UNCL_ARATH
ID UNCL_ARATH Reviewed; 408 AA.
AC Q9LT38;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Serine/threonine-protein kinase UCNL {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9SYB9};
DE AltName: Full=AGC serine/threonine-protein kinase subfamily 2 member 4 {ECO:0000303|PubMed:13678909};
DE AltName: Full=Protein UNICORN-LIKE {ECO:0000303|PubMed:22927420};
GN Name=UCNL {ECO:0000303|PubMed:22927420};
GN Synonyms=AGC2-4 {ECO:0000303|PubMed:13678909};
GN OrderedLocusNames=At3g20830 {ECO:0000312|Araport:AT3G20830};
GN ORFNames=MOE17.14 {ECO:0000312|EMBL:BAB02491.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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;
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 [4]
RP GENE FAMILY.
RX PubMed=13678909; DOI=10.1016/s1360-1385(03)00188-2;
RA Boegre L., Okresz L., Henriques R., Anthony R.G.;
RT "Growth signalling pathways in Arabidopsis and the AGC protein kinases.";
RL Trends Plant Sci. 8:424-431(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22927420; DOI=10.1073/pnas.1205089109;
RA Enugutti B., Kirchhelle C., Oelschner M., Torres Ruiz R.A., Schliebner I.,
RA Leister D., Schneitz K.;
RT "Regulation of planar growth by the Arabidopsis AGC protein kinase
RT UNICORN.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:15060-15065(2012).
CC -!- FUNCTION: Regulates planar ovule integument development.
CC {ECO:0000269|PubMed:22927420}.
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:0000250|UniProtKB:Q9SYB9};
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:0000250|UniProtKB:Q9SYB9};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22927420}. Nucleus
CC {ECO:0000269|PubMed:22927420}.
CC -!- TISSUE SPECIFICITY: Expressed in the epidermis and cortex of the
CC transition zone of the root apex. Expressed in rosette leaves, stems,
CC flowers and siliques. {ECO:0000269|PubMed:22927420}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutants ucn-2 and ucnl-5 are embryonic
CC lethal. {ECO:0000269|PubMed:22927420}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AB025629; BAB02491.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76429.1; -; Genomic_DNA.
DR EMBL; BT026453; ABH04560.1; -; mRNA.
DR RefSeq; NP_188719.1; NM_112974.3.
DR AlphaFoldDB; Q9LT38; -.
DR SMR; Q9LT38; -.
DR BioGRID; 6963; 1.
DR STRING; 3702.AT3G20830.1; -.
DR PaxDb; Q9LT38; -.
DR PRIDE; Q9LT38; -.
DR ProteomicsDB; 245275; -.
DR EnsemblPlants; AT3G20830.1; AT3G20830.1; AT3G20830.
DR GeneID; 821631; -.
DR Gramene; AT3G20830.1; AT3G20830.1; AT3G20830.
DR KEGG; ath:AT3G20830; -.
DR Araport; AT3G20830; -.
DR TAIR; locus:2091881; AT3G20830.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; Q9LT38; -.
DR OMA; RNFSRWI; -.
DR OrthoDB; 856721at2759; -.
DR PhylomeDB; Q9LT38; -.
DR PRO; PR:Q9LT38; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LT38; baseline and differential.
DR Genevisible; Q9LT38; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS:TAIR.
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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR000961; AGC-kinase_C.
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 Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..408
FT /note="Serine/threonine-protein kinase UCNL"
FT /id="PRO_0000430953"
FT DOMAIN 21..341
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 342..408
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 408 AA; 45889 MW; 2B10DAF014A6714E CRC64;
MEPSPSSPPS SPPEILDLDS IKALKILGKG ATGTVFLAHD VVSTSSSSSP FAVKLVPKSS
ASSLRRARWE IEVLRRLSVD SNQNPFLPRL LASFESPEYF AWAVPYCSGG DLNVLLHRQN
DGVFSSSVIR FYVAEIVCAL EHLHTMGIAY RDLKPENILI QQSGHVTLTD FDLSRSLKKP
LRPHFYQPDP ELIIDRKKSR SFSRLISPTA EKNKTGLKKT RSARVNPINR RKTSFSSGER
SNSFVGTDEY VSPEVIRGDG HDFAVDWWAL GVLTYEMMYG ETPFKGKSKK ETFRNVLMKE
PEFAGKPNDL TDLIRRLLVK DPNRRLGCHR GAAEIKELAF FAGVRWDLLT EVLRPPFIPL
RDDGELTVGG FDIREHFEKL RTTPSSAPPS PLRSPPHVCR KNDPFIEF
