HMDH1_ARATH
ID HMDH1_ARATH Reviewed; 592 AA.
AC P14891; Q6RW12;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 {ECO:0000303|PubMed:7588795, ECO:0000303|PubMed:8302869};
DE Short=AtHMGR1 {ECO:0000303|PubMed:7588795, ECO:0000303|PubMed:8302869};
DE Short=HMG-CoA reductase 1 {ECO:0000303|PubMed:7588795, ECO:0000303|PubMed:8302869};
DE EC=1.1.1.34 {ECO:0000255|PROSITE-ProRule:PRU10003};
GN Name=HMG1 {ECO:0000303|PubMed:2491679, ECO:0000303|PubMed:2649893,
GN ECO:0000303|PubMed:7496400};
GN Synonyms=HMGR1 {ECO:0000303|PubMed:7588795, ECO:0000303|PubMed:8302869};
GN OrderedLocusNames=At1g76490 {ECO:0000312|Araport:AT1G76490};
GN ORFNames=F14G6.9 {ECO:0000312|EMBL:AAG51957.1},
GN F15M4.1 {ECO:0000312|EMBL:AAF16652.1};
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 SHORT).
RC STRAIN=cv. Columbia;
RX PubMed=2491679; DOI=10.1007/bf00016018;
RA Caelles C., Ferrer A., Balcells L., Hegardt F.G., Boronat A.;
RT "Isolation and structural characterization of a cDNA encoding Arabidopsis
RT thaliana 3-hydroxy-3-methylglutaryl coenzyme A reductase.";
RL Plant Mol. Biol. 13:627-638(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=2649893; DOI=10.1073/pnas.86.8.2779;
RA Learned R.M., Fink G.R.;
RT "3-hydroxy-3-methylglutaryl-coenzyme A reductase from Arabidopsis thaliana
RT is structurally distinct from the yeast and animal enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2779-2783(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM LONG), TISSUE
RP SPECIFICITY, AND ALTERNATIVE INITIATION.
RX PubMed=7496400; DOI=10.1046/j.1365-313x.1995.8040541.x;
RA Lumbreras V., Campos N., Boronat A.;
RT "The use of an alternative promoter in the Arabidopsis thaliana HMG1 gene
RT generates an mRNA that encodes a novel 3-hydroxy-3-methylglutaryl coenzyme
RT A reductase isoform with an extended N-terminal region.";
RL Plant J. 8:541-549(1995).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
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 [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8302869; DOI=10.1073/pnas.91.3.927;
RA Enjuto M., Balcells L., Campos N., Caelles C., Arro M., Boronat A.;
RT "Arabidopsis thaliana contains two differentially expressed 3-hydroxy-3-
RT methylglutaryl-CoA reductase genes, which encode microsomal forms of the
RT enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:927-931(1994).
RN [8]
RP PROTEIN SEQUENCE OF 573-586, ACTIVITY REGULATION, AND PHOSPHORYLATION AT
RP SER-577.
RX PubMed=7588795; DOI=10.1111/j.1432-1033.1995.506_2.x;
RA Dale S., Arro M., Becerra B., Morrice N.G., Boronat A., Hardie D.G.,
RA Ferrer A.;
RT "Bacterial expression of the catalytic domain of 3-hydroxy-3-
RT methylglutaryl-CoA reductase (isoform HMGR1) from Arabidopsis thaliana, and
RT its inactivation by phosphorylation at Ser577 by Brassica oleracea 3-
RT hydroxy-3-methylglutaryl-CoA reductase kinase.";
RL Eur. J. Biochem. 233:506-513(1995).
RN [9]
RP PROTEIN SEQUENCE OF 573-586, ACTIVITY REGULATION, AND PHOSPHORYLATION AT
RP SER-577.
RX PubMed=10318703; DOI=10.1104/pp.120.1.257;
RA Sugden C., Donaghy P.G., Halford N.G., Hardie D.G.;
RT "Two SNF1-related protein kinases from spinach leaf phosphorylate and
RT inactivate 3-hydroxy-3-methylglutaryl-coenzyme A reductase, nitrate
RT reductase, and sucrose phosphate synthase in vitro.";
RL Plant Physiol. 120:257-274(1999).
RN [10]
RP INDUCTION BY LIGHT.
RX PubMed=8742338; DOI=10.1104/pp.110.2.645;
RA Learned R.M.;
RT "Light suppresses 3-Hydroxy-3-methylglutaryl coenzyme A reductase gene
RT expression in Arabidopsis thaliana.";
RL Plant Physiol. 110:645-655(1996).
RN [11]
RP INDUCTION BY LIGHT.
