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Guanine nucleotide-binding protein subunit beta (AGB1) (transducin)

 GBB_ARATH               Reviewed;         377 AA.
P49177;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-APR-2018, entry version 151.
RecName: Full=Guanine nucleotide-binding protein subunit beta;
AltName: Full=AGB1;
AltName: Full=transducin;
Name=GB1; OrderedLocusNames=At4g34460; ORFNames=T4L20.40;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=7937804; DOI=10.1073/pnas.91.20.9554;
Weiss C.A., Garnaat C.W., Mukai K., Hu Y., Ma H.;
"Isolation of cDNAs encoding guanine nucleotide-binding protein beta-
subunit homologues from maize (ZGB1) and Arabidopsis (AGB1).";
Proc. Natl. Acad. Sci. U.S.A. 91:9554-9558(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
INTERACTION WITH GG1.
STRAIN=cv. Columbia;
PubMed=11121078; DOI=10.1073/pnas.97.26.14784;
Mason M.G., Botella J.R.;
"Completing the heterotrimer: isolation and characterization of an
Arabidopsis thaliana G protein gamma-subunit cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 97:14784-14788(2000).
[5]
INTERACTION WITH GG2.
STRAIN=cv. Columbia;
PubMed=11513956; DOI=10.1016/S0167-4781(01)00262-7;
Mason M.G., Botella J.R.;
"Isolation of a novel G-protein gamma-subunit from Arabidopsis
thaliana and its interaction with Gbeta.";
Biochim. Biophys. Acta 1520:147-153(2001).
[6]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=17158913; DOI=10.1242/jcs.03284;
Adjobo-Hermans M.J.W., Goedhart J., Gadella T.W.J. Jr.;
"Plant G protein heterotrimers require dual lipidation motifs of
Galpha and Ggamma and do not dissociate upon activation.";
J. Cell Sci. 119:5087-5097(2006).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY IMBIBITION.
STRAIN=cv. Columbia;
PubMed=16581874; DOI=10.1104/pp.106.079038;
Pandey S., Chen J.-G., Jones A.M., Assmann S.M.;
"G-protein complex mutants are hypersensitive to abscisic acid
regulation of germination and postgermination development.";
Plant Physiol. 141:243-256(2006).
[8]
FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, TISSUE SPECIFICITY, AND
INDUCTION BY ALTERNARIA BRASSICICOLA AND FUSARIUM OXYSPORUM.
STRAIN=cv. Columbia;
PubMed=17468261; DOI=10.1105/tpc.107.050096;
Trusov Y., Rookes J.E., Tilbrook K., Chakravorty D., Mason M.G.,
Anderson D., Chen J.-G., Jones A.M., Botella J.R.;
"Heterotrimeric G protein gamma subunits provide functional
selectivity in Gbetagamma dimer signaling in Arabidopsis.";
Plant Cell 19:1235-1250(2007).
[9]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=17492287; DOI=10.1007/s00299-007-0356-1;
Anderson D.J., Botella J.R.;
"Expression analysis and subcellular localization of the Arabidopsis
thaliana G-protein beta-subunit AGB1.";
Plant Cell Rep. 26:1469-1480(2007).
[10]
DWD MOTIF.
PubMed=18223036; DOI=10.1105/tpc.107.055418;
Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
He Y.J., Xiong Y., Deng X.W.;
"Characterization of Arabidopsis and rice DWD proteins and their roles
as substrate receptors for CUL4-RING E3 ubiquitin ligases.";
Plant Cell 20:152-167(2008).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18397373; DOI=10.1111/j.1365-313X.2008.03506.x;
Pandey S., Monshausen G.B., Ding L., Assmann S.M.;
"Regulation of root-wave response by extra large and conventional G
proteins in Arabidopsis thaliana.";
Plant J. 55:311-322(2008).
[12]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
STRAIN=cv. Columbia;
PubMed=18441222; DOI=10.1104/pp.108.117655;
Trusov Y., Zhang W., Assmann S.M., Botella J.R.;
"Ggamma1 + Ggamma2 not equal to Gbeta: heterotrimeric G protein
Ggamma-deficient mutants do not recapitulate all phenotypes of Gbeta-
deficient mutants.";
Plant Physiol. 147:636-649(2008).
[13]
INTERACTION WITH XLG2.
