ID VIK_ARATH Reviewed; 438 AA. AC Q9XI87; Q56ZU2; Q8S9J9; Q9LMF8; DT 14-DEC-2022, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-SEP-2023, entry version 191. DE RecName: Full=Serine/threonine-protein kinase VIK {ECO:0000305|PubMed:19000166}; DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19000166, ECO:0000269|PubMed:21838775}; DE AltName: Full=VH1-interacting kinase {ECO:0000303|PubMed:21838775}; GN Name=VIK {ECO:0000303|PubMed:21838775}; GN OrderedLocusNames=At1g14000 {ECO:0000312|Araport:AT1G14000}; GN ORFNames=F16A14.22 {ECO:0000312|EMBL:AAF79405.1}, GN F7A19.9 {ECO:0000312|EMBL:AAD39286.1}; 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]. RC STRAIN=cv. Columbia; RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.; RT "Arabidopsis ORF Clones."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 323-438. 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 GENE FAMILY. RX PubMed=12119167; DOI=10.1016/s1360-1385(02)02302-6; RG MAPK group; RT "Mitogen-activated protein kinase cascades in plants: a new nomenclature."; RL Trends Plant Sci. 7:301-308(2002). RN [7] RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, INTERACTION WITH BRL2, RP INDUCTION BY AUXIN, AND TISSUE SPECIFICITY. RX PubMed=19000166; DOI=10.1111/j.1365-313x.2008.03742.x; RA Ceserani T., Trofka A., Gandotra N., Nelson T.; RT "VH1/BRL2 receptor-like kinase interacts with vascular-specific adaptor RT proteins VIT and VIK to influence leaf venation."; RL Plant J. 57:1000-1014(2009). RN [8] RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, INTERACTION WITH RP MSSP1/TMT1, TISSUE SPECIFICITY, INDUCTION BY SALT, AND SUBCELLULAR RP LOCATION. RX PubMed=21838775; DOI=10.1111/j.1365-313x.2011.04739.x; RA Wingenter K., Trentmann O., Winschuh I., Hoermiller I.I., Heyer A.G., RA Reinders J., Schulz A., Geiger D., Hedrich R., Neuhaus H.E.; RT "A member of the mitogen-activated protein 3-kinase family is involved in RT the regulation of plant vacuolar glucose uptake."; RL Plant J. 68:890-900(2011). CC -!- FUNCTION: Serine/threonine protein kinase which may function as an CC adapter protein for BRL2 (PubMed:19000166). Required during vascular CC development for the establishment of vein pattern in foliar organs CC (PubMed:19000166). Mediates MSSP1/TMT1 phosphorylation and activation CC to enhance its carrier activity and consequently vacuolar sugar CC accumulation, particularly in response to cold (PubMed:21838775). CC {ECO:0000269|PubMed:19000166, ECO:0000269|PubMed:21838775}. 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:19000166, ECO:0000269|PubMed:21838775}; 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:19000166, CC ECO:0000269|PubMed:21838775}; CC -!- SUBUNIT: Interacts with BRL2 (PubMed:19000166). Binds to MSSP1/TMT1 at CC the tonoplast (PubMed:21838775). {ECO:0000269|PubMed:19000166, CC ECO:0000269|PubMed:21838775}. CC -!- INTERACTION: CC Q9XI87; Q9ZPS9: BRL2; NbExp=2; IntAct=EBI-2292778, EBI-2292728; CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:21838775}. CC -!- TISSUE SPECIFICITY: Restricted to mature vascular cells CC (PubMed:19000166). Mostly expressed in mature leaves and seeds, and, to CC a lower level, in seedlings, young leaves, flowers and siliques CC (PubMed:21838775). {ECO:0000269|PubMed:19000166, CC ECO:0000269|PubMed:21838775}. CC -!- INDUCTION: Induced by auxin (e.g. IAA) (PubMed:19000166). Accumulates CC in response to salt (NaCl) (PubMed:21838775). CC {ECO:0000269|PubMed:19000166, ECO:0000269|PubMed:21838775}. CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:21838775}. CC -!