RX PubMed=9107038; DOI=10.1046/j.1365-313x.1997.11030499.x;
RA Learned R.M., Connolly E.L.;
RT "Light modulates the spatial patterns of 3-hydroxy-3-methylglutaryl
RT coenzyme A reductase gene expression in Arabidopsis thaliana.";
RL Plant J. 11:499-511(1997).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14871314; DOI=10.1111/j.1365-313x.2004.02003.x;
RA Suzuki M., Kamide Y., Nagata N., Seki H., Ohyama K., Kato H., Masuda K.,
RA Sato S., Kato T., Tabata S., Yoshida S., Muranaka T.;
RT "Loss of function of 3-hydroxy-3-methylglutaryl coenzyme A reductase 1
RT (HMG1) in Arabidopsis leads to dwarfing, early senescence and male
RT sterility, and reduced sterol levels.";
RL Plant J. 37:750-761(2004).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=15618432; DOI=10.1104/pp.104.050245;
RA Leivar P., Gonzalez V.M., Castel S., Trelease R.N., Lopez-Iglesias C.,
RA Arro M., Boronat A., Campos N., Ferrer A., Fernandez-Busquets X.;
RT "Subcellular localization of Arabidopsis 3-hydroxy-3-methylglutaryl-
RT coenzyme A reductase.";
RL Plant Physiol. 137:57-69(2005).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17917299; DOI=10.1248/cpb.55.1518;
RA Ohyama K., Suzuki M., Masuda K., Yoshida S., Muranaka T.;
RT "Chemical phenotypes of the hmg1 and hmg2 mutants of Arabidopsis
RT demonstrate the in-planta role of HMG-CoA reductase in triterpene
RT biosynthesis.";
RL Chem. Pharm. Bull. 55:1518-1521(2007).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19363204; DOI=10.1093/jxb/erp073;
RA Suzuki M., Nakagawa S., Kamide Y., Kobayashi K., Ohyama K.,
RA Hashinokuchi H., Kiuchi R., Saito K., Muranaka T., Nagata N.;
RT "Complete blockage of the mevalonate pathway results in male gametophyte
RT lethality.";
RL J. Exp. Bot. 60:2055-2064(2009).
RN [16]
RP FUNCTION, ACTIVITY REGULATION, AND INDUCTION.
RX PubMed=19041104; DOI=10.1016/j.phytochem.2008.10.010;
RA Nieto B., Fores O., Arro M., Ferrer A.;
RT "Arabidopsis 3-hydroxy-3-methylglutaryl-CoA reductase is regulated at the
RT post-translational level in response to alterations of the sphingolipid and
RT the sterol biosynthetic pathways.";
RL Phytochemistry 70:53-59(2009).
RN [17]
RP INTERACTION WITH B''ALPHA AND B''BETA, AND ACTIVITY REGULATION.
RX PubMed=21478440; DOI=10.1105/tpc.110.074278;
RA Leivar P., Antolin-Llovera M., Ferrero S., Closa M., Arro M., Ferrer A.,
RA Boronat A., Campos N.;
RT "Multilevel control of Arabidopsis 3-hydroxy-3-methylglutaryl coenzyme A
RT reductase by protein phosphatase 2A.";
RL Plant Cell 23:1494-1511(2011).
RN [18]
RP ACTIVITY REGULATION.
RX PubMed=23404890; DOI=10.1105/tpc.112.108696;
RA Doblas V.G., Amorim-Silva V., Pose D., Rosado A., Esteban A., Arro M.,
RA Azevedo H., Bombarely A., Borsani O., Valpuesta V., Ferrer A.,
RA Tavares R.M., Botella M.A.;
RT "The SUD1 gene encodes a putative E3 ubiquitin ligase and is a positive
RT regulator of 3-hydroxy-3-methylglutaryl coenzyme a reductase activity in
RT Arabidopsis.";
RL Plant Cell 25:728-743(2013).
RN [19]
RP ACTIVITY REGULATION, PHOSPHORYLATION AT SER-577, AND MUTAGENESIS OF
RP SER-577.
RX PubMed=28263378; DOI=10.1002/1873-3468.12618;
RA Robertlee J., Kobayashi K., Suzuki M., Muranaka T.;
RT "AKIN10, a representative Arabidopsis SNF1-related protein kinase 1
RT (SnRK1), phosphorylates and downregulates plant HMG-CoA reductase.";
RL FEBS Lett. 591:1159-1166(2017).
CC -!- FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor
CC of all isoprenoid compounds present in plants.
