2A5G_ARATH
ID 2A5G_ARATH Reviewed; 522 AA.
AC Q8RW96; O04377; O23394;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' gamma isoform;
DE Short=AtB' gamma;
DE Short=PP2A, B' subunit, gamma isoform;
GN Name=B'GAMMA; OrderedLocusNames=At4g15415; ORFNames=dl3750w, FCAALL.118;
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 [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9128737; DOI=10.1111/j.1432-1033.1997.00156.x;
RA Latorre K.A., Harris D.M., Rundle S.J.;
RT "Differential expression of three Arabidopsis genes encoding the B'
RT regulatory subunit of protein phosphatase 2A.";
RL Eur. J. Biochem. 245:156-163(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH PP2AA1.
RX PubMed=10091592; DOI=10.1046/j.1432-1327.1999.00154.x;
RA Haynes J.G., Hartung A.J., Hendershot J.D. III, Passingham R.S.,
RA Rundle S.J.;
RT "Molecular characterization of the B' regulatory subunit gene family of
RT Arabidopsis protein phosphatase 2A.";
RL Eur. J. Biochem. 260:127-136(1999).
RN [8]
RP NOMENCLATURE.
RX PubMed=12068121; DOI=10.1104/pp.020004;
RA Terol J., Bargues M., Carrasco P., Perez-Alonso M., Paricio N.;
RT "Molecular characterization and evolution of the protein phosphatase 2A B'
RT regulatory subunit family in plants.";
RL Plant Physiol. 129:808-822(2002).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=19672620; DOI=10.1007/s00425-009-0998-z;
RA Matre P., Meyer C., Lillo C.;
RT "Diversity in subcellular targeting of the PP2A B'eta subfamily members.";
RL Planta 230:935-945(2009).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21571669; DOI=10.1104/pp.111.178442;
RA Trotta A., Wrzaczek M., Scharte J., Tikkanen M., Konert G., Rahikainen M.,
RA Holmstroem M., Hiltunen H.M., Rips S., Sipari N., Mulo P., Weis E.,
RA von Schaewen A., Aro E.M., Kangasjaervi S.;
RT "Regulatory subunit B'gamma of protein phosphatase 2A prevents unnecessary
RT defense reactions under low light in Arabidopsis.";
RL Plant Physiol. 156:1464-1480(2011).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22041935; DOI=10.4161/psb.6.11.17829;
RA Trotta A., Konert G., Rahikainen M., Aro E.M., Kangasjaervi S.;
RT "Knock-down of protein phosphatase 2A subunit B'gamma promotes
RT phosphorylation of CALRETICULIN 1 in Arabidopsis thaliana.";
RL Plant Signal. Behav. 6:1665-1668(2011).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23976921; DOI=10.1371/journal.pone.0067987;
RA Heidari B., Nemie-Feyissa D., Kangasjarvi S., Lillo C.;
RT "Antagonistic regulation of flowering time through distinct regulatory
RT subunits of protein phosphatase 2A.";
RL PLoS ONE 8:E67987-E67987(2013).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ACO3, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25307043; DOI=10.1111/nph.13097;
RA Konert G., Trotta A., Kouvonen P., Rahikainen M., Durian G., Blokhina O.,
RA Fagerstedt K., Muth D., Corthals G.L., Kangasjaervi S.;
RT "Protein phosphatase 2A (PP2A) regulatory subunit B'gamma interacts with
RT cytoplasmic ACONITASE 3 and modulates the abundance of AOX1A and AOX1D in
RT Arabidopsis thaliana.";
RL New Phytol. 205:1250-1263(2015).
RN [14]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=26012558; DOI=10.1111/pce.12575;
RA Konert G., Rahikainen M., Trotta A., Durian G., Salojaervi J.,
RA Khorobrykh S., Tyystjaervi E., Kangasjaervi S.;
RT "Subunits B'gamma and B'zeta of protein phosphatase 2A regulate photo-
RT oxidative stress responses and growth in Arabidopsis thaliana.";
RL Plant Cell Environ. 38:2641-2651(2015).
RN [15]
RP FUNCTION, INTERACTION WITH BRI1, AND SUBCELLULAR LOCATION.
RX PubMed=26517938; DOI=10.1016/j.molp.2015.10.007;
RA Wang R., Liu M., Yuan M., Oses-Prieto J.A., Cai X., Sun Y.,
RA Burlingame A.L., Wang Z.Y., Tang W.;
RT "The brassinosteroid-activated BRI1 receptor kinase is switched off by
RT dephosphorylation mediated by cytoplasm-localized PP2A B' subunits.";
RL Mol. Plant 9:148-157(2016).
RN [16]
RP FUNCTION, AND INTERACTION WITH IGMT1 AND IGMT4.
