SNF4_ARATH
ID SNF4_ARATH Reviewed; 487 AA.
AC Q944A6; O04028; Q2QCL5; Q9FV59;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Sucrose nonfermenting 4-like protein;
DE Short=SNF4;
DE AltName: Full=CBS domain-containing protein CBSCBS3;
DE AltName: Full=SNF1-related protein kinase regulatory subunit betagamma;
DE Short=AKIN subunit betagamma;
DE Short=AKINbetagamma;
GN Name=SNF4; Synonyms=CBSCBS3; OrderedLocusNames=At1g09020;
GN ORFNames=F7G19.11;
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] (ISOFORM 1), INTERACTION WITH KIN10 AND KIN11,
RP AND TISSUE SPECIFICITY.
RX PubMed=10929106; DOI=10.1046/j.1365-313x.2000.00809.x;
RA Kleinow T., Bhalerao R., Breuer F., Umeda M., Salchert K., Koncz C.;
RT "Functional identification of an Arabidopsis Snf4 ortholog by screening for
RT heterologous multicopy suppressors of snf4 deficiency in yeast.";
RL Plant J. 23:115-122(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
RP INTERACTION WITH KIN10; KIN11; KINB1; KINB2; KINB3; HSPRO1 AND HSPRO2,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, COMPONENT OF A HETEROTRIMERIC
RP 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] (ISOFORM 1).
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 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 [7]
RP INTERACTION WITH KINB3.
RX PubMed=15803412; DOI=10.1007/s11103-004-5111-1;
RA Gissot L., Polge C., Bouly J.P., Lemaitre T., Kreis M., Thomas M.;
RT "AKINbeta3, a plant specific SnRK1 protein, is lacking domains present in
RT yeast and mammals non-catalytic beta-subunits.";
RL Plant Mol. Biol. 56:747-759(2004).
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 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 [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH KIN10.
RX PubMed=21235649; DOI=10.1111/j.1365-313x.2010.04462.x;
RA Bitrian M., Roodbarkelari F., Horvath M., Koncz C.;
RT "BAC-recombineering for studying plant gene regulation: developmental
RT control and cellular localization of SnRK1 kinase subunits.";
RL Plant J. 65:829-842(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH BZIP63.
RX PubMed=26263501; DOI=10.7554/elife.05828;
RA Mair A., Pedrotti L., Wurzinger B., Anrather D., Simeunovic A., Weiste C.,
RA Valerio C., Dietrich K., Kirchler T., Naegele T., Vicente Carbajosa J.,
RA Hanson J., Baena-Gonzalez E., Chaban C., Weckwerth W., Droege-Laser W.,
RA Teige M.;
RT "SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy
RT response in plants.";
RL Elife 4:0-0(2015).
RN [13]
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 [14]
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 [15]
RP INTERACTION WITH FLZ2; FLZ8 AND FLZ13.
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.
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 KIN10, KIN11, KINB1, KINB2, KINB3,
CC HSPRO1 AND HSPRO2. Interacts with BZIP63 (PubMed:26263501). Interacts
CC with FLZ2, FLZ8 and FLZ13 (PubMed:29945970).
CC {ECO:0000269|PubMed:10929106, ECO:0000269|PubMed:15803412,
CC ECO:0000269|PubMed:17028154, ECO:0000269|PubMed:21235649,
CC ECO:0000269|PubMed:25736509, ECO:0000269|PubMed:26263501,
CC ECO:0000269|PubMed:29945970}.
CC -!- INTERACTION:
CC Q944A6; F4HZY9: CINV1; NbExp=2; IntAct=EBI-2360649, EBI-2355385;
CC Q944A6; O04203: HSPRO2; NbExp=3; IntAct=EBI-2360649, EBI-1153953;
CC Q944A6; Q38997: KIN10; NbExp=2; IntAct=EBI-2360649, EBI-2107143;
CC Q944A6; Q84VQ1: KINB1; NbExp=2; IntAct=EBI-2360649, EBI-2042415;
CC Q944A6; Q9SCY5: KINB2; NbExp=3; IntAct=EBI-2360649, EBI-2042436;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17028154,
CC ECO:0000269|PubMed:21235649}. Cytoplasm {ECO:0000269|PubMed:17028154,
CC ECO:0000269|PubMed:21235649}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AKINbetagamma;
CC IsoId=Q944A6-1; Sequence=Displayed;
CC Name=2; Synonyms=AKINbetagammaI;
CC IsoId=Q944A6-2; Sequence=VSP_041656, VSP_041657;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in dividing cells, as well
CC as in shoot apex and flower buds, but expressed at a lower level in
CC differentiated tissues of roots, and leaves of rosette and
CC inflorescence. {ECO:0000269|PubMed:10929106,
CC ECO:0000269|PubMed:17028154}.
