KIN12_ARATH
ID KIN12_ARATH Reviewed; 494 AA.
AC Q9FLZ3; Q9ZRA0;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=SNF1-related protein kinase catalytic subunit alpha KIN12 {ECO:0000305};
DE Short=AKIN12 {ECO:0000303|PubMed:10220464};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=AKIN alpha-3 {ECO:0000305};
DE Short=AKINalpha3 {ECO:0000305};
DE AltName: Full=SNF1-related kinase 1.3 {ECO:0000303|PubMed:12805596};
DE Short=SnRK1.3 {ECO:0000303|PubMed:12805596};
GN Name=KIN12 {ECO:0000303|PubMed:17671505};
GN Synonyms=AKIN12 {ECO:0000303|PubMed:10220464},
GN KIN30 {ECO:0000303|PubMed:12805596}, SNRK1.3 {ECO:0000303|PubMed:12805596};
GN OrderedLocusNames=At5g39440 {ECO:0000312|Araport:AT5G39440};
GN ORFNames=MUL8.12 {ECO:0000312|EMBL:BAB11017.1};
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 [GENOMIC DNA] OF 1-291.
RC STRAIN=cv. Columbia;
RA Lessard P., Petit-Jean X., Bouly J.P., Kreis M., Thomas M.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12805596; DOI=10.1104/pp.102.011999;
RA Hrabak E.M., Chan C.W.M., Gribskov M., Harper J.F., Choi J.H., Halford N.,
RA Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M., Walker-Simmons K.,
RA Zhu J.-K., Harmon A.C.;
RT "The Arabidopsis CDPK-SnRK superfamily of protein kinases.";
RL Plant Physiol. 132:666-680(2003).
RN [5]
RP IDENTIFICATION.
RX PubMed=10220464; DOI=10.1073/pnas.96.9.5322;
RA Bhalerao R.P., Salchert K., Bako L., Oekresz L., Szabados L., Muranaka T.,
RA Machida Y., Schell J., Koncz C.;
RT "Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like
RT protein kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:5322-5327(1999).
RN [6]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=17671505; DOI=10.1038/nature06069;
RA Baena-Gonzalez E., Rolland F., Thevelein J.M., Sheen J.;
RT "A central integrator of transcription networks in plant stress and energy
RT signalling.";
RL Nature 448:938-942(2007).
RN [7]
RP REVIEW.
RX PubMed=17166759; DOI=10.1016/j.tplants.2006.11.005;
RA Polge C., Thomas M.;
RT "SNF1/AMPK/SnRK1 kinases, global regulators at the heart of energy
RT control?";
RL Trends Plant Sci. 12:20-28(2007).
CC -!- FUNCTION: Catalytic subunit of the probable trimeric SNF1-related
CC protein kinase (SnRK) complex, a central regulator of cellular energy
CC homeostasis, which, in response to seemingly unrelated darkness, sugar
CC and stress conditions, activates energy-producing pathways and inhibits
CC energy-consuming processes. May also be involved in the regulation of
CC fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase and
CC in assimilation of nitrogen by phosphorylating nitrate reductase.
CC {ECO:0000250|UniProtKB:Q38997}.
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 -!- ACTIVITY REGULATION: Activated by phosphorylation at Thr-175.
CC {ECO:0000250|UniProtKB:Q38997}.
CC -!- SUBUNIT: Subunit of a probable heterotrimeric complex consisting of an
CC alpha catalytic subunit, and a beta (KINB) and a gamma (KING or SNF4)
CC non-catalytic regulatory subunits. {ECO:0000250|UniProtKB:Q38997}.
CC -!- TISSUE SPECIFICITY: Expressed at very low levels.
CC {ECO:0000269|PubMed:17671505}.
CC -!- DOMAIN: The regulatory domain (RD) contains the auto-inhibitory domain
CC (AID) that inhibits kinase activity of the protein kinase domain (KD).
CC {ECO:0000250|UniProtKB:Q38997}.
CC -!- DOMAIN: The PPI motif mediates the interaction with the ABI (abscisic
CC acid-insensitive) phosphatases. {ECO:0000250|UniProtKB:Q38997}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q38997}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {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; U83177; AAD00542.1; -; Genomic_DNA.
DR EMBL; AB009054; BAB11017.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94433.1; -; Genomic_DNA.
DR RefSeq; NP_198760.1; NM_123306.1.
DR AlphaFoldDB; Q9FLZ3; -.
DR SMR; Q9FLZ3; -.
DR STRING; 3702.AT5G39440.1; -.
DR iPTMnet; Q9FLZ3; -.
DR PaxDb; Q9FLZ3; -.
DR PRIDE; Q9FLZ3; -.
DR EnsemblPlants; AT5G39440.1; AT5G39440.1; AT5G39440.
DR GeneID; 833940; -.
DR Gramene; AT5G39440.1; AT5G39440.1; AT5G39440.
DR KEGG; ath:AT5G39440; -.
DR Araport; AT5G39440; -.
DR TAIR; locus:2175663; AT5G39440.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_3_1; -.
DR InParanoid; Q9FLZ3; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q9FLZ3; -.
DR PRO; PR:Q9FLZ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLZ3; baseline and differential.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
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 InterPro; IPR015940; UBA.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF103243; SSF103243; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..494
FT /note="SNF1-related protein kinase catalytic subunit alpha
FT KIN12"
FT /id="PRO_0000445491"
FT DOMAIN 19..270
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 291..331
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 445..493
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 289..386
FT /note="Auto-inhibitory domain (AID)"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT REGION 293..494
FT /note="Regulatory domain (RD)"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT REGION 387..494
FT /note="PPI"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 25..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 175
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
SQ SEQUENCE 494 AA; 56696 MW; C8E5618DCE6EA259 CRC64;
MDGSSEKTTN KLVSILPNYR IGKTLGHGSF AKVKLALHVA TGHKVAIKIL NRSKIKNMGI
EIKVQREIKI LRFLMHPHII RQYEVIETPN DIYVVMEYVK SGELFDYIVE KGKLQEDEAR
HLFQQIISGV EYCHRNMIVH RDLKPENVLL DSQCNIKIVD FGLSNVMHDG HFLKTSCGSP
NYAAPEVISG KPYGPDVDIW SCGVILYALL CGTLPFDDEN IPNVFEKIKR GMYTLPNHLS
HFARDLIPRM LMVDPTMRIS ITEIRQHPWF NNHLPLYLSI PPLDTIDQAK KIEEEIIQNV
VNIGFDRNHV VDSLANRIQN EATVAYHLIL DNRNQNSVPN DPFQSKFKEI SDGIFNSTLP
VQNITSHVGH SFSALYGLKS NVKDDKTWTL GLQSQGSPYD IMTEIFKALQ NLKICWKKIG
LYNIKCRWVR SFAYYKNHTI EDECAIILPT VIKFEIQLYK VREGKYLLDI LRIDGPQFIF
FDLCVAFLRE LGVL