CC {ECO:0000269|PubMed:14871314, ECO:0000269|PubMed:17917299,
CC ECO:0000269|PubMed:19041104, ECO:0000269|PubMed:19363204}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-
CC methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10003};
CC -!- ACTIVITY REGULATION: Regulated at the post-translational level in
CC response to alterations of sphingolipid and sterol biosynthetic
CC pathways. Negatively regulated by a PP2A-dependent dephosphorylation
CC occurring at a site different than Ser-577. Completely inhibited by
CC mevinolin (IC(50) = 12.5 nM). Reversibly inactivated by phosphorylation
CC at Ser-577 by spinach or Brassica oleracea HMGR kinases in a cell-free
CC system (PubMed:7588795, PubMed:10318703). Down-regulated by KIN10
CC through its phosphorylation at Ser-577 (PubMed:28263378).
CC {ECO:0000269|PubMed:10318703, ECO:0000269|PubMed:19041104,
CC ECO:0000269|PubMed:21478440, ECO:0000269|PubMed:23404890,
CC ECO:0000269|PubMed:28263378, ECO:0000269|PubMed:7588795}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
CC -!- SUBUNIT: Interacts (via N-terminus) with B''ALPHA and B''BETA.
CC {ECO:0000269|PubMed:21478440}.
CC -!- SUBCELLULAR LOCATION: [Isoform Short]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15618432, ECO:0000269|PubMed:8302869}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Also observed within spherical
CC structures located along the endoplasmic reticulum strands.
CC {ECO:0000269|PubMed:15618432, ECO:0000269|PubMed:8302869}.
CC -!- SUBCELLULAR LOCATION: [Isoform Long]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15618432}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Short; Synonyms=HMGR1S {ECO:0000303|PubMed:15618432};
CC IsoId=P14891-1; Sequence=Displayed;
CC Name=Long; Synonyms=HMGR1L {ECO:0000303|PubMed:15618432};
CC IsoId=P14891-2; Sequence=VSP_041282;
CC -!- TISSUE SPECIFICITY: Found in all tissues. Isoform Short is expressed at
CC low levels specifically in flowers. Expressed in both the tapetum and
CC microspores. {ECO:0000269|PubMed:19363204, ECO:0000269|PubMed:7496400,
CC ECO:0000269|PubMed:8302869}.
CC -!- INDUCTION: Down-regulated by light in immature leaves, but not in
CC roots. Not regulated by myriocin, squalestatin or terbinafine.
CC {ECO:0000269|PubMed:19041104, ECO:0000269|PubMed:8742338,
CC ECO:0000269|PubMed:9107038}.
CC -!- DOMAIN: The N-terminal domain (1-178) of the short isoform is necessary
CC and sufficient for directing the protein to the endoplasmic reticulum
CC and to spherical structures.
CC -!- PTM: Inactivated by phosphorylation at Ser-577 by KIN10 activated form
CC (PubMed:28263378). Probably also phosphorylated at additional sites
CC (PubMed:7588795, PubMed:10318703). {ECO:0000269|PubMed:10318703,
CC ECO:0000269|PubMed:28263378, ECO:0000269|PubMed:7588795}.
CC -!- DISRUPTION PHENOTYPE: Dwarfing, early senescence, and sterility. 65%
CC lower levels in triterpenoids content and 50% lower levels in sterol
CC content. Hmg1 and hmg2 double mutants are lethal during male
CC gametophyte development. {ECO:0000269|PubMed:14871314,
CC ECO:0000269|PubMed:17917299, ECO:0000269|PubMed:19363204}.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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DR EMBL; X15032; CAA33139.1; -; mRNA.
DR EMBL; J04537; AAA76821.1; -; mRNA.
DR EMBL; L19261; AAA32814.1; -; Genomic_DNA.
DR EMBL; AY488113; AAR83122.1; -; mRNA.
DR EMBL; AC012394; AAF16652.1; -; Genomic_DNA.
DR EMBL; AC015450; AAG51957.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35849.1; -; Genomic_DNA.
DR EMBL; AF385690; AAK60283.1; -; mRNA.
DR EMBL; BT000703; AAN31847.1; -; mRNA.
DR EMBL; BT010468; AAQ65091.1; -; mRNA.
DR PIR; A32107; A32107.
DR RefSeq; NP_177775.2; NM_106299.4. [P14891-2]
DR AlphaFoldDB; P14891; -.
DR SMR; P14891; -.
DR STRING; 3702.AT1G76490.1; -.
DR iPTMnet; P14891; -.
DR PaxDb; P14891; -.
DR PRIDE; P14891; -.
DR ProteomicsDB; 232099; -. [P14891-1]
DR EnsemblPlants; AT1G76490.1; AT1G76490.1; AT1G76490. [P14891-2]
DR GeneID; 843982; -.