CC -!- DOMAIN: Kinase-interacting sequence (KIS) is required for interaction
CC with KIN10 or KIN11. {ECO:0000269|PubMed:11252725}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
CC subunit family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70406.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG10141.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF250335; AAG10141.1; ALT_INIT; mRNA.
DR EMBL; DQ132632; ABA12450.1; -; mRNA.
DR EMBL; DQ132633; ABA12451.1; -; mRNA.
DR EMBL; AC000106; AAB70406.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28383.1; -; Genomic_DNA.
DR EMBL; AF439826; AAL27498.1; -; mRNA.
DR EMBL; BT000625; AAN18191.1; -; mRNA.
DR PIR; B86222; B86222.
DR RefSeq; NP_563834.1; NM_100773.4. [Q944A6-1]
DR AlphaFoldDB; Q944A6; -.
DR SMR; Q944A6; -.
DR BioGRID; 22664; 67.
DR IntAct; Q944A6; 9.
DR STRING; 3702.AT1G09020.1; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR iPTMnet; Q944A6; -.
DR PaxDb; Q944A6; -.
DR PRIDE; Q944A6; -.
DR ProteomicsDB; 232545; -. [Q944A6-1]
DR EnsemblPlants; AT1G09020.1; AT1G09020.1; AT1G09020. [Q944A6-1]
DR GeneID; 837423; -.
DR Gramene; AT1G09020.1; AT1G09020.1; AT1G09020. [Q944A6-1]
DR KEGG; ath:AT1G09020; -.
DR Araport; AT1G09020; -.
DR TAIR; locus:2036079; AT1G09020.
DR eggNOG; KOG1616; Eukaryota.
DR eggNOG; KOG1764; Eukaryota.
DR HOGENOM; CLU_021740_7_1_1; -.
DR InParanoid; Q944A6; -.
DR OMA; ACVKMLE; -.
DR PhylomeDB; Q944A6; -.
DR PRO; PR:Q944A6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q944A6; baseline and differential.
DR Genevisible; Q944A6; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009569; C:chloroplast starch grain; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:1901982; F:maltose binding; IDA:TAIR.
DR GO; GO:0030295; F:protein kinase activator activity; ISS:TAIR.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0019887; F:protein kinase regulator activity; IDA:TAIR.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; HDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:TAIR.
DR GO; GO:0000266; P:mitochondrial fission; IMP:TAIR.
DR GO; GO:0016559; P:peroxisome fission; IMP:TAIR.
DR GO; GO:0009859; P:pollen hydration; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; IBA:GO_Central.
DR GO; GO:0045859; P:regulation of protein kinase activity; IPI:TAIR.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:TAIR.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.580.10; -; 2.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR Pfam; PF00571; CBS; 2.
DR SMART; SM00116; CBS; 3.
DR SUPFAM; SSF54631; SSF54631; 2.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51371; CBS; 4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Carbohydrate metabolism; CBS domain;
KW Cytoplasm; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..487
FT /note="Sucrose nonfermenting 4-like protein"
FT /id="PRO_0000412195"
FT DOMAIN 165..227
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 260..324
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 350..408
FT /note="CBS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 432..487
FT /note="CBS 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 22..101
FT /note="Kinase-interacting sequence (KIS)"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 394
FT /note="S -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17028154"
FT /id="VSP_041656"
FT VAR_SEQ 395..487
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17028154"
FT /id="VSP_041657"
SQ SEQUENCE 487 AA; 53466 MW; 4545FE3BF2C4EBEC CRC64;
MFGSTLDSSR GNSAASGQLL TPTRFVWPYG GRRVFLSGSF TRWTEHVPMS PLEGCPTVFQ
VICNLTPGYH QYKFFVDGEW RHDEHQPFVS GNGGVVNTIF ITGPDMVPAG FSPETLGRSN
MDVDDVFLRT ADPSQEAVPR MSGVDLELSR HRISVLLSTR TAYELLPESG KVIALDVNLP
VKQAFHILYE QGIPLAPLWD FGKGQFVGVL GPLDFILILR ELGTHGSNLT EEELETHTIA
AWKEGKAHIS RQYDGSGRPY PRPLVQVGPY DNLKDVALKI LQNKVAAVPV IYSSLQDGSY
PQLLHLASLS GILKCICRYF RHSSSSLPIL QQPICSIPLG TWVPRIGESS SKPLATLRPH
ASLGSALALL VQAEVSSIPV VDDNDSLIDI YSRSDITALA KDKAYAQIHL DDMTVHQALQ
LGQDASPPYG IFNGQRCHMC LRSDSLVKVM ERLANPGVRR LVIVEAGSKR VEGIISLSDV
FQFLLGL
