PID2_ARATH
ID PID2_ARATH Reviewed; 525 AA.
AC Q64FQ2; O48785; Q0WP71;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein kinase PINOID 2;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase AGC1-10;
GN Name=PID2; Synonyms=AGC1-10; OrderedLocusNames=At2g26700; ORFNames=F18A8.7;
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 / MRNA].
RA Berendzen K.W., Okresz L., Anthony R., Henriques R., Bogre L., Koncz C.;
RT "Characterization of an AGC family member kinase, AGC1-10.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [5]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=19075219; DOI=10.1073/pnas.0809761106;
RA Cheng Y., Qin G., Dai X., Zhao Y.;
RT "NPY genes and AGC kinases define two key steps in auxin-mediated
RT organogenesis in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:21017-21022(2008).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the regulation of
CC auxin signaling. Plays a minor role in the regulation of cellular auxin
CC efflux and cotyledon organogenesis. {ECO:0000269|PubMed:19075219}.
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 -!- 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;
CC -!- INTERACTION:
CC Q64FQ2; Q9XF67: PDPK1; NbExp=2; IntAct=EBI-1103769, EBI-1103587;
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the embryogenesis in the
CC provascular tissues. {ECO:0000269|PubMed:19075219}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19075219}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB95304.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF01078.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY705432; AAU14162.1; -; Genomic_DNA.
DR EMBL; AY705433; AAU14163.1; -; mRNA.
DR EMBL; AC003105; AAB95304.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07877.1; -; Genomic_DNA.
DR EMBL; AK229209; BAF01078.1; ALT_INIT; mRNA.
DR PIR; G84663; G84663.
DR RefSeq; NP_180238.2; NM_128227.5.
DR AlphaFoldDB; Q64FQ2; -.
DR SMR; Q64FQ2; -.
DR BioGRID; 2563; 1.
DR IntAct; Q64FQ2; 1.
DR STRING; 3702.AT2G26700.1; -.
DR PaxDb; Q64FQ2; -.
DR PRIDE; Q64FQ2; -.
DR EnsemblPlants; AT2G26700.1; AT2G26700.1; AT2G26700.
DR GeneID; 817211; -.
DR Gramene; AT2G26700.1; AT2G26700.1; AT2G26700.
DR KEGG; ath:AT2G26700; -.
DR Araport; AT2G26700; -.
DR TAIR; locus:2043813; AT2G26700.
DR eggNOG; KOG0610; Eukaryota.
DR eggNOG; KOG4198; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; Q64FQ2; -.
DR OMA; PWVPKEE; -.
DR OrthoDB; 799520at2759; -.
DR PhylomeDB; Q64FQ2; -.
DR PRO; PR:Q64FQ2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q64FQ2; baseline and differential.
DR Genevisible; Q64FQ2; 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:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0048825; P:cotyledon development; IGI:TAIR.
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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Auxin signaling pathway; Developmental protein; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..525
FT /note="Protein kinase PINOID 2"
FT /id="PRO_0000411971"
FT DOMAIN 87..465
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 466..525
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 93..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 214
FT /note="D -> G (in Ref. 4; BAF01078)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 59294 MW; 75D92040920BB88F CRC64;
MANSSIFYKD NESDYESSTV GPDSSRRTSW LSSSFTASPS CSSISHLSNH GLNSYNQSKP
HKANQVAWEA MARLRRCCGR AVGLEHFRLL KRLGSGDIGS VYLCQIRGSP ETAFYAMKVV
DKEAVAVKKK LGRAEMEKKI LGMLDHPFCP TLYAAFEASH YSFLVMEYCP GGDLYAVRLR
QPSKRFTISS TRFYAAETLV ALEYLHMMGI VYRDLKPENV LIREDGHVML SDFDLSFKCD
VVPQFLSDND RDRGHQEDDD DISIRRKCST PSCTTTPLNP VISCFSPTSS RRRKKNVVTT
TIHENAAGTS DSVKSNDVSR TFSRSPSSCS RVSNGLRDIS GGCPSIFAEP INARSKSFVG
THEYLAPEVI SGQGHGSAVD WWTYGIFLYE MIFGRTPFKG DNNEKTLVNI LKAPLTFPKV
IVNSPKEYED MVNAQDLIIK LLVKNPKKRL GSLKGSIEIK RHEFFEGVNW ALIRSIKPPW
VPKEETSHKT KGDNRSVNYY LPPRFMMSRK ERNEPYHVSN YFDYF