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Protein

Protein kinase PINOID

Gene

PID

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase involved in the regulation of auxin signaling. Acts as a positive regulator of cellular auxin efflux and regulates organ development by enhancing polar auxin transport. Phosphorylates conserved serine residues in the PIN auxin efflux carriers. Phosphorylation of PIN proteins is required and sufficient for apical-basal PIN polarity that enables directional intercellular auxin fluxes, which mediate differential growth, tissue patterning and organogenesis. Acts in association with PIN1 to control the establishment of bilateral symmetry and promotion of cotyledon outgrowth. Regulates root gravitropism through modulation of PIN2-dependent basipetal auxin transport. Required for polarization of PIN3-dependent auxin transport for hypocotyl gravitropic response. The protein kinase activity of PID is essential for its auxin efflux regulatory function. PID kinase and PP2A phosphatase activities antagonistically regulate phosphorylation of PIN proteins, affecting PIN sorting.15 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by magnesium and PDK1. Inhibited by staurosporine. Repressed by calcium.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091ATPPROSITE-ProRule annotation
Active sitei205 – 2051Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi81 – 899ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: TAIR
  • protein kinase activity Source: TAIR
  • protein serine/threonine kinase activity Source: TAIR

GO - Biological processi

  • auxin-activated signaling pathway Source: TAIR
  • auxin polar transport Source: TAIR
  • cotyledon development Source: UniProtKB
  • intracellular signal transduction Source: GO_Central
  • phyllome development Source: TAIR
  • positive gravitropism Source: TAIR
  • response to auxin Source: TAIR
  • response to karrikin Source: TAIR
  • root hair elongation Source: TAIR
  • root hair initiation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Auxin signaling pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT2G34650-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase PINOID (EC:2.7.11.1)
Alternative name(s):
Protein kinase ABRUPTUS
Gene namesi
Name:PID
Synonyms:ABR
Ordered Locus Names:At2g34650
ORF Names:T31E10.1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G34650.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: TAIR
  • cytoplasm Source: GO_Central
  • cytosol Source: UniProtKB-SubCell
  • nucleus Source: GO_Central
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Pleiotropic defects in the development of floral organs, cotyledons and leaves, especially in the number of organs produced. Loss of function induces an apical-to-basal shift in PIN1 polar targeting at the inflorescence apex, accompanied by defective organogenesis.5 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi84 – 841G → S in pid-10; intermediate pid phenotype. 1 Publication
Mutagenesisi128 – 1281E → K in pid-5 and pid-11; strong pid phenotype. 1 Publication
Mutagenesisi166 – 1661H → S in pid-13; weak pid phenotype. 1 Publication
Mutagenesisi205 – 2051D → A: Loss of autophosphorylation. Loss of localization to the cell periphery. 3 Publications
Mutagenesisi225 – 2251D → G: Increases autophosphorylation activity. 1 Publication
Mutagenesisi226 – 2261L → F in pid-3; strong pid phenotype. 1 Publication
Mutagenesisi288 – 2903SGS → EGE: Increases autophosphorylation activity. Loss of phosphorylation by PDK1. 2 Publications
Mutagenesisi294 – 2941T → E: Loss of autophosphorylation. 1 Publication
Mutagenesisi300 – 3001P → Q in pid-8; weak pid phenotype. 1 Publication
Mutagenesisi378 – 3781R → K in pid-4 and pid-12; strong pid phenotype. 1 Publication
Mutagenesisi380 – 3801G → R in pid-2; intermediate pid phenotype. 1 Publication
Mutagenesisi435 – 4384FDYF → VDYV: Decreases autophosphorylation 3-fold. Loss of phosphorylation by PDK1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Protein kinase PINOIDPRO_0000411970Add
BLAST

Post-translational modificationi

Autophosphorylated. Phosphorylated by PDK1.

Proteomic databases

PaxDbiO64682.
PRIDEiO64682.

Expressioni

Tissue specificityi

Expressed in root hair cells, shoot xylem parenchyma cells and endodermis around the vasculature. Expressed in anther primordia, vasculature of the growing flower stalk, young pedicels and bracts and developing sepals, but not in petals. In pistils, transiently expressed in the vasculature of the style and the septum, and in the integuments and funiculus of the developing ovule.2 Publications

Developmental stagei

Expressed during embryogenesis at the globular stage on the apical flanks of the embryo, where the cotyledons are subsequently formed. Expression in the cotyledons persists at the heart stage until the mid-torpedo stage. At the bent-cotyledon stage, expressed weakly in the apical meristem. At the early phase of flowering, expressed in discrete groups of cells on the flanks of the apex initially marking the floral anlagen. During primordia differentiation, expressed in the adaxial portion of the primordia. In developing flowers, transiently expressed in nascent floral organs and then decreases as floral organs mature.1 Publication

Inductioni

By auxin.2 Publications

Gene expression databases

GenevisibleiO64682. AT.

