UNC_ARATH
ID UNC_ARATH Reviewed; 404 AA.
AC Q9SYB9;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Serine/threonine-protein kinase UCN {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:22927420};
DE AltName: Full=AGC serine/threonine-protein kinase subfamily 2 member 3 {ECO:0000303|PubMed:13678909};
DE AltName: Full=Protein UNICORN {ECO:0000303|PubMed:22927420};
GN Name=UNC {ECO:0000303|PubMed:22927420};
GN Synonyms=AGC2-3 {ECO:0000303|PubMed:13678909};
GN OrderedLocusNames=At1g51170 {ECO:0000312|Araport:AT1G51170,
GN ECO:0000312|EMBL:AEE32630.1};
GN ORFNames=F11M15.3 {ECO:0000312|EMBL:AAD30630.1},
GN F23H24.1 {ECO:0000312|EMBL:AAG50535.1};
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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-55
RP AND GLY-165, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
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 by suppressing
CC aberrantly oriented growth. Maintains planar growth of integuments by
CC repressing the developmental regulator and transcription factor KAN4
CC which is involved in the control of early integument growth and
CC polarity. Restricts growth in stamen filaments, petals, and cotyledons.
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:0000269|PubMed:22927420};
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:22927420};
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 and developing flowers. Expressed in
CC rosette leaves, stems and siliques. {ECO:0000269|PubMed:22927420}.
CC -!- DISRUPTION PHENOTYPE: Ectopic growth in filaments and petals,
CC distortion of integument planar growth and aberrant embryogenesis and
CC partial lethality in ucn-1 embryos. The double mutants ucn-2 and ucnl-5
CC are embryonic 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; AC006085; AAD30630.1; -; Genomic_DNA.
DR EMBL; AC079828; AAG50535.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32630.1; -; Genomic_DNA.
DR EMBL; BT029004; ABI93913.1; -; mRNA.
DR EMBL; AK229385; BAF01247.1; -; mRNA.
DR PIR; C96549; C96549.
DR RefSeq; NP_564584.1; NM_103996.4.
DR AlphaFoldDB; Q9SYB9; -.
DR SMR; Q9SYB9; -.
DR BioGRID; 26765; 2.
DR IntAct; Q9SYB9; 2.
DR MINT; Q9SYB9; -.
DR STRING; 3702.AT1G51170.1; -.
DR iPTMnet; Q9SYB9; -.
DR PaxDb; Q9SYB9; -.
DR PRIDE; Q9SYB9; -.
DR EnsemblPlants; AT1G51170.1; AT1G51170.1; AT1G51170.
DR GeneID; 841540; -.
DR Gramene; AT1G51170.1; AT1G51170.1; AT1G51170.
DR KEGG; ath:AT1G51170; -.
DR Araport; AT1G51170; -.
DR TAIR; locus:2008331; AT1G51170.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; Q9SYB9; -.
DR OMA; VAWDMLT; -.
DR OrthoDB; 856721at2759; -.
DR PhylomeDB; Q9SYB9; -.
DR PRO; PR:Q9SYB9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYB9; baseline and differential.
DR Genevisible; Q9SYB9; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA: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:0080060; P:integument development; IMP:TAIR.
DR GO; GO:0051782; P:negative regulation of cell division; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0036290; P:protein trans-autophosphorylation; IDA:TAIR.
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; 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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..404
FT /note="Serine/threonine-protein kinase UCN"
FT /id="PRO_0000430952"
FT DOMAIN 22..340
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 341..404
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000305"
FT REGION 185..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 55
FT /note="K->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22927420"
FT MUTAGEN 165
FT /note="G->S: In ucn-1; loss of activity."
FT /evidence="ECO:0000269|PubMed:22927420"
SQ SEQUENCE 404 AA; 45665 MW; 17BD70E18A25B063 CRC64;
METRPSSSSS LSPATNLNLD RLKVLKLLGK GATGTVFLVH DSVSDSSVSS PFALKLVDKS
SASSLRRARW EIQILRRLSD DTNPNPFLPK LLASSESSEF IAWALPYCSG GDLNVLRQRQ
NDGVFSSSVI KFYLAEIVCA LDHLHTMGIA YRDLKPENIL LQESGHVTLT DFDLSCSLNK
PTRPEFYHLS DPEPDPNPES NLSHNKKSLR IFRQKKKKTK SARVNPITRR RLSFSGGERS
NSFVGTDEYI SPEVIRGDGH DFAVDWWALG VLTYEMMYGE TPFKGRNKKE TFRNVLVKEP
EFAGKPSDLT DLIRRLLVKD PTKRFGFWRG AAEIKEHAFF KGVRWELLTE VLRPPFIPLR
DDGDLTGKVT EESGFGIKEY FEKLKTPPLP LPHECSENNP FVDF
