PRK6_ARATH
ID PRK6_ARATH Reviewed; 659 AA.
AC Q3E991;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 4.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Pollen receptor-like kinase 6 {ECO:0000303|PubMed:23024212};
DE Short=AtPRK6 {ECO:0000303|PubMed:23024212};
DE Flags: Precursor;
GN Name=PRK6 {ECO:0000303|PubMed:23024212};
GN OrderedLocusNames=At5g20690 {ECO:0000312|Araport:AT5G20690};
GN ORFNames=T1M15.90 {ECO:0000312|EMBL:AF296832};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=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 [4]
RP GENE FAMILY, AND NOMENCLATURE.
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP INTERACTION WITH ROPGEF8; ROPGEF9; ROPGEF12; ROPGEF13; PRK3; LIP1 AND LIP2,
RP AND DOMAIN.
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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 27-262, FUNCTION, DISULFIDE
RP BONDS, INTERACTION WITH LURE1.2, AND MUTAGENESIS OF GLU-226; TYR-227;
RP ASP-234; 239-ASN-ILE-240 AND ASN-239.
RX PubMed=29109411; DOI=10.1038/s41467-017-01323-8;
RA Zhang X., Liu W., Nagae T.T., Takeuchi H., Zhang H., Han Z.,
RA Higashiyama T., Chai J.;
RT "Structural basis for receptor recognition of pollen tube attraction
RT peptides.";
RL Nat. Commun. 8:1331-1331(2017).
CC -!- FUNCTION: Key receptor for sensing species-specific attractants in
CC cooperation with other pollen receptor-like kinases (PubMed:26961657).
CC Essential for pollen tube reorientation toward attractant peptides
CC (PubMed:26961657, PubMed:29109411). {ECO:0000269|PubMed:26961657,
CC ECO:0000269|PubMed:29109411}.
CC -!- SUBUNIT: Interacts with ROPGEF8, ROPGEF9, ROPGEF12, ROPGEF13, PRK3,
CC LIP1 and LIP2 (PubMed:26961657). Binds to LURE peptides via its LRR
CC repeats; interacts with LURE1.1, LURE1.2, LURE1.3 and LURE1.4
CC (PubMed:29109411). {ECO:0000269|PubMed:26961657,
CC ECO:0000269|PubMed:29109411}.
CC -!- INTERACTION:
CC Q3E991; Q93ZS4: NIK3; NbExp=2; IntAct=EBI-20657264, EBI-17121474;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26961657};
CC Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic granule
CC {ECO:0000269|PubMed:26961657}. Note=Re-localizes asymmetrically to
CC direct tip growth direction toward the attractant peptides.
CC {ECO:0000269|PubMed:26961657}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the pollen tube,
CC predominantly at the tip. {ECO:0000269|PubMed:26961657}.
CC -!- DOMAIN: The juxtamembrane domain (288-383) is required for interactions
CC with ROPGEFs, while the kinase domain (384-659) is required for pollen
CC tube growth. {ECO:0000269|PubMed:26961657}.
CC -!- DOMAIN: The protein kinase domain may be catalytically impaired due to
CC the lack of the conserved Asp active site at position 512, which is
CC replaced by a Asn residue. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: Impaired response to the ovular attractant
CC LURE1.2. {ECO:0000269|PubMed:26961657}.
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; AF296832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92878.1; -; Genomic_DNA.
DR EMBL; FJ708781; ACN59372.1; -; mRNA.
DR RefSeq; NP_197569.2; NM_122076.3.
DR PDB; 5Y9W; X-ray; 1.85 A; A/B=27-262.
DR PDB; 5YAH; X-ray; 2.10 A; B=27-262.
DR PDBsum; 5Y9W; -.
DR PDBsum; 5YAH; -.
DR AlphaFoldDB; Q3E991; -.
DR SMR; Q3E991; -.
DR BioGRID; 17467; 9.
DR IntAct; Q3E991; 10.
DR STRING; 3702.AT5G20690.1; -.
DR PaxDb; Q3E991; -.
DR PRIDE; Q3E991; -.
DR ProteomicsDB; 226414; -.
DR EnsemblPlants; AT5G20690.1; AT5G20690.1; AT5G20690.