RX PubMed=27598402; DOI=10.1111/tpj.13326;
RA Rahikainen M., Trotta A., Alegre S., Pascual J., Vuorinen K., Overmyer K.,
RA Moffatt B., Ravanel S., Glawischnig E., Kangasjaervi S.;
RT "PP2A-B'gamma modulates foliar trans-methylation capacity and the formation
RT of 4-methoxy-indol-3-yl-methyl glucosinolate in Arabidopsis leaves.";
RL Plant J. 89:112-127(2017).
CC -!- FUNCTION: The B regulatory subunit may modulate substrate selectivity
CC and catalytic activity, and also may direct the localization of the
CC catalytic enzyme to a particular subcellular compartment (By
CC similarity). Required for the formation of the PP2A holoenzyme that
CC negatively regulates brassinosteroid signaling by dephosphorylating and
CC inactivating BRI1 in the cytoplasm (PubMed:26517938). Seems to be
CC functionally connected with CPR5 and may mediate the negative
CC regulation of defense reactions and senescence under low irradiances.
CC May contribute to the epigenetic regulation of defense gene expression
CC (PubMed:21571669). Involved in the control of methoxylation of indole
CC glucosinolates and formation of 4-methoxy- indol-3-yl-methyl
CC glucosinolate in leaves, through direct interaction with indole
CC glucosinolate methyltransferases (PubMed:27598402). Involved in growth
CC regulation and stress signaling (PubMed:26012558). Involved in the
CC regulation of reactive oxygen species (ROS) signaling and maintenance
CC of cellular ROS homeostasis (PubMed:26012558, PubMed:25307043).
CC Required to control the level of ACO3 phosphorylation in the cytoplasm.
CC Regulates hydrogen peroxide metabolism by controlling the abundance of
CC AOX1A and AXO3/AOX1D in leaf mitochondria (PubMed:25307043). May
CC mediate dephosphorylation of CRT1 and promote the degradation of
CC unfolded proteins in endoplasmic reticulum (ER) (PubMed:22041935).
CC Involved in the regulation of flowering time by repressing FLC, the
CC main flowering repressor gene (PubMed:23976921).
CC {ECO:0000250|UniProtKB:Q13362, ECO:0000269|PubMed:21571669,
CC ECO:0000269|PubMed:22041935, ECO:0000269|PubMed:23976921,
CC ECO:0000269|PubMed:25307043, ECO:0000269|PubMed:26012558,
CC ECO:0000269|PubMed:26517938, ECO:0000269|PubMed:27598402}.
CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of a
CC catalytic subunit (subunits C), a constant regulatory subunit (subunit
CC A), and a variety of regulatory subunits such as subunits B (the
CC R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families)
CC (Probable). Interacts with BRI1 (PubMed:26517938). Interacts with IGMT1
CC and IGMT4 (PubMed:27598402). Interacts with ACO3 in the cytosol
CC (PubMed:25307043). {ECO:0000269|PubMed:25307043,
CC ECO:0000269|PubMed:26517938, ECO:0000269|PubMed:27598402,
CC ECO:0000305|PubMed:10091592}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19672620,
CC ECO:0000269|PubMed:21571669, ECO:0000269|PubMed:25307043,
CC ECO:0000269|PubMed:26517938}. Nucleus {ECO:0000269|PubMed:19672620}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously at low levels
CC (PubMed:9128737). Expressed in roots, emerging lateral roots,
CC cotyledons, leaves, floral stalks and flowers (PubMed:26012558).
CC {ECO:0000269|PubMed:26012558, ECO:0000269|PubMed:9128737}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:9128737}.
CC -!- DISRUPTION PHENOTYPE: Wrinkled leaves, stunted growth, delayed
CC flowering and formation of age-dependent yellowing lesions
CC (PubMed:21571669, PubMed:22041935, PubMed:23976921). Conditional
CC phenotype with premature yellowing and constitutive reactive oxygen
CC species (ROS) production in distinct peripheral areas of mature leaves
CC when grown under moderate light intensity and low humidity. May
CC partially evade the accumulation of H(2)O(2) via alternative oxidases
CC (AOX) activity. Increased levels of AOX1A and AOX1D in leaf
CC mitochondria. Increased level of ACO3 phosphorylation.
CC {ECO:0000269|PubMed:21571669, ECO:0000269|PubMed:22041935,
CC ECO:0000269|PubMed:23976921, ECO:0000269|PubMed:25307043}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10320.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g15410 has been split into 2 genes: At4g15410 and At4g15415.; Evidence={ECO:0000305};
CC Sequence=CAB78583.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g15410 has been split into 2 genes: At4g15410 and At4g15415.; Evidence={ECO:0000305};
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DR EMBL; U73528; AAB58902.1; -; mRNA.
