KINB2_ARATH
ID KINB2_ARATH Reviewed; 289 AA.
AC Q9SCY5; F4JLS7; O23481;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=SNF1-related protein kinase regulatory subunit beta-2;
DE Short=AKIN subunit beta-2;
DE Short=AKINB2;
DE Short=AKINbeta2;
GN Name=KINB2; OrderedLocusNames=At4g16360; ORFNames=dl4210w, FCAALL.163;
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], INTERACTION WITH KIN11 AND KING1, INDUCTION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10417704; DOI=10.1046/j.1365-313x.1999.00476.x;
RA Bouly J.-P., Gissot L., Lessard P., Kreis M., Thomas M.;
RT "Arabidopsis thaliana proteins related to the yeast SIP and SNF4 interact
RT with AKINalpha1, an SNF1-like protein kinase.";
RL Plant J. 18:541-550(1999).
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].
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP DOMAIN KIS.
RX PubMed=11252725; DOI=10.1093/embo-reports/kve001;
RA Lumbreras V., Alba M.M., Kleinow T., Koncz C., Pages M.;
RT "Domain fusion between SNF1-related kinase subunits during plant
RT evolution.";
RL EMBO Rep. 2:55-60(2001).
RN [8]
RP INTERACTION WITH KIN10 AND KIN11.
RX PubMed=11522840; DOI=10.1093/nar/29.17.3685;
RA Ferrando A., Koncz-Kalman Z., Farras R., Tiburcio A., Schell J., Koncz C.;
RT "Detection of in vivo protein interactions between Snf1-related kinase
RT subunits with intron-tagged epitope-labelling in plants cells.";
RL Nucleic Acids Res. 29:3685-3693(2001).
RN [9]
RP INTERACTION WITH SNF4, COMPONENT OF A HETEROTRIMERIC COMPLEX, AND SUBUNIT.
RX PubMed=17028154; DOI=10.1104/pp.106.087718;
RA Gissot L., Polge C., Jossier M., Girin T., Bouly J.-P., Kreis M.,
RA Thomas M.;
RT "AKINbetagamma contributes to SnRK1 heterotrimeric complexes and interacts
RT with two proteins implicated in plant pathogen resistance through its
RT KIS/GBD sequence.";
RL Plant Physiol. 142:931-944(2006).
RN [10]
RP MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2, AND SUBCELLULAR LOCATION.
RX PubMed=17827350; DOI=10.1105/tpc.107.051870;
RA Pierre M., Traverso J.A., Boisson B., Domenichini S., Bouchez D.,
RA Giglione C., Meinnel T.;
RT "N-myristoylation regulates the SnRK1 pathway in Arabidopsis.";
RL Plant Cell 19:2804-2821(2007).
RN [11]
RP REVIEW.
RX PubMed=17166759; DOI=10.1016/j.tplants.2006.11.005;
RA Polge C., Thomas M.;
RT "SNF1/AMPK/SnRK1 kinases, global regulators at the heart of energy
RT control?";
RL Trends Plant Sci. 12:20-28(2007).
RN [12]
RP COMPONENT OF A HETEROTRIMERIC COMPLEX, AND SUBUNIT.
RX PubMed=25736509; DOI=10.1111/tpj.12813;
RA Emanuelle S., Hossain M.I., Moller I.E., Pedersen H.L., van de Meene A.M.,
RA Doblin M.S., Koay A., Oakhill J.S., Scott J.W., Willats W.G., Kemp B.E.,
RA Bacic A., Gooley P.R., Stapleton D.I.;
RT "SnRK1 from Arabidopsis thaliana is an atypical AMPK.";
RL Plant J. 82:183-192(2015).
RN [13]
RP REVIEW.
RX PubMed=27812990; DOI=10.1007/978-3-319-43589-3_17;
RA Margalha L., Valerio C., Baena-Gonzalez E.;
RT "Plant SnRK1 kinases: structure, regulation, and function.";
RL EXS 107:403-438(2016).
RN [14]
RP SUMOYLATION.
RX PubMed=26662259; DOI=10.1111/tpj.13096;
RA Crozet P., Margalha L., Butowt R., Fernandes N., Elias C.A., Orosa B.,
RA Tomanov K., Teige M., Bachmair A., Sadanandom A., Baena-Gonzalez E.;
RT "SUMOylation represses SnRK1 signaling in Arabidopsis.";
RL Plant J. 85:120-133(2016).
RN [15]
RP INTERACTION WITH FLZ PROTEINS.
RX PubMed=29945970; DOI=10.1074/jbc.ra118.002073;
RA Jamsheer K M., Shukla B.N., Jindal S., Gopan N., Mannully C.T., Laxmi A.;
RT "The FCS-like zinc finger scaffold of the kinase SnRK1 is formed by the
RT coordinated actions of the FLZ domain and intrinsically disordered
RT regions.";
RL J. Biol. Chem. 293:13134-13150(2018).
CC -!- FUNCTION: Regulatory subunit of the probable trimeric SNF1-related
CC protein kinase (SnRK) complex, which may play a role in a signal
CC transduction cascade regulating gene expression and carbohydrate
CC metabolism in higher plants. The SnRK complex may also be involved in
CC the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA
CC carboxylase and in assimilation of nitrogen by phosphorylating nitrate
CC reductase.