Interactioni

Subunit structurei

Interacts with PDK1, CML12 and PBP1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CML12P250714EBI-1393382,EBI-1238781
PBP1Q9LSQ64EBI-1393382,EBI-1393367
PDPK1Q9XF673EBI-1393382,EBI-1103587

Protein-protein interaction databases

BioGridi3376. 4 interactions.
DIPiDIP-39595N.
IntActiO64682. 6 interactions.
STRINGi3702.AT2G34650.1.

Structurei

3D structure databases

ProteinModelPortaliO64682.
SMRiO64682. Positions 7-412.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 394320Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini395 – 43844AGC-kinase C-terminalAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0610. Eukaryota.
ENOG410XQ0C. LUCA.
HOGENOMiHOG000233027.
InParanoidiO64682.
OMAiMSLGTTN.
OrthoDBiEOG09360H0K.
PhylomeDBiO64682.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O64682-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRESDGEMS LGTTNSPISS GTESCSSFSR LSFDAPPSTI PEEESFLSLK
60 70 80 90 100
PHRSSDFAYA EIRRRKKQGL TFRDFRLMRR IGAGDIGTVY LCRLAGDEEE
110 120 130 140 150
SRSSYFAMKV VDKEALALKK KMHRAEMEKT ILKMLDHPFL PTLYAEFEAS
160 170 180 190 200
HFSCIVMEYC SGGDLHSLRH RQPHRRFSLS SARFYAAEVL VALEYLHMLG
210 220 230 240 250
IIYRDLKPEN ILVRSDGHIM LSDFDLSLCS DSIAAVESSS SSPENQQLRS
260 270 280 290 300
PRRFTRLARL FQRVLRSKKV QTLEPTRLFV AEPVTARSGS FVGTHEYVAP
310 320 330 340 350
EVASGGSHGN AVDWWAFGVF LYEMIYGKTP FVAPTNDVIL RNIVKRQLSF
360 370 380 390 400
PTDSPATMFE LHARNLISGL LNKDPTKRLG SRRGAAEVKV HPFFKGLNFA
410 420 430
LIRTLTPPEI PSSVVKKPMK SATFSGRSSN KPAAFDYF
Length:438
Mass (Da):49,271
Last modified:August 1, 1998 - v1
Checksum:i29A33E80FF96B032
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF232236 mRNA. Translation: AAF40202.1.
AC004077 Genomic DNA. Translation: AAC26704.1.
CP002685 Genomic DNA. Translation: AEC09003.1.
PIRiC84759.
RefSeqiNP_181012.1. NM_129019.4.
UniGeneiAt.19528.

Genome annotation databases

EnsemblPlantsiAT2G34650.1; AT2G34650.1; AT2G34650.
GeneIDi818030.
GrameneiAT2G34650.1; AT2G34650.1; AT2G34650.
KEGGiath:AT2G34650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF232236 mRNA. Translation: AAF40202.1.
AC004077 Genomic DNA. Translation: AAC26704.1.
CP002685 Genomic DNA. Translation: AEC09003.1.
PIRiC84759.
RefSeqiNP_181012.1. NM_129019.4.
UniGeneiAt.19528.

3D structure databases

ProteinModelPortaliO64682.
SMRiO64682. Positions 7-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3376. 4 interactions.
DIPiDIP-39595N.
IntActiO64682. 6 interactions.
STRINGi3702.AT2G34650.1.

Proteomic databases

PaxDbiO64682.
PRIDEiO64682.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G34650.1; AT2G34650.1; AT2G34650.
GeneIDi818030.
GrameneiAT2G34650.1; AT2G34650.1; AT2G34650.
KEGGiath:AT2G34650.

Organism-specific databases

TAIRiAT2G34650.

Phylogenomic databases

eggNOGiKOG0610. Eukaryota.
ENOG410XQ0C. LUCA.
HOGENOMiHOG000233027.
InParanoidiO64682.
OMAiMSLGTTN.
OrthoDBiEOG09360H0K.
PhylomeDBiO64682.

Enzyme and pathway databases

BioCyciARA:AT2G34650-MONOMER.

Miscellaneous databases

PROiO64682.

Gene expression databases

GenevisibleiO64682. AT.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPID_ARATH
AccessioniPrimary (citable) accession number: O64682
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: August 1, 1998
Last modified: September 7, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Plants overexpressing PID are small with dark green, curled leaves, with vegetative and floral organs defects and reduced apical dominance and internode elongation. Specific overexpression of PID in root hair cells suppresses root hair development. Over-expression of PID induces a basal-to-apical shift in PIN2 and PIN4 localization, resulting in the loss of auxin gradients and strong defects in embryo and seedling roots.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.