DR EMBL; Z97338; CAB10320.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161541; CAB78583.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83598.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83599.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66523.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66524.1; -; Genomic_DNA.
DR EMBL; AY093761; AAM10385.1; -; mRNA.
DR EMBL; BT020581; AAW80854.1; -; mRNA.
DR PIR; F71418; F71418.
DR RefSeq; NP_001319948.1; NM_001341040.1.
DR RefSeq; NP_001319949.1; NM_001341039.1.
DR RefSeq; NP_567464.1; NM_117630.3.
DR RefSeq; NP_849390.1; NM_179059.2.
DR AlphaFoldDB; Q8RW96; -.
DR SMR; Q8RW96; -.
DR BioGRID; 12508; 5.
DR STRING; 3702.AT4G15415.2; -.
DR iPTMnet; Q8RW96; -.
DR PaxDb; Q8RW96; -.
DR PRIDE; Q8RW96; -.
DR ProteomicsDB; 245169; -.
DR EnsemblPlants; AT4G15415.1; AT4G15415.1; AT4G15415.
DR EnsemblPlants; AT4G15415.2; AT4G15415.2; AT4G15415.
DR EnsemblPlants; AT4G15415.4; AT4G15415.4; AT4G15415.
DR EnsemblPlants; AT4G15415.5; AT4G15415.5; AT4G15415.
DR GeneID; 827211; -.
DR Gramene; AT4G15415.1; AT4G15415.1; AT4G15415.
DR Gramene; AT4G15415.2; AT4G15415.2; AT4G15415.
DR Gramene; AT4G15415.4; AT4G15415.4; AT4G15415.
DR Gramene; AT4G15415.5; AT4G15415.5; AT4G15415.
DR KEGG; ath:AT4G15415; -.
DR Araport; AT4G15415; -.
DR TAIR; locus:505006470; AT4G15415.
DR eggNOG; KOG2085; Eukaryota.
DR HOGENOM; CLU_012437_4_1_1; -.
DR OMA; HIFLRVI; -.
DR OrthoDB; 890437at2759; -.
DR PhylomeDB; Q8RW96; -.
DR PRO; PR:Q8RW96; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8RW96; baseline and differential.
DR Genevisible; Q8RW96; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:TAIR.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0009759; P:indole glucosinolate biosynthetic process; IMP:TAIR.
DR GO; GO:0006555; P:methionine metabolic process; IMP:TAIR.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:1900056; P:negative regulation of leaf senescence; IMP:TAIR.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:UniProtKB.
DR GO; GO:2000031; P:regulation of salicylic acid mediated signaling pathway; IEP:TAIR.
DR GO; GO:0033353; P:S-adenosylmethionine cycle; IMP:TAIR.
DR GO; GO:0010090; P:trichome morphogenesis; IGI:TAIR.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002554; PP2A_B56.
DR PANTHER; PTHR10257; PTHR10257; 1.
DR Pfam; PF01603; B56; 1.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Brassinosteroid signaling pathway; Cytoplasm; Flowering; Nucleus;
KW Plant defense; Reference proteome; Stress response.
FT CHAIN 1..522
FT /note="Serine/threonine protein phosphatase 2A 59 kDa
FT regulatory subunit B' gamma isoform"
FT /id="PRO_0000071462"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 384
FT /note="F -> L (in Ref. 5; AAM10385)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 59157 MW; AACF6C94287760EA CRC64;
MIKQIFGKLP RKPSKSSHND SNPNGEGGVN SYYIPNSGIS SISKPSSKSS ASNSNGANGT
VIAPSSTSSN RTNQVNGVYE ALPSFRDVPT SEKPNLFIKK LSMCCVVFDF NDPSKNLREK
EIKRQTLLEL VDYIATVSTK LSDAAMQEIA KVAVVNLFRT FPSANHESKI LETLDVDDEE
PALEPAWPHL QVVYELLLRF VASPMTDAKL AKRYIDHSFV LKLLDLFDSE DQREREYLKT
ILHRIYGKFM VHRPFIRKAI NNIFYRFIFE TEKHNGIAEL LEILGSIING FALPLKEEHK
LFLIRALIPL HRPKCASAYH QQLSYCIVQF VEKDFKLADT VIRGLLKYWP VTNSSKEVMF
LGELEEVLEA TQAAEFQRCM VPLFRQIARC LNSSHFQVAE RALFLWNNDH IRNLITQNHK
VIMPIVFPAM ERNTRGHWNQ AVQSLTLNVR KVMAETDQIL FDECLAKFQE DEANETEVVA
KREATWKLLE ELAASKSVSN EAVLVPRFSS SVTLATGKTS GS
