ID KIN11_ARATH Reviewed; 512 AA.
AC P92958; A6XGQ9; P92968; Q3E7R4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 01-MAY-2013, entry version 106.
DE RecName: Full=SNF1-related protein kinase catalytic subunit alpha KIN11;
DE Short=AKIN11;
DE EC=2.7.11.1;
DE AltName: Full=AKIN alpha-1;
DE Short=AKINalpha1;
GN Name=KIN11; Synonyms=SNF1, SNRK1.2; OrderedLocusNames=At3g29160;
GN ORFNames=MXE2.16;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH AKINB1; AKINB2 AND
RP AKING1, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
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
RT interact with AKINalpha1, an SNF1-like protein kinase.";
RL Plant J. 18:541-550(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AUTOPHOSPHORYLATION,
RP AND INTERACTION WITH PRL1.
RX PubMed=10220464; DOI=10.1073/pnas.96.9.5322;
RA Bhalerao R.P., Salchert K., Bako L., Oekresz L., Szabados L.,
RA Muranaka T., Machida Y., Schell J., Koncz C.;
RT "Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like
RT protein kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:5322-5327(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Fu H.;
RT "Functional differentiation of ubiquitin-interacting factors from
RT Arabidopsis.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [6]
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.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP INTERACTION WITH SNF4.
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
RT screening for heterologous multicopy suppressors of snf4 deficiency in
RT yeast.";
RL Plant J. 23:115-122(2000).
RN [8]
RP FUNCTION, AND INTERACTION WITH SKP1 AND PAD1.
RX PubMed=11387208; DOI=10.1093/emboj/20.11.2742;
RA Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A.,
RA Salchert K., del Pozo C., Schell J., Koncz C.;
RT "SKP1-SnRK protein kinase interactions mediate proteasomal binding of
RT a plant SCF ubiquitin ligase.";
RL EMBO J. 20:2742-2756(2001).
RN [9]
RP INTERACTION WITH KINB2.
RX PubMed=11522840; DOI=10.1093/nar/29.17.3685;
RA Ferrando A., Koncz-Kalman Z., Farras R., Tiburcio A., Schell J.,
RA 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 [10]
RP INTERACTION WITH DSP4.
RX PubMed=12148529; DOI=10.1046/j.1365-313X.2002.01250.x;
RA Fordham-Skelton A.P., Chilley P., Lumbreras V., Reignoux S.,
RA Fenton T.R., Dahm C.C., Pages M., Gatehouse J.A.;
RT "A novel higher plant protein tyrosine phosphatase interacts with
RT SNF1-related protein kinases via a KIS (kinase interaction sequence)
RT domain.";
RL Plant J. 29:705-715(2002).
RN [11]
RP INTERACTION WITH TOMATO GOLDEN MOSAIC VIRUS AL2 AND BEET CURLY TOP
RP VIRUS L2, AND ENZYME REGULATION.
RX PubMed=12671096; DOI=10.1105/tpc.009530;
RA Hao L., Wang H., Sunter G., Bisaro D.M.;
RT "Geminivirus AL2 and L2 proteins interact with and inactivate SNF1
RT kinase.";
RL Plant Cell 15:1034-1048(2003).
RN [12]
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
RT in yeast and mammals non-catalytic beta-subunits.";
RL Plant Mol. Biol. 56:747-759(2004).
RN [13]
RP PHOSPHORYLATION AT THR-176, AND ENZYME REGULATION.
RX PubMed=19339507; DOI=10.1104/pp.108.132787;
RA Shen W., Reyes M.I., Hanley-Bowdoin L.;
RT "Arabidopsis protein kinases GRIK1 and GRIK2 specifically activate
RT SnRK1 by phosphorylating its activation loop.";
RL Plant Physiol. 150:996-1005(2009).
CC -!- FUNCTION: Catalytic 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
CC in the regulation of fatty acid synthesis by phosphorylation of
CC acetyl-CoA carboxylase and in assimilation of nitrogen by
CC phosphorylating nitrate reductase. In vitro, KIN11 exhibits kinase
CC activity on sucrose phosphate synthase and the kinase activity is
CC inhibited by PRL1. May be a subunit of a SCF ubiquitin ligase
CC complex and thus be involved in proteasomal ubiquitination.
CC Involved in innate antiviral defenses.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- ENZYME REGULATION: Inactivated by the begomovirus AL2 protein or
CC the curtovirus L2 protein. Activated by phosphorylation at Thr-
CC 176.
CC -!- SUBUNIT: Subunit of a probable heterotrimeric complex consisting
CC of an alpha catalytic (KIN10 or KIN11) subunit, and a beta (KINB)
CC and a gamma (KING or SNF4) non-catalytic regulatory subunits.
CC Interacts with KINB2, KINB3, SNF4 and probably with KINB1 and
CC KING1. Interacts with SKP1/ASK1, PAD1 and the N-terminus of PRL1.
CC Potential subunit of a SCF ubiquitin ligase complex consisting of
CC a SNF1-related protein kinase, SKP1 and CUL1. The association of
CC the SCF complex with the proteasome may be mediated by PAD1 and
CC seems to be inhibited by the interaction with PRL1. Interacts with
CC DSP4. Interacts with the begomovirus AL2 protein and the
CC curtovirus L2 protein.
