PRK1_PETIN
ID PRK1_PETIN Reviewed; 720 AA.
AC Q40902;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Pollen receptor-like kinase 1 {ECO:0000303|PubMed:8038606};
DE EC=2.7.10.1 {ECO:0000305|PubMed:8038606};
DE EC=2.7.11.1 {ECO:0000305|PubMed:8038606};
GN Name=PRK1 {ECO:0000303|PubMed:8038606};
OS Petunia integrifolia (Violet-flowered petunia) (Salpiglossis integrifolia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4103 {ECO:0000312|EMBL:AAA33715.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AUTOPHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RC TISSUE=Pollen;
RX PubMed=8038606; DOI=10.2307/3869874;
RA Mu J.H., Lee H.S., Kao T.H.;
RT "Characterization of a pollen-expressed receptor-like kinase gene of
RT Petunia inflata and the activity of its encoded kinase.";
RL Plant Cell 6:709-721(1994).
RN [2]
RP FUNCTION.
RX DOI=10.1046/j.1365-313X.1996.9050613.x;
RA Lee H.-S., Karunanandaa B., McCubbin A., Gilroy S., Kao T.-H.;
RT "PRK1, a receptor-like kinase of Petunia inflata, is essential for
RT postmeiotic development of pollen.";
RL Plant J. 9:613-624(1996).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX DOI=10.1007/s004970050108;
RA Lee H.-S., Chung Y.-Y., Das C., Karunanandaa B., van Went J.L., Mariani C.,
RA Kao T.-H.;
RT "Embryo sac development is affected in Petunia inflata plants transformed
RT with an antisense gene encoding the extracellular domain of receptor kinase
RT PRK1.";
RL Sex. Plant Reprod. 10:341-350(1997).
RN [4]
RP FUNCTION, INTERACTION WITH KIP1, MUTAGENESIS OF LYS-462, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AUTOPHOSPHORYLATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11500547; DOI=10.1104/pp.126.4.1480;
RA Skirpan A.L., McCubbin A.G., Ishimizu T., Wang X., Hu Y., Dowd P.E., Ma H.,
RA Kao T.;
RT "Isolation and characterization of kinase interacting protein 1, a pollen
RT protein that interacts with the kinase domain of PRK1, a receptor-like
RT kinase of petunia.";
RL Plant Physiol. 126:1480-1492(2001).
CC -!- FUNCTION: Dual-specificity kinase with both serine/threonine and
CC tyrosine kinase activities (PubMed:8038606). Required for postmeiotic
CC development of microspores (Ref.2). Involved in embryo sac development
CC at the late stages of megagametogenesis (Ref.3). Involved in the
CC phosphorylation of KIP1 (PubMed:11500547).
CC {ECO:0000269|PubMed:11500547, ECO:0000269|PubMed:8038606,
CC ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
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:0000305|PubMed:8038606};
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:0000305|PubMed:8038606};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000305|PubMed:8038606};
CC -!- SUBUNIT: Interacts with KIP1. {ECO:0000269|PubMed:11500547}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:8038606};
CC Single-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:11500547}.
CC -!- TISSUE SPECIFICITY: Expressed in mature pollen grains and pollen tubes,
CC but not in style, petal, leaf, root or sepal (PubMed:8038606,
CC PubMed:11500547). Very low expression in the ovary (Ref.3).
CC {ECO:0000269|PubMed:11500547, ECO:0000269|PubMed:8038606,
CC ECO:0000269|Ref.3}.
CC -!- DEVELOPMENTAL STAGE: Detected around the time of microspore mitosis
CC with a peak in mature pollen grains. {ECO:0000269|PubMed:11500547,
CC ECO:0000269|PubMed:8038606}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:11500547,
CC ECO:0000269|PubMed:8038606}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; L27341; AAA33715.1; -; Genomic_DNA.
DR AlphaFoldDB; Q40902; -.
DR SMR; Q40902; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0090406; C:pollen tube; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0010152; P:pollen maturation; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Endoplasmic reticulum; Kinase; Leucine-rich repeat;
KW Membrane; Microsome; Nucleotide-binding; Phosphoprotein; Receptor; Repeat;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..720
FT /note="Pollen receptor-like kinase 1"
FT /id="PRO_5000142439"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 40..64
FT /note="LRR 1; degenerate"
FT /evidence="ECO:0000305|PubMed:8038606"
FT REPEAT 123..146
FT /note="LRR 2; degenerate"
FT /evidence="ECO:0000305|PubMed:8038606"
FT REPEAT 154..179
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 226..248
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 249..273
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT DOMAIN 434..702
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 288..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 440..448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 462
FT /note="K->R: Reduced autophosphorylation and strongly
FT decreased interaction with KIP1."
FT /evidence="ECO:0000269|PubMed:11500547"
SQ SEQUENCE 720 AA; 79549 MW; BA41E848F1721F89 CRC64;
MMTEVHDAGR PRVVIFNGSQ LQREAIIPFA SRSSCFHHQL CSRGHLLIIF LLLVSPFNDA
AVDVDGDDND NLIIDHVPDA KSSSEALLNF KSSLSTSSPR GHEVLGSWIP SNSPCSGNNG
NWLGVLCYEG DVWGLQLENL DLSGVIDIDS LLPLHFLRTL SFMNNSFKGQ CLIGISLEPS
SHCTCPIIAS PVRSRMMLPG YDLSQEALFG KQPIQRQHPH LPGYLLPQVF ELSLENNRFT
GSIPHFPPNV LKVLNLSNNQ LEGPIPPALS LMDPTTFSGN KGLCGKPLES ACNSPSQEAN
NPDSRNSSTI SGQSSTDVIR KSPTRLSKVM LIVAVCLVVL CLLIVLILII RRRSHSSSQN
PQPVESNYSN NDRDQNAFTS SAPDDHVTLS GNSTYSNNQH SNSNKAEAPT AAVVGKLSFV
RDDRPRFDLQ DLLRASAEVL GSGNLGSSYK ALLMDGQAVV VKRFKQMNHV AKEDFHEHMR
RLGRLTHPNL LPLVAYYYRK EEKLLVYDYA SNGSLASHLH GNQSRLDWSS RLKIVKGVAK
ALAYLHNELP SLALPHGHLK SSNVLLDKYL NPVLMDYTLV PLVNLAQVQH LLVAYKAPEY
AQQGRITRKT DVWSLGILIL ETLTGKFPTN YLALSTGYGT ELATWVDTII RDNESAFDKE
MNTTKDSQGQ IRKLFDIGVA CCQEDLDTRW DLKEVVQSIQ SLNDKDHGHS NSDQMHDAGV