DR Gramene; AT1G76490.1; AT1G76490.1; AT1G76490. [P14891-2]
DR KEGG; ath:AT1G76490; -.
DR Araport; AT1G76490; -.
DR TAIR; locus:2011656; AT1G76490.
DR eggNOG; KOG2480; Eukaryota.
DR HOGENOM; CLU_001734_2_2_1; -.
DR InParanoid; P14891; -.
DR OMA; KSPIPDP; -.
DR OrthoDB; 907394at2759; -.
DR PhylomeDB; P14891; -.
DR BioCyc; ARA:AT1G76490-MON; -.
DR BioCyc; MetaCyc:AT1G76490-MON; -.
DR BRENDA; 1.1.1.34; 399.
DR UniPathway; UPA00058; UER00103.
DR PRO; PR:P14891; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P14891; baseline and differential.
DR Genevisible; P14891; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IDA:TAIR.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; ISS:TAIR.
DR GO; GO:0016126; P:sterol biosynthetic process; IMP:TAIR.
DR CDD; cd00643; HMG-CoA_reductase_classI; 1.
DR Gene3D; 1.10.3270.10; -; 1.
DR Gene3D; 3.30.70.420; -; 1.
DR Gene3D; 3.90.770.10; -; 1.
DR InterPro; IPR002202; HMG_CoA_Rdtase.
DR InterPro; IPR023074; HMG_CoA_Rdtase_cat_sf.
DR InterPro; IPR023076; HMG_CoA_Rdtase_CS.
DR InterPro; IPR004554; HMG_CoA_Rdtase_eu_arc.
DR InterPro; IPR023282; HMG_CoA_Rdtase_N.
DR InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_sf.
DR InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom_sf.
DR PANTHER; PTHR10572; PTHR10572; 1.
DR Pfam; PF00368; HMG-CoA_red; 1.
DR PRINTS; PR00071; HMGCOARDTASE.
DR SUPFAM; SSF55035; SSF55035; 1.
DR SUPFAM; SSF56542; SSF56542; 1.
DR TIGRFAMs; TIGR00533; HMG_CoA_R_NADP; 1.
DR PROSITE; PS00066; HMG_COA_REDUCTASE_1; 1.
DR PROSITE; PS00318; HMG_COA_REDUCTASE_2; 1.
DR PROSITE; PS01192; HMG_COA_REDUCTASE_3; 1.
DR PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Isoprene biosynthesis; Membrane; NADP; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..592
FT /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase 1"
FT /id="PRO_0000114433"
FT TRANSMEM 47..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..171
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 172..592
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT COMPBIAS 10..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 265
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 397
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 473
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 571
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10318703,
FT ECO:0000269|PubMed:28263378, ECO:0000269|PubMed:7588795"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MKKKQAGPQQTCEFVSYKTLLISPSHLSRHLTTSLLSPLSPPWRDYS
FT FPPM (in isoform Long)"
FT /evidence="ECO:0000303|PubMed:7496400"
FT /id="VSP_041282"
FT MUTAGEN 577
FT /note="S->A: Abolishes the inactivation of activity by
FT KIN10."
FT /evidence="ECO:0000269|PubMed:28263378"
SQ SEQUENCE 592 AA; 63598 MW; 7EE10127460D3573 CRC64;
MDLRRRPPKP PVTNNNNSNG SFRSYQPRTS DDDHRRRATT IAPPPKASDA LPLPLYLTNA
VFFTLFFSVA YYLLHRWRDK IRYNTPLHVV TITELGAIIA LIASFIYLLG FFGIDFVQSF
ISRASGDAWD LADTIDDDDH RLVTCSPPTP IVSVAKLPNP EPIVTESLPE EDEEIVKSVI
DGVIPSYSLE SRLGDCKRAA SIRREALQRV TGRSIEGLPL DGFDYESILG QCCEMPVGYI
QIPVGIAGPL LLDGYEYSVP MATTEGCLVA STNRGCKAMF ISGGATSTVL KDGMTRAPVV
RFASARRASE LKFFLENPEN FDTLAVVFNR SSRFARLQSV KCTIAGKNAY VRFCCSTGDA
MGMNMVSKGV QNVLEYLTDD FPDMDVIGIS GNFCSDKKPA AVNWIEGRGK SVVCEAVIRG
EIVNKVLKTS VAALVELNML KNLAGSAVAG SLGGFNAHAS NIVSAVFIAT GQDPAQNVES
SQCITMMEAI NDGKDIHISV TMPSIEVGTV GGGTQLASQS ACLNLLGVKG ASTESPGMNA
RRLATIVAGA VLAGELSLMS AIAAGQLVRS HMKYNRSSRD ISGATTTTTT TT