PubMed=19825634; DOI=10.1093/mp/ssp001;
Zhu H., Li G.J., Ding L., Cui X., Berg H., Assmann S.M., Xia Y.;
"Arabidopsis extra large G-protein 2 (XLG2) interacts with the Gbeta
subunit of heterotrimeric G protein and functions in disease
resistance.";
Mol. Plant 2:513-525(2009).
[14]
FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH NDL1; NDL2 AND
NDL3.
STRAIN=cv. Columbia;
PubMed=19948787; DOI=10.1105/tpc.109.065557;
Mudgil Y., Uhrig J.F., Zhou J., Temple B., Jiang K., Jones A.M.;
"Arabidopsis N-MYC DOWNREGULATED-LIKE1, a positive regulator of auxin
transport in a G protein-mediated pathway.";
Plant Cell 21:3591-3609(2009).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20862254; DOI=10.1371/journal.pone.0012833;
Booker K.S., Schwarz J., Garrett M.B., Jones A.M.;
"Glucose attenuation of auxin-mediated bimodality in lateral root
formation is partly coupled by the heterotrimeric G protein complex.";
PLoS ONE 5:E12833-E12833(2010).
[16]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=21980142; DOI=10.1093/mp/ssr082;
Delgado-Cerezo M., Sanchez-Rodriguez C., Escudero V., Miedes E.,
Fernandez P.V., Jorda L., Hernandez-Blanco C., Sanchez-Vallet A.,
Bednarek P., Schulze-Lefert P., Somerville S., Estevez J.M.,
Persson S., Molina A.;
"Arabidopsis heterotrimeric G-protein regulates cell wall defense and
resistance to necrotrophic fungi.";
Mol. Plant 5:98-114(2012).
[17]
INTERACTION WITH WNK8.
PubMed=22940907; DOI=10.1038/ncb2568;
Urano D., Phan N., Jones J.C., Yang J., Huang J., Grigston J.,
Taylor J.P., Jones A.M.;
"Endocytosis of the seven-transmembrane RGS1 protein activates G-
protein-coupled signalling in Arabidopsis.";
Nat. Cell Biol. 14:1079-1088(2012).
[18]
INTERACTION WITH RACK1A; RACK1B AND RACK1C.
PubMed=25731164; DOI=10.1038/nature14243;
Cheng Z., Li J.F., Niu Y., Zhang X.C., Woody O.Z., Xiong Y.,
Djonovic S., Millet Y., Bush J., McConkey B.J., Sheen J.,
Ausubel F.M.;
"Pathogen-secreted proteases activate a novel plant immune pathway.";
Nature 521:213-216(2015).
[19]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ZAR1.
PubMed=27014878; DOI=10.1371/journal.pgen.1005933;
Yu T.Y., Shi D.Q., Jia P.F., Tang J., Li H.J., Liu J., Yang W.C.;
"The Arabidopsis receptor kinase ZAR1 is required for zygote
asymmetric division and its daughter cell fate.";
PLoS Genet. 12:E1005933-E1005933(2016).
-!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
involved as a modulator or transducer in various transmembrane
signaling systems. The beta and gamma chains are required for the
GTPase activity, for replacement of GDP by GTP, and for G protein-
effector interaction. Together with GCR1 and GPA1, acts as a
negative regulator of ABA during seed germination and early
seedling development. The heterotrimeric G-protein controls
defense responses to necrotrophic and vascular fungi probably by
modulating cell wall-related genes expression (e.g. lower xylose
content in cell walls); involved in resistance to fungal pathogens
such as Alternaria brassicicola and Fusarium oxysporum. Modulates
root architecture (e.g. lateral root formation). Acts with XGL3 in
the positive regulation of root waving and root skewing. Involved
in the asymmetric division of zygote and specification of apical
and basal cell lineages (PubMed:27014878).
{ECO:0000269|PubMed:16581874, ECO:0000269|PubMed:17468261,
ECO:0000269|PubMed:18397373, ECO:0000269|PubMed:18441222,
ECO:0000269|PubMed:19948787, ECO:0000269|PubMed:20862254,
ECO:0000269|PubMed:21980142, ECO:0000269|PubMed:27014878}.
