SIK1_ARATH
ID SIK1_ARATH Reviewed; 836 AA.
AC O24527; Q56WD6; Q56WZ7; Q8VYC1; Q9LQA1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Serine/threonine-protein kinase 1 {ECO:0000303|PubMed:26685188, ECO:0000303|PubMed:30212650};
DE EC=2.7.11.1 {ECO:0000269|PubMed:30212650};
GN Name=SIK1 {ECO:0000303|PubMed:26685188, ECO:0000303|PubMed:30212650};
GN OrderedLocusNames=At1g69220 {ECO:0000312|Araport:AT1G69220};
GN ORFNames=F23O10.20 {ECO:0000312|EMBL:AAG52499.1},
GN F4N2.24 {ECO:0000312|EMBL:AAF27066.1};
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 [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Hypocotyl;
RA Winge P., Brembu T., Bones A.M.;
RT "Cloning of a Arabidopsis thaliana serine/threonine kinase with homology to
RT yeast STE20 and mammalian stress activated kinases.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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] (ISOFORM 2).
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] OF 420-836 (ISOFORM 1/2).
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MOB1A AND MOB1B, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=26685188; DOI=10.1093/jxb/erv538;
RA Xiong J., Cui X., Yuan X., Yu X., Sun J., Gong Q.;
RT "The Hippo/STE20 homolog SIK1 interacts with MOB1 to regulate cell
RT proliferation and cell expansion in Arabidopsis.";
RL J. Exp. Bot. 67:1461-1475(2016).
RN [7]
RP FUNCTION, MUTAGENESIS OF LYS-278 AND ASP-371, DISRUPTION PHENOTYPE,
RP CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND INTERACTION WITH BIK1.
RC STRAIN=cv. Columbia;
RX PubMed=30212650; DOI=10.1016/j.chom.2018.08.007;
RA Zhang M., Chiang Y.-H., Toruno T.Y., Lee D., Ma M., Liang X., Lal N.K.,
RA Lemos M., Lu Y.-J., Ma S., Liu J., Day B., Dinesh-Kumar S.P., Dehesh K.,
RA Dou D., Zhou J.-M., Coaker G.;
RT "The MAP4 Kinase SIK1 Ensures Robust Extracellular ROS Burst and
RT Antibacterial Immunity in Plants.";
RL Cell Host Microbe 24:379.e5-391.e5(2018).
CC -!- FUNCTION: Serine/threonine-protein kinase (PubMed:30212650). Regulates
CC organ size in coordination with MOB1A by modulating cell proliferation
CC and cell expansion, possibly by facilitating cell cycle exit
CC (PubMed:26685188). Positive regulator of the pathogen-associated
CC molecular pattern (PAMP, e.g. flg22)-triggered immunity (PTI) signaling
CC by stabilizing BIK1 and activating RBOHD by phosphorylation to promote
CC the extracellular reactive oxygen species (ROS) burst involved in
CC defense responses to bacterial infection (PubMed:30212650).
CC {ECO:0000269|PubMed:26685188, ECO:0000269|PubMed:30212650}.
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=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:30212650};
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=2.7.11.1; Evidence={ECO:0000269|PubMed:30212650};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P70218};
CC -!- SUBUNIT: Interacts with MOB1A and MOB1B via its N-terminal region at
CC the plasma membrane and in the nucleus (PubMed:26685188). Binds to BIK1
CC to phosphorylate and stabilize it (PubMed:30212650). Interacts with and
CC phosphorylates RBOHD upon flagellin perception to activate it
CC (PubMed:30212650). {ECO:0000269|PubMed:26685188,
CC ECO:0000269|PubMed:30212650}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26685188}.
CC Nucleus {ECO:0000269|PubMed:26685188}. Golgi apparatus, trans-Golgi
CC network {ECO:0000269|PubMed:26685188}. Early endosome
CC {ECO:0000269|PubMed:26685188}. Note=Observed at the plasma membrane and
CC in the nucleus when associated with MOB1A.
CC {ECO:0000269|PubMed:26685188}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O24527-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O24527-2; Sequence=VSP_061351;
CC -!- TISSUE SPECIFICITY: Mostly expressed in mature tissues of roots,
CC shoots, hypocotyls, cotyledons, stems, leaves and flowers, as well as
CC in the shoot apical meristem (SAM). {ECO:0000269|PubMed:26685188}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, observed in the hypocotyls of both
CC etiolated and light-grown plants (PubMed:26685188). Also expressed in
CC the quiescent center and the maturation zone of primary roots
CC (PubMed:26685188). Later present in cotyledons and the first pair of
CC true leaves (PubMed:26685188). Accumulates strongly in mature rosette
CC leaves (PubMed:26685188). Detected in the pollen of opened flowers
CC (PubMed:26685188). Lower levels in dividing tissues (PubMed:26685188).
CC Present in developed vascular tissues, stipules of true leaves, mature
CC trichomes and guard cells (PubMed:26685188).
CC {ECO:0000269|PubMed:26685188}.
CC -!- PTM: Autophosphorylates. {ECO:0000269|PubMed:30212650}.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants with reduced cell numbers,
CC endoreduplication and cell expansion leading to a slow growth
CC (PubMed:26685188, PubMed:30212650). Altered pathogen-associated
CC molecular pattern (PAMP)-triggered immunity (PTI) signaling
CC characterized by a compromised ability to elicit a reactive oxygen
CC species (ROS) burst in response to microbial features (e.g. flg22)
CC (PubMed:30212650). Enhanced resistance to the bacterial pathogen
CC Pseudomonas syringae pv. tomato DC3000 (Pst) due to high levels of
CC salicylic acid (SA) and subsequent constitutive expression of
CC pathogenesis-related genes (e.g. PR1) and associated with reduced
CC jasmonic acid (JA) levels (PubMed:30212650). The double mutant sik1
CC mob1a is arrested at the seedling stage (PubMed:26685188).
