SIS8_ARATH
ID SIS8_ARATH Reviewed; 1030 AA.
AC Q9C9U5; Q0WM41; Q8L625;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable serine/threonine-protein kinase SIS8 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=MAPKK kinase SIS8 {ECO:0000305};
DE AltName: Full=Protein SUGAR INSENSITIVE 8 {ECO:0000303|PubMed:24320620};
GN Name=SIS8 {ECO:0000303|PubMed:24320620};
GN Synonyms=AT6 {ECO:0000303|PubMed:18299802};
GN OrderedLocusNames=At1g73660 {ECO:0000312|Araport:AT1G73660};
GN ORFNames=F25P22.8 {ECO:0000312|EMBL:AAG52069.1};
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;
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 [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] OF 707-1030.
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 FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18299802; DOI=10.1007/s11103-008-9306-8;
RA Gao L., Xiang C.B.;
RT "The genetic locus At1g73660 encodes a putative MAPKKK and negatively
RT regulates salt tolerance in Arabidopsis.";
RL Plant Mol. Biol. 67:125-134(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, INTERACTION WITH UGT72E1, AND SUBCELLULAR LOCATION.
RX PubMed=24320620; DOI=10.1111/tpj.12404;
RA Huang Y., Li C.Y., Qi Y., Park S., Gibson S.I.;
RT "SIS8, a putative mitogen-activated protein kinase kinase kinase, regulates
RT sugar-resistant seedling development in Arabidopsis.";
RL Plant J. 77:577-588(2014).
CC -!- FUNCTION: Acts as negative regulator of salt tolerance
CC (PubMed:18299802). Mediates sugar response during early seedling
CC development (PubMed:24320620). {ECO:0000269|PubMed:18299802,
CC ECO:0000269|PubMed:24320620}.
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:0000305};
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:0000305};
CC -!- SUBUNIT: Interacts with UGT72E1. {ECO:0000269|PubMed:24320620}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24320620}.
CC Note=Colocalizes with UGT72E1 in the nucleus.
CC {ECO:0000269|PubMed:24320620}.
CC -!- TISSUE SPECIFICITY: Expressed roots, rosette and cauline leaves, and at
CC lower levels in flowers and siliques. {ECO:0000269|PubMed:18299802}.
CC -!- INDUCTION: Down-regulated by salt treatment.
CC {ECO:0000269|PubMed:18299802}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit increased tolerance to salt
CC stress during germination (PubMed:18299802). No visible phenotype under
CC normal growth conditions, but mutant plants display a sugar-resistant
CC seedling development phenotype (PubMed:24320620).
CC {ECO:0000269|PubMed:18299802, ECO:0000269|PubMed:24320620}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC012679; AAG52069.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35494.1; -; Genomic_DNA.
DR EMBL; AY099627; AAM20478.1; -; mRNA.
DR EMBL; AK229991; BAF01815.1; -; mRNA.
DR PIR; F96763; F96763.
DR RefSeq; NP_177507.1; NM_106025.4.
DR AlphaFoldDB; Q9C9U5; -.
DR SMR; Q9C9U5; -.
DR STRING; 3702.AT1G73660.1; -.
DR iPTMnet; Q9C9U5; -.
DR PaxDb; Q9C9U5; -.
DR PRIDE; Q9C9U5; -.
DR ProteomicsDB; 234568; -.
DR EnsemblPlants; AT1G73660.1; AT1G73660.1; AT1G73660.
DR GeneID; 843701; -.
DR Gramene; AT1G73660.1; AT1G73660.1; AT1G73660.
DR KEGG; ath:AT1G73660; -.
DR Araport; AT1G73660; -.
DR TAIR; locus:2027794; AT1G73660.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_006806_1_0_1; -.
DR InParanoid; Q9C9U5; -.
DR OMA; VIHESRN; -.
DR OrthoDB; 126394at2759; -.
DR PhylomeDB; Q9C9U5; -.
DR PRO; PR:Q9C9U5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9U5; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA: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; IBA:GO_Central.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISS:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003903; UIM_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
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; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase.
FT CHAIN 1..1030
FT /note="Probable serine/threonine-protein kinase SIS8"
FT /id="PRO_0000440871"
FT DOMAIN 748..1003
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 44..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 871
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 754..762
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 775
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 103
FT /note="S -> T (in Ref. 3; AAM20478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1030 AA; 112206 MW; 9BD7125FB1DF1B38 CRC64;
MKVKEETLKN LGDGVVLRPV DHCSSIWSMK MNMKNFLKKL HISPNQSDEA EGSISTTKSN
HHKSIDVSSS SSPRSHHSNS PEIKPFSGLS NWLSSVGHRK IPSPPNSFNA KNRAATVDDT
VVVNGSEHVD LGSKDPAVEE ENQIQLALEL SAREDPEATQ IEAIKQFSLG SCAPENSPAE
LIAYRYWNYN CLGYDDKILD GFYDLYGVLN ASSAERIPPL LDLQGTPVSD GVTWEAVLVN
RSGDSNLLRL EQMALDIAAK SRSVSSSGFV NSELVRKLAI LVGDYMGGPV VHPESMLRAW
RSLSYSLKAT LGSMVLPLGS LTIGLARHRA LLFKVLCDSV GVPCRIVKGQ QYTGSEDVAM
NFIKADDGRE YIVDLMGDPG TLIPADAAGL QIDYDESAYS ASPGDNDSIH VASSSNGIES
SYEENTEFRT GEHRSSTKSS GERNQSGGGG DLIVHPNISR EDVKNQKKVE KAPFQNLSSR
PIHSFTHMRS PSWTEGVSSP AAQRMKVKDV SQYMIDAAKE NPRLAQKLHD VLLESGVVAP
PNLFSEVYPQ QLEATVESKN STEAKKERGK DLETTQEGRH QNGFGPVRFL PPLPRVQSKT
NAHDQRDNGK VVSQSDSSHS EASSTEYART VPAAVAAAAV VASSMVAAAA AKSANSDSSP
IELPAAAAAT ATAAAVVATA AAVSRQLELG SNSDGDDGSG GHEPQGSGDS NHGPNSGGER
ISDKSIGNES SKSDCDDVSD CEILWEEITV GERIGLGSYG EVYRGDWHGT EVAVKKFLDQ
DLTGEALEEF RSEVRIMKKL RHPNIVLFMG AVTRPPNLSI VTEFLPRGSL YRLIHRPNNQ
LDERRRLRMA LDAARGMNYL HSCNPMIVHR DLKSPNLLVD KNWVVKVCDF GLSRMKHSTY
LSSKSTAGTA EWMAPEVLRN EPADEKCDVY SYGVILWELF TLQQPWGKMN PMQVVGAVGF
QHRRLDIPDF VDPAIADLIS KCWQTDSKLR PSFAEIMASL KRLQKPVTGS NIPRPVPSSS
SLPTEHEQKD
