YAK1_ARATH
ID YAK1_ARATH Reviewed; 956 AA.
AC Q8RWH3; Q56YT6; Q9FGC1;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Dual specificity protein kinase YAK1 homolog {ECO:0000305};
DE Short=AtYAK1 {ECO:0000303|PubMed:26452715};
DE EC=2.7.12.1 {ECO:0000269|PubMed:26452715};
DE AltName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase YAK1 {ECO:0000305};
GN Name=YAK1 {ECO:0000303|PubMed:26452715};
GN OrderedLocusNames=At5g35980 {ECO:0000312|Araport:AT5G35980};
GN ORFNames=MEE13.9 {ECO:0000312|EMBL:BAB09254.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [6]
RP IDENTIFICATION BY 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 [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, AND
RP PHOSPHORYLATION AT SER-222.
RX PubMed=26452715; DOI=10.1016/j.febslet.2015.09.025;
RA Kim D., Ntui V.O., Zhang N., Xiong L.;
RT "Arabidopsis Yak1 protein (AtYak1) is a dual specificity protein kinase.";
RL FEBS Lett. 589:3321-3327(2015).
RN [8]
RP FUNCTION, INDUCTION BY DROUGHT STRESS, AND DISRUPTION PHENOTYPE.
RX PubMed=27264339; DOI=10.1002/1873-3468.12234;
RA Kim D., Ntui V.O., Xiong L.;
RT "Arabidopsis YAK1 regulates abscisic acid response and drought
RT resistance.";
RL FEBS Lett. 590:2201-2209(2016).
CC -!- FUNCTION: Dual specificity protein kinase that phosphorylates ANN1,
CC ANN2 and CP29B at serine and threonine residues, and ANN1, ANN2 and
CC ANN4 at tyrosine residues. May regulate the phosphorylation status of
CC annexin proteins (PubMed:26452715). Acts as positive regulator in
CC abscisic acid (ABA)-mediated regulation of postgermination growth and
CC drought response. May regulate the expression of ABA-responsive genes
CC such as RD22, RD29A, LTI65/RD29B and RAB18 (PubMed:27264339).
CC {ECO:0000269|PubMed:26452715, ECO:0000269|PubMed:27264339}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC Evidence={ECO:0000269|PubMed:26452715};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.1; Evidence={ECO:0000269|PubMed:26452715};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC Evidence={ECO:0000269|PubMed:26452715};
CC -!- INDUCTION: Induced by drought stress. {ECO:0000269|PubMed:27264339}.
CC -!- PTM: Autophosphorylated at Ser-222. {ECO:0000269|PubMed:26452715}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seedlings exhibit decreased sensitivity to
CC abscisic acid (ABA) inhibition of seed germination, cotyledon greening,
CC seedling growth, and stomatal movement. Decreased tolerance to drought
CC stress. {ECO:0000269|PubMed:27264339}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AED94036.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB09254.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD93822.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD93839.1; Type=Frameshift; Evidence={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; AB026643; BAB09254.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94035.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94036.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY093090; AAM13089.1; -; mRNA.
DR EMBL; BT010549; AAQ65172.1; -; mRNA.
DR EMBL; AK221229; BAD93822.1; ALT_FRAME; mRNA.
DR EMBL; AK221235; BAD93839.1; ALT_FRAME; mRNA.
DR EMBL; AK230350; BAF02149.1; -; mRNA.
DR RefSeq; NP_001031970.1; NM_001036893.2.
DR RefSeq; NP_198447.2; NM_122989.4.
DR AlphaFoldDB; Q8RWH3; -.
DR SMR; Q8RWH3; -.
DR IntAct; Q8RWH3; 5.
DR MINT; Q8RWH3; -.
DR STRING; 3702.AT5G35980.1; -.
DR iPTMnet; Q8RWH3; -.
DR PaxDb; Q8RWH3; -.
DR PRIDE; Q8RWH3; -.
DR ProteomicsDB; 228629; -.
DR EnsemblPlants; AT5G35980.1; AT5G35980.1; AT5G35980.
DR GeneID; 833590; -.
DR Gramene; AT5G35980.1; AT5G35980.1; AT5G35980.
DR KEGG; ath:AT5G35980; -.
DR Araport; AT5G35980; -.
DR TAIR; locus:2162868; AT5G35980.
DR eggNOG; KOG0667; Eukaryota.
DR InParanoid; Q8RWH3; -.
DR OrthoDB; 194243at2759; -.
DR PhylomeDB; Q8RWH3; -.
DR BRENDA; 2.7.12.1; 399.
DR PRO; PR:Q8RWH3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RWH3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:TAIR.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..956
FT /note="Dual specificity protein kinase YAK1 homolog"
FT /id="PRO_0000442107"
FT DOMAIN 122..464
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 620..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 128..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26452715"
SQ SEQUENCE 956 AA; 105523 MW; 45016D7F01E11481 CRC64;
MDDIDSSDGA AAARAGEIGS IGVSTPWKPI QLVFKRYLPQ NGSASKVHVA VKKPVVVRLT
RDLVETYKIC DPQFKYRGEL NPKRYLTTPS VGVNNDGFDN VNYDLILAVN DDFCSSDSRQ
RYIVKDLLGH GTFGQVAKCW VPETNSFVAV KVIKNQLAYY QQALVEVSIL TTLNKKYDPE
DKNHIVRIYD YFLHQSHLCI CFELLDMNLY ELIKINQFRG LSLSIVKLFS KQILLGLALL
KDAGIIHCDL KPENILLCAS VKPTEIKIID FGSACMEDKT VYSYIQSRYY RSPEVLLGYQ
YTTAIDMWSF GCIVAELFLG LPLFPGGSEF DILRRMIEIL GKQPPDYVLK EAKNTNKFFK
CVGSVHNLGN GGTYGGLKSA YMALTGEEFE AREKKKPEIG KEYFNHKNLE EIVKSYPYKI
NLPEDDVVKE TQIRLALIDF LKGLMEFDPA KRWSPFQAAK HPFITGEPFT CPYNPPPETP
RVHVTQNIKV DHHPGEGHWF AAGLSPHVSG RTRIPMHNSP HFQMMPYSHA NSYGSIGSYG
SYNDGTIQDN SYGSYGGTGN MFAYYSPVNH PGLYMQNQGG VSMLGTSPDA RRRVMQYPHG
NGPNGLGTSP SAGNFAPLPL GTSPSQFTPN TNNQFLAGSP GHHGPTSPVR NSCHGSPLGK
MAAFSQINRR MSAGYSGGSQ SQDSSLSQAQ GHGMDNFYQN EGYSGQFSGS PSRRQLDSGV
KNRKQTQGGT TLSTGYSTHN NANSSLRSNM YNPSSTAHHL ENPDTALSVP DPGDWDPNYS
DDLLLEEDSA DESSLANAFS RGMQLGSTDA SSYSRRFNSN ASTSSSNPTT QRRYAPNQAF
SQVETGSPPS NDPHARFGQH IPGSQYIPHV SQNSPSRLGQ QPPQRYNHGR PNAGRTMDRN
HMNAQLPPSN TNSGGQQRSP RSSSYTNGVP WGRRTNNHVP NVPSTSHGRV DYGSIA