KING1_ARATH
ID KING1_ARATH Reviewed; 424 AA.
AC Q8LBB2; Q9S7W6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=SNF1-related protein kinase regulatory subunit gamma-1;
DE Short=AKIN subunit gamma-1;
DE Short=AKING1;
DE Short=AKINgamma1;
DE AltName: Full=CBS domain-containing protein CBSCBS1;
GN Name=KING1; Synonyms=CBSCBS1; OrderedLocusNames=At3g48530;
GN ORFNames=T8P19.40;
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; KINB1 AND KINB2,
RP INDUCTION, TISSUE SPECIFICITY, COMPONENT OF A HETEROTRIMERIC COMPLEX, AND
RP SUBUNIT.
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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 [5]
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 [6]
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 [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19400948; DOI=10.1186/1471-2164-10-200;
RA Kushwaha H.R., Singh A.K., Sopory S.K., Singla-Pareek S.L., Pareek A.;
RT "Genome wide expression analysis of CBS domain containing proteins in
RT Arabidopsis thaliana (L.) Heynh and Oryza sativa L. reveals their
RT developmental and stress regulation.";
RL BMC Genomics 10:200-200(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
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).
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.
CC {ECO:0000269|PubMed:10417704}.
CC -!- TISSUE SPECIFICITY: Expressed in vegetative organs and, to lower
CC extent, in reproductive organs. {ECO:0000269|PubMed:10417704}.
CC -!- INDUCTION: Strongly induced in the dark. {ECO:0000269|PubMed:10417704}.
CC -!- PTM: Sumoylated by SIZ1. {ECO:0000269|PubMed:26662259}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
CC subunit family. {ECO:0000305}.
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DR EMBL; AJ132317; CAB64720.1; -; mRNA.
DR EMBL; AL133315; CAB62342.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78427.1; -; Genomic_DNA.
DR EMBL; AY042839; AAK68779.1; -; mRNA.
DR EMBL; AY081464; AAM10026.1; -; mRNA.
DR EMBL; AY087317; AAM64867.1; -; mRNA.
DR PIR; T46197; T46197.
DR RefSeq; NP_190422.1; NM_114711.2.
DR AlphaFoldDB; Q8LBB2; -.
DR SMR; Q8LBB2; -.
DR BioGRID; 9331; 3.
DR IntAct; Q8LBB2; 3.
DR STRING; 3702.AT3G48530.1; -.
DR iPTMnet; Q8LBB2; -.
DR PaxDb; Q8LBB2; -.
DR PRIDE; Q8LBB2; -.
DR ProteomicsDB; 250693; -.
DR EnsemblPlants; AT3G48530.1; AT3G48530.1; AT3G48530.
DR GeneID; 824012; -.
DR Gramene; AT3G48530.1; AT3G48530.1; AT3G48530.
DR KEGG; ath:AT3G48530; -.
DR Araport; AT3G48530; -.
DR TAIR; locus:2114475; AT3G48530.
DR eggNOG; KOG1764; Eukaryota.
DR HOGENOM; CLU_036145_0_0_1; -.
DR InParanoid; Q8LBB2; -.
DR OMA; VRQQDYK; -.
DR OrthoDB; 1471847at2759; -.
DR PhylomeDB; Q8LBB2; -.
DR PRO; PR:Q8LBB2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LBB2; baseline and differential.
DR Genevisible; Q8LBB2; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019887; F:protein kinase regulator activity; IPI:TAIR.
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; 3.10.580.10; -; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR Pfam; PF00571; CBS; 2.
DR SMART; SM00116; CBS; 4.
DR SUPFAM; SSF54631; SSF54631; 2.
DR PROSITE; PS51371; CBS; 4.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Carbohydrate metabolism; CBS domain;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Nitrate assimilation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9CAR3"
FT CHAIN 2..424
FT /note="SNF1-related protein kinase regulatory subunit
FT gamma-1"
FT /id="PRO_0000204387"
FT DOMAIN 63..131
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 185..244
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 263..324
FT /note="CBS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 350..408
FT /note="CBS 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9CAR3"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT CONFLICT 175
FT /note="K -> E (in Ref. 5; AAM64867)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="D -> E (in Ref. 5; AAM64867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 47423 MW; 3193C4AA9D0BE1DE CRC64;
MATVPEIKIM RSESLGHRSD VSSPEAKLGM RVEDLWDEQK PQLSPNEKLN ACFESIPVSA
FPLSSDSQDI EIRSDTSLAE AVQTLSKFKV LSAPVVDVDA PEDASWIDRY IGIVEFPGIV
VWLLHQLEPP SPRSPAVAAS NGFSHDFTTD VLDNGDSAVT SGNFFEVLTS SELYKNTKVR
DISGTFRWAP FLALQKENSF LTMLLLLSKY KMKSIPVVDL GVAKIENIIT QSGVIHMLAE
CAGLLWFEDW GIKTLSEVGL PIMSKDHIIK IYEDEPVLQA FKLMRRKRIG GIPVIERNSE
KPVGNISLRD VQFLLTAPEI YHDYRSITTK NFLVSVREHL EKCGDTSAPI MSGVIACTKN
HTLKELILML DAEKIHRIYV VDDFGNLEGL ITLRDIIARL VHEPSGYFGD FFDGVMPLPE
NYRV