CC -!- SUBUNIT: Subunit of a probable heterotrimeric complex consisting of an
CC alpha catalytic (KIN10 or KIN11) subunit, and a beta (KINB) and a gamma
CC (KING or SNF4) non-catalytic regulatory subunits (PubMed:17028154,
CC PubMed:25736509). Interacts with SNF4. Interacts with FLZ1, FLZ2, FLZ8,
CC FLZ9, FLZ10, FLZ12, FLZ13 and FLZ14 (PubMed:29945970).
CC {ECO:0000269|PubMed:10417704, ECO:0000269|PubMed:11522840,
CC ECO:0000269|PubMed:17028154, ECO:0000269|PubMed:25736509,
CC ECO:0000269|PubMed:29945970}.
CC -!- INTERACTION:
CC Q9SCY5; Q38997: KIN10; NbExp=3; IntAct=EBI-2042436, EBI-2107143;
CC Q9SCY5; P92958: KIN11; NbExp=4; IntAct=EBI-2042436, EBI-307202;
CC Q9SCY5; Q944A6: SNF4; NbExp=3; IntAct=EBI-2042436, EBI-2360649;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17827350}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SCY5-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, roots, flower buds and
CC flowers. Not detectable in siliques. {ECO:0000269|PubMed:10417704}.
CC -!- INDUCTION: Repressed in the dark. {ECO:0000269|PubMed:10417704}.
CC -!- DOMAIN: Kinase-interacting sequence (KIS) is specific for the alpha
CC catalytic subunit interaction and Association with SNF1 Complex (ASC)
CC is specific for the gamma non-catalytic regulatory subunit interaction.
CC {ECO:0000269|PubMed:11252725}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:26662259}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10413.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB78678.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ132316; CAB64719.1; -; mRNA.
DR EMBL; Z97341; CAB10413.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL161543; CAB78678.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP002687; AEE83735.2; -; Genomic_DNA.
DR EMBL; AF360248; AAK25958.1; -; mRNA.
DR EMBL; BT020423; AAW28550.1; -; mRNA.
DR PIR; C71430; C71430.
DR RefSeq; NP_193369.3; NM_117731.7.
DR AlphaFoldDB; Q9SCY5; -.
DR SMR; Q9SCY5; -.
DR BioGRID; 12624; 58.
DR IntAct; Q9SCY5; 7.
DR STRING; 3702.AT4G16360.3; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR iPTMnet; Q9SCY5; -.
DR PaxDb; Q9SCY5; -.
DR PeptideAtlas; Q9SCY5; -.
DR PRIDE; Q9SCY5; -.
DR ProteomicsDB; 237090; -. [Q9SCY5-1]
DR GeneID; 827331; -.
DR KEGG; ath:AT4G16360; -.
DR Araport; AT4G16360; -.
DR eggNOG; KOG1616; Eukaryota.
DR InParanoid; Q9SCY5; -.
DR OrthoDB; 956412at2759; -.
DR PhylomeDB; Q9SCY5; -.
DR PRO; PR:Q9SCY5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SCY5; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProt.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR006828; ASC_dom.
DR InterPro; IPR037256; ASC_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR043554; KINB.
DR PANTHER; PTHR46316; PTHR46316; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR Pfam; PF04739; AMPKBI; 1.
DR SMART; SM01010; AMPKBI; 1.
DR SUPFAM; SSF160219; SSF160219; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Carbohydrate metabolism; Cell membrane;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Lipoprotein; Membrane; Myristate; Nitrate assimilation;
KW Nucleotide-binding; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17827350"
FT CHAIN 2..289
FT /note="SNF1-related protein kinase regulatory subunit beta-
FT 2"
FT /id="PRO_0000204372"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..180
FT /note="Kinase-interacting sequence (KIS)"
FT REGION 217..289
FT /note="Association with SNF1 complex (ASC)"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:17827350"
FT MUTAGEN 2
FT /note="G->A: Loss of plasma membrane localization."
FT /evidence="ECO:0000269|PubMed:17827350"
FT CONFLICT 7..10
FT /note="REEA -> KENR (in Ref. 3; AEE83735)"
FT /evidence="ECO:0000305"
FT CONFLICT 7..10
FT /note="REEA -> KRKP (in Ref. 2; CAB10413 and 3; CAB78678)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="E -> D (in Ref. 2; CAB10413 and 3; CAB78678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 31993 MW; FF76EAD739E0CEBB CRC64;
MGNVNAREEA NSNNASAVED EDAEICSREA MSAASDGNHV APPELMGQSP PHSPRATQSP
LMFAPQVPVL PLQRPDEIHI PNPSWMQSPS SLYEEASNEQ GIPTMITWCH GGKEIAVEGS
WDNWKTRSRL QRSGKDFTIM KVLPSGVYEY RFIVDGQWRH APELPLARDD AGNTFNILDL
QDYVPEDIQS ISGFEPPQSP ENSYSNLLLG AEDYSKEPPV VPPHLQMTLL NLPAANPDIP
SPLPRPQHVI LNHLYMQKGK SGPSVVALGS THRFLAKYVT VVLYKSLQR