CC -!- INTERACTION:
CC Q9FEB5:DSP4; NbExp=2; IntAct=EBI-307202, EBI-307215;
CC Q9SCY5:KINB2; NbExp=4; IntAct=EBI-307202, EBI-2042436;
CC Q42384:PRL1; NbExp=2; IntAct=EBI-307202, EBI-1382964;
CC Q9LVG2:TOE2; NbExp=2; IntAct=EBI-307202, EBI-4424568;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P92958-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P92958-2; Sequence=VSP_034567, VSP_034568;
CC Note=Derived from EST data. No experimental confirmation
CC available;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, flower buds,
CC flowers, siliques and leaves.
CC -!- INDUCTION: Induced by sucrose.
CC -!- PTM: Autophosphorylated. Phosphorylated at Thr-176 by GRIK1/SNAK2
CC and GRIK2/SNAK1.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC Ser/Thr protein kinase family. SNF1 subfamily.
CC -!- SIMILARITY: Contains 1 KA1 (kinase-associated) domain.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC URL="http://plantsp.genomics.purdue.edu/family/class.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X94755; CAA64382.1; -; mRNA.
DR EMBL; X99279; CAA67671.1; -; mRNA.
DR EMBL; DQ778956; ABH11526.1; -; mRNA.
DR EMBL; AB018121; BAB01993.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77542.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77543.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77544.1; -; Genomic_DNA.
DR EMBL; AY070468; AAL49934.1; -; mRNA.
DR EMBL; AY149927; AAN31081.1; -; mRNA.
DR IPI; IPI00523787; -.
DR IPI; IPI00548800; -.
DR PIR; T52633; T52633.
DR RefSeq; NP_566843.1; NM_113839.3.
DR RefSeq; NP_974374.1; NM_202645.2.
DR RefSeq; NP_974375.1; NM_202646.1.
DR UniGene; At.184; -.
DR ProteinModelPortal; P92958; -.
DR SMR; P92958; 19-492.
DR IntAct; P92958; 30.
DR STRING; 3702.AT3G29160.2-P; -.
DR PRIDE; P92958; -.
DR EnsemblPlants; AT3G29160.1; AT3G29160.1; AT3G29160.
DR EnsemblPlants; AT3G29160.2; AT3G29160.2; AT3G29160.
DR GeneID; 822566; -.
DR KEGG; ath:AT3G29160; -.
DR TAIR; At3g29160; -.
DR HOGENOM; HOG000233016; -.
DR InParanoid; P92958; -.
DR OMA; PREIMNE; -.
DR PhylomeDB; P92958; -.
DR ProtClustDB; CLSN2688899; -.
DR ArrayExpress; P92958; -.
DR Genevestigator; P92958; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; 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 GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.
DR InterPro; IPR001772; KA1_dom.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_cat_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF103243; Kinase-assoc_KA1; 1.
DR SUPFAM; SSF56112; Kinase_like; 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral protein; ATP-binding;
KW Carbohydrate metabolism; Complete proteome; Fatty acid biosynthesis;
KW Fatty acid metabolism; Host-virus interaction; Kinase;
KW Lipid biosynthesis; Lipid metabolism; Nitrate assimilation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation pathway.
FT CHAIN 1 512 SNF1-related protein kinase catalytic
FT subunit alpha KIN11.
FT /FTId=PRO_0000086129.
FT DOMAIN 20 272 Protein kinase.
FT DOMAIN 293 333 UBA.
FT DOMAIN 463 511 KA1.
FT NP_BIND 26 34 ATP (By similarity).
FT REGION 399 512 Interaction with PAD1 and SKP1.
FT ACT_SITE 143 143 Proton acceptor (By similarity).
FT BINDING 49 49 ATP (By similarity).
FT MOD_RES 176 176 Phosphothreonine; by GRIK1 or GRIK2.
FT VAR_SEQ 352 359 DSGSNPMR -> WFQSYAHT (in isoform 2).
FT /FTId=VSP_034567.
FT VAR_SEQ 360 512 Missing (in isoform 2).
FT /FTId=VSP_034568.
FT CONFLICT 291 291 A -> T (in Ref. 1; CAA64382).
SQ SEQUENCE 512 AA; 58690 MW; 4FBEF55D3EC60F87 CRC64;
MDHSSNRFGN NGVESILPNY KLGKTLGIGS FGKVKIAEHV VTGHKVAIKI LNRRKIKNME
MEEKVRREIK ILRLFMHPHI IRQYEVIETT SDIYVVMEYV KSGELFDYIV EKGRLQEDEA
RNFFQQIISG VEYCHRNMVV HRDLKPENLL LDSRCNIKIA DFGLSNVMRD GHFLKTSCGS
PNYAAPEVIS GKLYAGPEVD VWSCGVILYA LLCGTLPFDD ENIPNLFKKI KGGIYTLPSH
LSSEARDLIP RMLIVDPVKR ITIPEIRQHR WFQTHLPRYL AVSPPDTVEQ AKKINEEIVQ
EVVNMGFDRN QVLESLRNRT QNDATVTYYL LLDNRFRVPS GYLESEFQET TDSGSNPMRT
PEAGASPVGH WIPAHVDHYG LGARSQVPVD RKWALGLQSH AHPREIMNEV LKALQELNVC
WKKIGHYNMK CRWVPGLADG QNTMVNNQLH FRDESSIIED DCAMTSPTVI KFELQLYKAR
EEKYLLDIQR VNGPQFLFLD LCAAFLTELR VI
//