-!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
gamma. Interacts with the gamma subunits GG1 and GG2. The dimers
GB1-GG1 and GB1-GG2 interact with NDL1, NDL2 and NDL3. Interacts
with WNK8. Interacts with XLG2 (PubMed:11121078, PubMed:11513956,
PubMed:17158913, PubMed:17468261, PubMed:19825634,
PubMed:19948787, PubMed:22940907). Interacts with RACK1A, RACK1B
and RACK1C (PubMed:25731164). Interacts with ZAR1 (via GBeta-
binding domain) (PubMed:27014878). {ECO:0000269|PubMed:11121078,
ECO:0000269|PubMed:11513956, ECO:0000269|PubMed:17158913,
ECO:0000269|PubMed:17468261, ECO:0000269|PubMed:19825634,
ECO:0000269|PubMed:19948787, ECO:0000269|PubMed:22940907,
ECO:0000269|PubMed:25731164, ECO:0000269|PubMed:27014878}.
-!- INTERACTION:
Q9FDX9:GG1; NbExp=7; IntAct=EBI-1632851, EBI-1750878;
Q93V47:GG2; NbExp=2; IntAct=EBI-1632851, EBI-1751115;
P18064:GPA1; NbExp=4; IntAct=EBI-1632851, EBI-443890;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17158913,
ECO:0000269|PubMed:17492287, ECO:0000269|PubMed:27014878}.
Cytoplasm {ECO:0000269|PubMed:17158913}. Nucleus
{ECO:0000269|PubMed:17492287, ECO:0000269|PubMed:27014878}.
Note=Localized to the cell membrane when attached to gamma
subunits as GG1 and GG2 or to both the plasma membrane and the
nucleus when interacting with ZAR1. {ECO:0000269|PubMed:17158913,
ECO:0000269|PubMed:27014878}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=P49177-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed in seedlings (especially at the
hypocotyl/root junction), roots, leaves (restricted to veins and
guard cells), and flowers (PubMed:17468261, PubMed:18441222). Also
present in hydathods (PubMed:17468261). Expressed in guard cells,
mesophyll tissue of cotyledons, trichomes and whole siliques, but
not in seeds (PubMed:17492287). {ECO:0000269|PubMed:17468261,
ECO:0000269|PubMed:17492287, ECO:0000269|PubMed:18441222}.
-!- DEVELOPMENTAL STAGE: In flowers, mostly expressed in stigma and
pollen, and moderately present in sepals and stamen filaments. In
siliques, observed at both ends, gradually disappearing toward the
center. {ECO:0000269|PubMed:18441222}.
-!- INDUCTION: Induced upon imbibition. Induced locally by Alternaria
brassicicola but systemically by Fusarium oxysporum.
{ECO:0000269|PubMed:16581874, ECO:0000269|PubMed:17468261}.
-!- DOMAIN: The DWD box is required for interaction with DDB1A.
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Hypersensitivity to abscisic acid (ABA) and
glucose (Glc) during and after seed germination. Shorter
hypocotyls and abnormal roots architecture; more auxin-induced
lateral roots. Enhanced susceptibility to necrotrophic and
vascular pathogenic fungi, such as Alternaria brassicicola,
Plectosphaerella cucumerina and Fusarium oxysporum associated with
a disturbed expression of genes involved in cell wall metabolism.
Longer and wider primary roots with faster growth. Severely
compromised root waving and abnormal root skewing response.
Hypersensitivity to ethylene (ACC). {ECO:0000269|PubMed:16581874,
ECO:0000269|PubMed:17468261, ECO:0000269|PubMed:18397373,
ECO:0000269|PubMed:18441222, ECO:0000269|PubMed:19948787,
ECO:0000269|PubMed:20862254, ECO:0000269|PubMed:21980142}.
-!- SIMILARITY: Belongs to the WD repeat G protein beta family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U12232; AAA50445.1; -; mRNA.
EMBL; AL023094; CAA18825.1; -; Genomic_DNA.
EMBL; AL161585; CAB80163.1; -; Genomic_DNA.
EMBL; CP002687; AEE86381.1; -; Genomic_DNA.
PIR; T05266; T05266.
RefSeq; NP_195172.1; NM_119611.5. [P49177-1]
UniGene; At.22855; -.
ProteinModelPortal; P49177; -.
SMR; P49177; -.
BioGrid; 14879; 95.
DIP; DIP-40108N; -.
IntAct; P49177; 6.
STRING; 3702.AT4G34460.1; -.
TCDB; 8.A.92.1.2; the g-protein AlphaBetaGama complex (gpc) family.