- DISRUPTION PHENOTYPE: Reduced sensitivity to auxin (e.g. 2,4-D and NPA) CC and brassinosteroids (BRs) associated with altered vein pattern in CC foliar organs (PubMed:19000166). Decreased vacuolar sugar import CC associated with reduced fresh weight when grown on high glucose CC containing medium or in response to cold stress (PubMed:21838775). CC Altered intracellular sugar compartmentation due to altered regulation CC of MSSP1/TMT1 (PubMed:21838775). {ECO:0000269|PubMed:19000166, CC ECO:0000269|PubMed:21838775}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF79405.1; Type=Erroneous gene model prediction; 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; AC007576; AAD39286.1; -; Genomic_DNA. DR EMBL; AC068197; AAF79405.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002684; AEE29097.1; -; Genomic_DNA. DR EMBL; AY075653; AAL77660.1; -; mRNA. DR EMBL; BT026491; ABH04598.1; -; mRNA. DR EMBL; AK220869; BAD94246.1; -; mRNA. DR PIR; C86273; C86273. DR RefSeq; NP_172853.1; NM_101266.4. DR AlphaFoldDB; Q9XI87; -. DR SMR; Q9XI87; -. DR IntAct; Q9XI87; 1. DR STRING; 3702.AT1G14000.1; -. DR iPTMnet; Q9XI87; -. DR PaxDb; Q9XI87; -. DR ProteomicsDB; 187249; -. DR EnsemblPlants; AT1G14000.1; AT1G14000.1; AT1G14000. DR GeneID; 837960; -. DR Gramene; AT1G14000.1; AT1G14000.1; AT1G14000. DR KEGG; ath:AT1G14000; -. DR Araport; AT1G14000; -. DR TAIR; AT1G14000; VIK. DR eggNOG; KOG0192; Eukaryota. DR HOGENOM; CLU_000288_7_35_1; -. DR InParanoid; Q9XI87; -. DR OMA; CWSGDIH; -. DR OrthoDB; 3028364at2759; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9XI87; baseline and differential. DR GO; GO:0005576; C:extracellular region; HDA:TAIR. DR GO; GO:0000325; C:plant-type vacuole; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:UniProtKB. 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:0009734; P:auxin-activated signaling pathway; IMP:TAIR. DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:TAIR. DR GO; GO:0071333; P:cellular response to glucose stimulus; IMP:UniProtKB. DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR. DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; IMP:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB. DR GO; GO:1902074; P:response to salt; IEP:UniProtKB. DR CDD; cd13999; STKc_MAP3K-like; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. 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 PANTHER; PTHR44329:SF273; SERINE/THREONINE-PROTEIN KINASE STY8; 1. DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1. DR Pfam; PF12796; Ank_2; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR PIRSF; PIRSF000654; Integrin-linked_kinase; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00248; ANK; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF48403; Ankyrin repeat; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 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 ANK repeat; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase; KW Vacuole. FT CHAIN 1..438 FT /note="Serine/threonine-protein kinase VIK" FT /id="PRO_0000456810" FT REPEAT 36..65 FT /note="ANK 1" FT /evidence="ECO:0000255" FT REPEAT 70..99 FT /note="ANK 2" FT /evidence="ECO:0000255" FT REPEAT 103..133 FT /note="ANK 3" FT /evidence="ECO:0000255" FT DOMAIN 162..427 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 285 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 168..176 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 189 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT CONFLICT 17 FT /note="A -> V (in Ref. 3; AAL77660)" FT /evidence="ECO:0000305" SQ SEQUENCE 438 AA; 49335 MW; C61F80724E24BBD2 CRC64; MSSDSPAAGD GGEQAAAGTS VPSPSYDKQK EKARVSRTSL ILWHAHQNDA AAVRKLLEED PTLVHARDYD KRTPLHVASL HGWIDVVKCL LEFGADVNAQ DRWKNTPLAD AEGARKQKMI ELLKSHGGLS YGQNGSHFEP KPVPPPIPKK CDWEIEPAEL DFSNAAMIGK GSFGEIVKAY WRGTPVAVKR ILPSLSDDRL VIQDFRHEVD LLVKLRHPNI VQFLGAVTER KPLMLITEYL RGGDLHQYLK EKGGLTPTTA VNFALDIARG MTYLHNEPNV IIHRDLKPRN VLLVNSSADH LKVGDFGLSK LIKVQNSHDV YKMTGETGSY RYMAPEVFKH RRYDKKVDVF SFAMILYEML EGEPPFANHE PYEAAKHVSD GHRPTFRSKG CTPDLRELIV KCWDADMNQR PSFLDILKRL EKIKETLPSD HHWGLFTS //