KINB1_ARATH
ID KINB1_ARATH Reviewed; 283 AA.
AC Q84VQ1; Q9SCY6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=SNF1-related protein kinase regulatory subunit beta-1;
DE Short=AKIN subunit beta-1;
DE Short=AKINB1;
DE Short=AKINbeta1;
GN Name=KINB1; OrderedLocusNames=At5g21170; ORFNames=T10F18.200;
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 AKIN11 AND AKING1, 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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP INTERACTION WITH CBL1.
RX PubMed=23437128; DOI=10.1371/journal.pone.0056412;
RA Li Z.Y., Xu Z.S., Chen Y., He G.Y., Yang G.X., Chen M., Li L.C., Ma Y.Z.;
RT "A novel role for Arabidopsis CBL1 in affecting plant responses to glucose
RT and gibberellin during germination and seedling development.";
RL PLoS ONE 8:E56412-E56412(2013).
RN [10]
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 [11]
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 [12]
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 [13]
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 and CBL1. Interacts with FLZ1,
CC FLZ2, FLZ8, FLZ9, FLZ10, FLZ12, FLZ13, FLZ14 and FLZ15
CC (PubMed:29945970). {ECO:0000269|PubMed:10417704,
CC ECO:0000269|PubMed:17028154, ECO:0000269|PubMed:23437128,
CC ECO:0000269|PubMed:25736509, ECO:0000269|PubMed:29945970}.
CC -!- INTERACTION:
CC Q84VQ1; Q944A6: SNF4; NbExp=2; IntAct=EBI-2042415, 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=Q84VQ1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in vegetative organs and, to lower
CC extent, in reproductive organs. {ECO:0000269|PubMed:10417704}.
CC -!- INDUCTION: Rapidly and strongly induced in the dark, quickly repressed
CC by light. {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 by SIZ1. {ECO:0000269|PubMed:26662259}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ132315; CAB64718.1; -; mRNA.
DR EMBL; AC140977; AAO73894.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92944.1; -; Genomic_DNA.
DR EMBL; AY088139; AAM65684.1; -; mRNA.
DR RefSeq; NP_197615.1; NM_122124.4. [Q84VQ1-1]
DR AlphaFoldDB; Q84VQ1; -.
DR SMR; Q84VQ1; -.
DR BioGRID; 17518; 59.
DR IntAct; Q84VQ1; 5.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR iPTMnet; Q84VQ1; -.
DR PRIDE; Q84VQ1; -.
DR ProteomicsDB; 238221; -. [Q84VQ1-1]
DR EnsemblPlants; AT5G21170.1; AT5G21170.1; AT5G21170. [Q84VQ1-1]
DR GeneID; 832243; -.
DR Gramene; AT5G21170.1; AT5G21170.1; AT5G21170. [Q84VQ1-1]
DR KEGG; ath:AT5G21170; -.
DR Araport; AT5G21170; -.
DR HOGENOM; CLU_070949_0_0_1; -.
DR InParanoid; Q84VQ1; -.
DR PhylomeDB; Q84VQ1; -.
DR PRO; PR:Q84VQ1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84VQ1; baseline and differential.
DR Genevisible; Q84VQ1; AT.
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 InterPro; IPR037170; KINB1.
DR PANTHER; PTHR46316; PTHR46316; 1.
DR PANTHER; PTHR46316:SF11; PTHR46316:SF11; 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..283
FT /note="SNF1-related protein kinase regulatory subunit beta-
FT 1"
FT /id="PRO_0000204371"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..178
FT /note="Kinase-interacting sequence (KIS)"
FT REGION 215..283
FT /note="Association with SNF1 complex (ASC)"
FT COMPBIAS 17..31
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 79
FT /note="P -> PS (in Ref. 1; CAB64718 and 4; AAM65684)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="A -> T (in Ref. 1; CAB64718 and 4; AAM65684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 283 AA; 30724 MW; 116B50C319B5DDCA CRC64;
MGNANGKDED AAAGSGGADV TSSSARSNGG DPSARSRHRR PSSDSMSSSP PGSPARSPSP
FLFAPQVPVA PLQRANAPPP NNIQWNQSQR VFDNPPEQGI PTIITWNQGG NDVAVEGSWD
NWRSRKKLQK SGKDHSILFV LPSGIYHYKV IVDGESKYIP DLPFVADEVG NVCNILDVHN
FVPENPESIV EFEAPPSPDH SYGQTLPAAE DYAKEPLAVP PQLHLTLLGT TEETAIATKP
QHVVLNHVFI EQGWTPQSIV ALGLTHRFES KYITVVLYKP LTR