PaxDb; P49177; -.
PRIDE; P49177; -.
EnsemblPlants; AT4G34460.1; AT4G34460.1; AT4G34460. [P49177-1]
GeneID; 829597; -.
Gramene; AT4G34460.1; AT4G34460.1; AT4G34460. [P49177-1]
KEGG; ath:AT4G34460; -.
Araport; AT4G34460; -.
TAIR; locus:2139489; AT4G34460.
eggNOG; KOG0286; Eukaryota.
eggNOG; ENOG410XQUX; LUCA.
HOGENOM; HOG000176356; -.
InParanoid; P49177; -.
KO; K04536; -.
OMA; TCNVWDT; -.
OrthoDB; EOG09360BYZ; -.
PhylomeDB; P49177; -.
Reactome; R-ATH-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
PRO; PR:P49177; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; P49177; baseline and differential.
Genevisible; P49177; AT.
GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IPI:TAIR.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; ISS:TAIR.
GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
GO; GO:0009817; P:defense response to fungus, incompatible interaction; IMP:TAIR.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:TAIR.
GO; GO:0010154; P:fruit development; IMP:TAIR.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:EnsemblPlants.
GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
GO; GO:0048527; P:lateral root development; IMP:TAIR.
GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
GO; GO:1905392; P:plant organ morphogenesis; IMP:TAIR.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
GO; GO:2000280; P:regulation of root development; IGI:UniProtKB.
GO; GO:0009723; P:response to ethylene; IMP:TAIR.
GO; GO:0009991; P:response to extracellular stimulus; IMP:TAIR.
GO; GO:0048364; P:root development; IMP:TAIR.
GO; GO:0009845; P:seed germination; IMP:TAIR.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR001632; Gprotein_B.
InterPro; IPR016346; Guanine_nucleotide-bd_bsu.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR19850; PTHR19850; 1.
Pfam; PF00400; WD40; 7.
PRINTS; PR00319; GPROTEINB.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 2.
PROSITE; PS50082; WD_REPEATS_2; 5.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Abscisic acid signaling pathway; Alternative splicing; Cell membrane;
Complete proteome; Cytoplasm; Membrane; Nucleus; Plant defense;
Reference proteome; Repeat; Transducer; WD repeat.
CHAIN 1 377 Guanine nucleotide-binding protein
subunit beta.
/FTId=PRO_0000127722.
REPEAT 63 93 WD 1.
REPEAT 105 135 WD 2.
REPEAT 154 185 WD 3.
REPEAT 202 233 WD 4.
REPEAT 246 276 WD 5.
REPEAT 292 323 WD 6.
REPEAT 339 369 WD 7.
MOTIF 220 235 DWD box 1.
MOTIF 263 278 DWD box 1.
SEQUENCE 377 AA; 41006 MW; 06673A2F707A2F44 CRC64;
MSVSELKERH AVATETVNNL RDQLRQRRLQ LLDTDVARYS AAQGRTRVSF GATDLVCCRT
LQGHTGKVYS LDWTPERNRI VSASQDGRLI VWNALTSQKT HAIKLPCAWV MTCAFSPNGQ
SVACGGLDSV CSIFSLSSTA DKDGTVPVSR MLTGHRGYVS CCQYVPNEDA HLITSSGDQT
CILWDVTTGL KTSVFGGEFQ SGHTADVLSV SISGSNPNWF ISGSCDSTAR LWDTRAASRA
VRTFHGHEGD VNTVKFFPDG YRFGTGSDDG TCRLYDIRTG HQLQVYQPHG DGENGPVTSI
AFSVSGRLLF AGYASNNTCY VWDTLLGEVV LDLGLQQDSH RNRISCLGLS ADGSALCTGS
WDSNLKIWAF GGHRRVI


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CSB-EL009607MO Mouse Guanine nucleotide-binding protein subunit beta-4(GNB4) ELISA kit 96T
CSB-EL009605PI Pig Guanine nucleotide-binding protein subunit beta-2-like 1(GNB2L1) ELISA kit SpeciesPig 96T
CSB-EL009608HU Human Guanine nucleotide-binding protein subunit beta-5(GNB5) ELISA kit 96T
CSB-EL009607HU Human Guanine nucleotide-binding protein subunit beta-4(GNB4) ELISA kit 96T


 

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