PID_ORYSJ
ID PID_ORYSJ Reviewed; 484 AA.
AC Q2QM77; A0A0P0YCM1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein kinase PINOID;
DE Short=OsPID;
DE EC=2.7.11.1;
GN Name=PID; OrderedLocusNames=Os12g0614600, LOC_Os12g42020;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY AUXIN.
RX PubMed=17303594; DOI=10.1093/pcp/pcm024;
RA Morita Y., Kyozuka J.;
RT "Characterization of OsPID, the rice ortholog of PINOID, and its possible
RT involvement in the control of polar auxin transport.";
RL Plant Cell Physiol. 48:540-549(2007).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the regulation of
CC auxin signaling. May control polar auxin transport and probably plays a
CC role in the pattern formation and organogenesis in the rice shoot.
CC {ECO:0000269|PubMed:17303594}.
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 -!- TISSUE SPECIFICITY: Expressed in the shoot apical meristem at the
CC boundary of the new forming meristems. Expressed in the regions where
CC panicle branches are produced, in developing flower and vascular
CC bundles. {ECO:0000269|PubMed:17303594}.
CC -!- INDUCTION: By auxin. {ECO:0000269|PubMed:17303594}.
CC -!- MISCELLANEOUS: Plants overexpressing PID show variety of development
CC abnormalities, such as delay of adventitious root development, curled
CC growth of shoots and agravitropism.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; DP000011; ABA99407.1; -; Genomic_DNA.
DR EMBL; AP008218; BAF30287.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT18079.1; -; Genomic_DNA.
DR EMBL; AK106290; BAG97667.1; -; mRNA.
DR RefSeq; XP_015619092.1; XM_015763606.1.
DR AlphaFoldDB; Q2QM77; -.
DR SMR; Q2QM77; -.
DR STRING; 4530.OS12T0614600-01; -.
DR iPTMnet; Q2QM77; -.
DR PaxDb; Q2QM77; -.
DR PRIDE; Q2QM77; -.
DR EnsemblPlants; Os12t0614600-01; Os12t0614600-01; Os12g0614600.
DR GeneID; 4352785; -.
DR Gramene; Os12t0614600-01; Os12t0614600-01; Os12g0614600.
DR KEGG; osa:4352785; -.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; Q2QM77; -.
DR OMA; ERESPCM; -.
DR OrthoDB; 799520at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q2QM77; OS.
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: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:0009908; P:flower development; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000012; P:regulation of auxin polar transport; NAS:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR GO; GO:0048367; P:shoot system development; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Auxin signaling pathway; Developmental protein; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..484
FT /note="Protein kinase PINOID"
FT /id="PRO_0000411972"
FT DOMAIN 111..427
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 428..484
FT /note="AGC-kinase C-terminal"
FT REGION 445..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 117..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 484 AA; 51769 MW; 918C9EEE1E77079D CRC64;
MVAAVRAPVK PEMVELSPAA MERYSSDADT TAPNSSLSSA ASSTGSLARC SSLSRLSFDC
SPSAAVAAAA TSCSPPRASV LLRPHRSGDV AWAAIRAAST TSAAPLGPRD FKLVRRIGGG
DIGTVYLCRL RSSPERESPC MYAMKVVDRR AVARKQKLGR AAAEKRILRQ LDHPFLPTLF
ADFDATPHFS CAVMEFCPGG DLHSLRHRMP SRRFPLPSAR FYAAEVLLAI EYLHMMGIVY
RDLKPENVLI RADGHIMLTD FDLSLQSTTS PSLDGDTDTD DEASGGASCF PDHLLRFKRR
RNAVAAPRPR FVAEPVDARS CSFVGTHEYV APEVASGGAH GAAVDWWAYG VFLYELIYGR
TPFAGATNEA TLRNIVRRPL AFPSGSGSCG PADADARDLI ARLLAKDPAA RLGSRRGAAD
VKSHPFFKSL NLALLRSSRP PVVPGAGAGA APLHRSQSCK AAPTTPPPPT TTKPANATAR
FDLF
