PRK3_ARATH
ID PRK3_ARATH Reviewed; 633 AA.
AC Q9M1L7;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Pollen receptor-like kinase 3 {ECO:0000303|PubMed:12139002};
DE Short=AtPRK3 {ECO:0000303|PubMed:23024212};
DE EC=2.7.11.1 {ECO:0000305};
DE Flags: Precursor;
GN Name=PRK3 {ECO:0000303|PubMed:12139002};
GN OrderedLocusNames=At3g42880 {ECO:0000312|Araport:AT3G42880};
GN ORFNames=F18P9.40 {ECO:0000312|EMBL:CAB86675.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [5]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12139002; DOI=10.1023/a:1016077014583;
RA Kim H.U., Cotter R., Johnson S., Senda M., Dodds P., Kulikauska R.,
RA Tang W., Ezcura I., Herzmark P., McCormick S.;
RT "New pollen-specific receptor kinases identified in tomato, maize and
RT Arabidopsis: the tomato kinases show overlapping but distinct localization
RT patterns on pollen tubes.";
RL Plant Mol. Biol. 50:1-16(2002).
RN [6]
RP FUNCTION, GENE FAMILY, NOMENCLATURE, INTERACTION WITH ROPGEF1, AND ACTIVITY
RP REGULATION.
RX PubMed=23024212; DOI=10.1093/mp/sss103;
RA Chang F., Gu Y., Ma H., Yang Z.;
RT "AtPRK2 Promotes ROP1 activation via RopGEFs in the control of polarized
RT pollen tube growth.";
RL Mol. Plant 6:1187-1201(2013).
RN [7]
RP INTERACTION WITH PRK6.
RX PubMed=26961657; DOI=10.1038/nature17413;
RA Takeuchi H., Higashiyama T.;
RT "Tip-localized receptors control pollen tube growth and LURE sensing in
RT Arabidopsis.";
RL Nature 531:245-248(2016).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 26-233, AND DISULFIDE BONDS.
RA Xu G., Chakraborty S., Pan H.;
RT "Structure of a Pollen Receptor Kinase 3.";
RL Submitted (JUL-2017) to the PDB data bank.
CC -!- FUNCTION: Receptor-like kinase involved in the control of pollen
CC germination and pollen tube polar growth (PubMed:23024212). Can
CC phosphorylate ROPGEF1 in vitro (PubMed:23024212).
CC {ECO:0000269|PubMed:23024212}.
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};
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};
CC -!- ACTIVITY REGULATION: The phosphorylation activity is calcium-
CC independent. {ECO:0000269|PubMed:23024212}.
CC -!- SUBUNIT: Interacts in vitro with ROPGEF1 (via PRONE domain)
CC (PubMed:23024212). Interacts with PRK6 (PubMed:26961657).
CC {ECO:0000269|PubMed:23024212, ECO:0000269|PubMed:26961657}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen and/or in flowers, but not in
CC leaves. {ECO:0000269|PubMed:12139002}.
CC -!- DOMAIN: The protein kinase domain may be catalytically impaired due to
CC the lack of the conserved Asp active site at position 486, which is
CC replaced by a Asn residue. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL138654; CAB86675.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77758.1; -; Genomic_DNA.
DR EMBL; DQ446723; ABE65985.1; -; mRNA.
DR EMBL; FJ708731; ACN59326.1; -; mRNA.
DR PIR; T47346; T47346.
DR RefSeq; NP_189874.1; NM_114156.2.
DR PDB; 5WLS; X-ray; 2.50 A; A/B=26-233.
DR PDBsum; 5WLS; -.
DR AlphaFoldDB; Q9M1L7; -.
DR SMR; Q9M1L7; -.
DR IntAct; Q9M1L7; 21.
DR STRING; 3702.AT3G42880.1; -.
DR PaxDb; Q9M1L7; -.
DR PRIDE; Q9M1L7; -.
DR ProteomicsDB; 226502; -.
DR EnsemblPlants; AT3G42880.1; AT3G42880.1; AT3G42880.
DR GeneID; 823335; -.
DR Gramene; AT3G42880.1; AT3G42880.1; AT3G42880.
DR KEGG; ath:AT3G42880; -.
DR Araport; AT3G42880; -.
DR TAIR; locus:2078546; AT3G42880.
DR eggNOG; ENOG502QRTV; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q9M1L7; -.
DR OMA; YCQKGQT; -.
DR OrthoDB; 289498at2759; -.
DR PhylomeDB; Q9M1L7; -.
DR PRO; PR:Q9M1L7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1L7; baseline and differential.
DR Genevisible; Q9M1L7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0080092; P:regulation of pollen tube growth; IMP:TAIR.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
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 3D-structure; ATP-binding; Disulfide bond; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..633
FT /note="Pollen receptor-like kinase 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431924"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 90..115
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 117..137
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 138..162
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 163..186
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 188..210
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT DOMAIN 358..633
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 294..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 364..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 458
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 53..62
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:5WLS"
FT DISULFID 224..232
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:5WLS"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:5WLS"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:5WLS"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:5WLS"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:5WLS"
FT HELIX 84..88
FT /evidence="ECO:0007829|PDB:5WLS"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5WLS"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:5WLS"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:5WLS"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5WLS"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:5WLS"
FT TURN 132..137
FT /evidence="ECO:0007829|PDB:5WLS"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:5WLS"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:5WLS"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:5WLS"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:5WLS"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:5WLS"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:5WLS"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:5WLS"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:5WLS"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:5WLS"
SQ SEQUENCE 633 AA; 70249 MW; D3A1859FF9E02169 CRC64;
MTAVLFLCFL LICFSFTPSL QNVSESEPLV RFKRSVNITK GDLNSWRTGT DPCNGKWFGI
YCQKGQTVSG IHVTRLGLSG TINIEDLKDL PNLRTIRLDN NLLSGPLPPF FKLPGLKSLL
LSNNSFSGEI ADDFFKETPQ LKRVFLDNNR LSGKIPASLM QLAGLEELHM QGNQFTGEIP
PLTDGNKVLK SLDLSNNDLE GEIPITISDR KNLEMKFEGN QRLCGSPLNI ECDEKPSSTG
SGNEKNNTAK AIFMVILFLL IFLFVVAIIT RWKKKRQPEF RMLGKDHLSD QESVEVRVPD
SIKKPIDSSK KRSNAEGSSK KGSSHNGKGA GGGPGSGMGD IIMVNSEKGS FGLPDLMKAA
AEVLGNGSLG SAYKAVMANG LSVVVKRIRD MNKLAREAFD TEMQRFGKLR HPNVLTPLAY
HYRREEKLVV SEYMPKSSLL YVLHGDRGVY HSELTWATRL KIIQGVARGM DFLHEEFASY
DLPHGNLKSS NVLLSETYEP LISDYAFLPL LQPNNASQAL FAFKSPEFVQ NQQVSPKSDV
YCLGIIVLEV MTGKFPSQYL NTGKGGTDIV EWVQSSIAQH KEEELIDPEI ASNTDSIKQM
VELLRIGAAC IASNPNERQN MKEIVRRIER VTL