CC {ECO:0000269|PubMed:26685188, ECO:0000269|PubMed:30212650}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF27066.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD94209.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U96613; AAB68776.1; -; mRNA.
DR EMBL; AC008262; AAF27066.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC018364; AAG52499.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34896.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34897.1; -; Genomic_DNA.
DR EMBL; AY072199; AAL60020.1; -; mRNA.
DR EMBL; AY133857; AAM91791.1; -; mRNA.
DR EMBL; AK222106; BAD95044.1; -; mRNA.
DR EMBL; AK221882; BAD94209.1; ALT_INIT; mRNA.
DR PIR; B96716; B96716.
DR RefSeq; NP_564955.1; NM_105589.4.
DR AlphaFoldDB; O24527; -.
DR SMR; O24527; -.
DR STRING; 3702.AT1G69220.1; -.
DR PaxDb; O24527; -.
DR PRIDE; O24527; -.
DR ProteomicsDB; 183309; -.
DR ProteomicsDB; 191328; -.
DR EnsemblPlants; AT1G69220.1; AT1G69220.1; AT1G69220. [O24527-1]
DR EnsemblPlants; AT1G69220.2; AT1G69220.2; AT1G69220. [O24527-2]
DR GeneID; 843253; -.
DR Gramene; AT1G69220.1; AT1G69220.1; AT1G69220. [O24527-1]
DR Gramene; AT1G69220.2; AT1G69220.2; AT1G69220. [O24527-2]
DR KEGG; ath:AT1G69220; -.
DR Araport; AT1G69220; -.
DR TAIR; locus:2026459; AT1G69220.
DR eggNOG; KOG0576; Eukaryota.
DR HOGENOM; CLU_008661_0_0_1; -.
DR InParanoid; O24527; -.
DR OMA; ICGEIEM; -.
DR OrthoDB; 967913at2759; -.
DR PhylomeDB; O24527; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O24527; baseline and differential.
DR GO; GO:0005694; C:chromosome; HDA:TAIR.
DR GO; GO:0000775; C:chromosome, centromeric region; HDA:TAIR.
DR GO; GO:0005769; C:early endosome; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; IMP:TAIR.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:TAIR.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; IMP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Developmental protein;
KW Endosome; Golgi apparatus; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..836
FT /note="Serine/threonine-protein kinase 1"
FT /id="PRO_0000454501"
FT DOMAIN 249..503
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 371
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 255..263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10141"
FT VAR_SEQ 229..256
FT /note="SKMSTTSLPDSITREDPTTKYEFLNELG -> R (in isoform 2)"
FT /id="VSP_061351"
FT MUTAGEN 278
FT /note="K->R: Loss of kinase activity leading to a reduced
FT autophosphorylation. Impaired ability to phosphorylate
FT BIK1; when associated with A-371."
FT /evidence="ECO:0000269|PubMed:30212650"
FT MUTAGEN 371
FT /note="D->A: Loss of kinase activity. Impaired ability to
FT phosphorylate BIK1; when associated with R-278."
FT /evidence="ECO:0000269|PubMed:30212650"
SQ SEQUENCE 836 AA; 92722 MW; 805F18FDFA430762 CRC64;
MDHNSPKSRR SRKPEPKPDI YSTFVVHSDS DSDQGRDRDK RKAKPEEDEN VDLYATMVYK
GDSDGEGEED DDDDSMLPPL LKRLPKDFGG GASLDYDDDD GDESGDFGTM IVKTDRSSHS
KKNSPYSSKP RMGVSPRRRA RGGDEESSDE EDEEEDDDDD DGDYGTFVVK SKDKKGKKKD
KEIDMTTMGR AVASMQKSNF GGKTRKLDPS SSSSKLHGED NRKMQQQNSK MSTTSLPDSI
TREDPTTKYE FLNELGKGSY GSVYKARDLK TSEIVAVKVI SLTEGEEGYE EIRGEIEMLQ
QCNHPNVVRY LGSYQGEDYL WIVMEYCGGG SVADLMNVTE EALEEYQIAY ICREALKGLA
YLHSIYKVHR DIKGGNILLT EQGEVKLGDF GVAAQLTRTM SKRNTFIGTP HWMAPEVIQE
NRYDGKVDVW ALGVSAIEMA EGLPPRSSVH PMRVLFMISI EPAPMLEDKE KWSLVFHDFV
AKCLTKEPRL RPTAAEMLKH KFVERCKTGA SAMSPKIEKS RQIRATMALQ AQSVVAPSLE
DTSTLGPKSS EELGITVPSK PPQNSTEAPL TSTLNRQHIT GNTVLAGEGG DFGTMIVHGE
DETEESDSRS QLVREKESSS SQFEGVPREF PGEELPDSWI HDKKKPPAID LPVEASISQS
MQASSSHEHR TKLHNIAGTQ MEGGSDASGS TLKNETVGRK AFALQDKLWS IYAAGNTVPI
PFLRATDISP IALLSENMIG GMQQDGNGTV AVEALQELFT SSDPQSKKGR RGQNEMPLPP
SVYQRLTTSS SLMNLAQVLA YHRACYEEMP LQELQATQEQ QTIQNLCDTL RTILRL
