; Genomic_DNA.
DR   EMBL; AK227209; BAE99247.1; -; mRNA.
DR   PIR; T05647; T05647.
DR   RefSeq; NP_195533.2; NM_119981.4.
DR   AlphaFoldDB; F4JSZ5; -.
DR   SMR; F4JSZ5; -.
DR   STRING; 3702.AT4G38200.1; -.
DR   PaxDb; F4JSZ5; -.
DR   PRIDE; F4JSZ5; -.
DR   ProteomicsDB; 240344; -.
DR   EnsemblPlants; AT4G38200.1; AT4G38200.1; AT4G38200.
DR   GeneID; 829976; -.
DR   Gramene; AT4G38200.1; AT4G38200.1; AT4G38200.
DR   KEGG; ath:AT4G38200; -.
DR   Araport; AT4G38200; -.
DR   TAIR; locus:2120923; AT4G38200.
DR   eggNOG; KOG0929; Eukaryota.
DR   HOGENOM; CLU_000691_0_0_1; -.
DR   InParanoid; F4JSZ5; -.
DR   OMA; DLYITFF; -.
DR   OrthoDB; 815698at2759; -.
DR   PRO; PR:F4JSZ5; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JSZ5; baseline and differential.
DR   Genevisible; F4JSZ5; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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   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; 1.
DR   SUPFAM; SSF48425; SSF48425; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..1687
FT                   /note="Brefeldin A-inhibited guanine nucleotide-exchange
FT                   protein 1"
FT                   /id="PRO_0000420950"
FT   DOMAIN          532..719
FT                   /note="SEC7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT   REGION          494..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1229..1248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..524
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        634
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1687 AA;  187537 MW;  3A4181CB4EE0EF69 CRC64;
     MSSSQNLGGA TRCGRVIGPS LDKIIKNAAW RKHTFLVSAC KSVLDKLEAL SDSPDPSSPL
     FGLTTSDADA VLQPLLLSLD TGYAKVIEPA LDCSFKLFSL SLLRGEVCSS SPDSLLYKLI
     HAICKVCGIG EESIELAVLR VLLAAVRSPR ILIRGDCLLH LVRTCYNVYL GGFNGTNQIC
     AKSVLAQIML IVFTRSEANS MDASLKTVNV NDLLAITDKN VNEGNSVHIC QGFINDVITA
     GEAAPPPDFA LVQPPEEGAS STEDEGTGSK IREDGFLLFK NLCKLSMKFS SQENTDDQIL
     VRGKTLSLEL LKVIIDNGGP IWLSDERFLN AIKQLLCLSL LKNSALSVMS IFQLQCAIFT
     TLLRKYRSGM KSEVGIFFPM LVLRVLENVL QPSFVQKMTV LSLLENICHD PNLIIDIFVN
     FDCDVESPNI FERIVNGLLK TALGPPPGSS TILSPVQDIT FRHESVKCLV SIIKAMGTWM
     DQQLSVGDSL LPKSLENEAP ANNHSNSNEE DGTTIDHDFH PDLNPESSDA ATLEQRRAYK
     IERQKGVTLF NRKPSKGIEF LISSKKVGNS PDEVVSFLRN TTGLNATMIG DYLGEREDFP
     MKVMHAYVDS FDFKEMNFGE AIRFFLRGFR LPGEAQKIDR IMEKFAERFC KCNPNSFSSA
     DTAYVLAYSV IMLNTDAHNI MVKEKMTKAD FIRNNRGIDD GKDLPEEYLG ALYDQVVINE
     IKMSSDSSAP ESRQSNGLNK LLGLDGILNL VYWTQTEEKA VGANGLLIKD IQEKFRSKSG
     KSESAYHVVT DVAILRFMVE VSWGPMLAAF SVTLDQSDDR LAAVECLRGF RYAVHVTAVM
     GMQTQRDAFV TSMAKFTNLH CAGDMKQKNV DAVKAIISIA IEDGNHLQDA WEHILTCLSR
     IEHLQLLGEG APSDASYFAS TETEEKKALG FPNLKKKGAL QNPVMMAVVR GGSYDSSTIG
     PNMPGLVKQD QINNFIANLN LLDQIGSFQL NNVYAHSQRL KTEAIVAFVK ALCKVSMSEL
     QSPTDPRVFS LTKLVEIAHY NMNRIRLVWS RIWSILSDFF VSVGLSENLS VAIFVMDSLR
     QLSMKFLERE ELANYNFQNE FLRPFVIVMQ KSSSAEIREL IVRCISQMVL SRVSNVKSGW
     KSVFKVFTTA AADERKNIVL LAFETMEKIV REYFSYITET EATTFTDCVR CLITFTNSTF
     TSDVSLNAIA FLRFCALKLA DGGLVWNEKG RSSSPSTPVT DDHSPSTQNF MDADENISYW
     VPLLTGLSKL TSDSRSAIRK SSLEVLFNIL KDHGHIFSRT FWIGVFSSVI YPIFNSVWGE
     NDLLSKDEHS SFPSTFSSHP SEVSWDAETS AMAAQYLVDL FVSFFTVIRS QLSSVVSLLA
     GLIRSPAQGP TVAGVGALLR LADELGDRFS ENEWKEIFLA VNEAASLTLS SFMKTLRTMD
     DIPDEDTLSD QDFSNEDDID EDSLQTMSYV VARTKSHITV QLQVVQVVTD LYRIHQQSLL
     ASHVTVILEI LSSISSHAHQ LNSDLILQKK VRRACSILEL SEPPMLHFEN DTFQNYLDIL
     QAIVTNNPGV SLELNVESQL MTVCMQILKM YLKCTLFQGD ELEETRQPKN WILPMGAASK
     EEAAARSPLV VAVLKALREL KRDSFKRYAP NFFPLLVELV RSEHSSSQVP QVLSTVFHTC
     MGAMMDE
 
 
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