DR GeneID; 832192; -.
DR Gramene; AT5G20690.1; AT5G20690.1; AT5G20690.
DR KEGG; ath:AT5G20690; -.
DR Araport; AT5G20690; -.
DR TAIR; locus:2180409; AT5G20690.
DR eggNOG; ENOG502QRTV; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q3E991; -.
DR OMA; EPFDVEM; -.
DR OrthoDB; 289498at2759; -.
DR PRO; PR:Q3E991; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q3E991; baseline and differential.
DR Genevisible; Q3E991; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0090404; C:pollen tube tip; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:TAIR.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0010183; P:pollen tube guidance; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
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 SMART; SM00369; LRR_TYP; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..659
FT /note="Pollen receptor-like kinase 6"
FT /id="PRO_0000401340"
FT TOPO_DOM 27..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 95..118
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 120..142
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 143..167
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 168..190
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 192..214
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT DOMAIN 384..659
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 226..242
FT /note="LURE peptides binding"
FT /evidence="ECO:0000269|PubMed:29109411,
FT ECO:0007744|PDB:5Y9W, ECO:0007744|PDB:5YAH"
FT REGION 241..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 390..398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 484
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 557
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 58..67
FT /evidence="ECO:0000269|PubMed:29109411,
FT ECO:0007744|PDB:5Y9W, ECO:0007744|PDB:5YAH"
FT DISULFID 229..237
FT /evidence="ECO:0000269|PubMed:29109411,
FT ECO:0007744|PDB:5Y9W, ECO:0007744|PDB:5YAH"
FT MUTAGEN 226
FT /note="E->A: Normal interaction with LURE1.2."
FT /evidence="ECO:0000269|PubMed:29109411"
FT MUTAGEN 227
FT /note="Y->A: Normal interaction with LURE1.2."
FT /evidence="ECO:0000269|PubMed:29109411"
FT MUTAGEN 234
FT /note="D->A: Compromised interaction with LURE1.2. Reduced
FT pollen tube attraction."
FT /evidence="ECO:0000269|PubMed:29109411"
FT MUTAGEN 239..240
FT /note="Missing: Compromised interaction with LURE1.2.
FT Reduced pollen tube attraction."
FT /evidence="ECO:0000269|PubMed:29109411"
FT MUTAGEN 239
FT /note="N->A: Normal interaction with LURE1.2. Normal pollen
FT tube attraction."
FT /evidence="ECO:0000269|PubMed:29109411"
FT CONFLICT 396
FT /note="G -> R (in Ref. 1; AF296832)"
FT /evidence="ECO:0000305"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5Y9W"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5Y9W"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:5Y9W"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:5Y9W"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:5Y9W"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:5Y9W"
FT TURN 137..142
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:5Y9W"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:5Y9W"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:5Y9W"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5Y9W"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:5Y9W"
SQ SEQUENCE 659 AA; 72637 MW; D21AED432C32409A CRC64;
MAAAVLNPGF FLLILLLSFS ISPSLQYVSE SEPLVRFKNS VKITKGDLNS WREGTDPCSG
KWFGIYCQKG LTVSGIHVTR LGLSGTITVD DLKDLPNLKT IRLDNNLLSG PLPHFFKLRG
LKSLMLSNNS FSGEIRDDFF KDMSKLKRLF LDHNKFEGSI PSSITQLPQL EELHMQSNNL
TGEIPPEFGS MKNLKVLDLS TNSLDGIVPQ SIADKKNLAV NLTENEYLCG PVVDVGCENI
ELNDPQEGQP PSKPSSSVPE TSNKAAINAI MVSISLLLLF FIIVGVIKRR NKKKNPDFRM
LANNRENDVV EVRISESSST TAKRSTDSSR KRGGHSDDGS TKKGVSNIGK GGNGGGGGAL
GGGMGDIIMV NTDKGSFGLP DLMKAAAEVL GNGSLGSAYK AVMTTGLSVV VKRIRDMNQL
AREPFDVEMR RFGKLRHPNI LTPLAYHYRR EEKLVVSEYM PKSSLLYVLH GDRGIYHSEL
TWATRLKIIQ GVAHGMKFLH EEFASYDLPH GNLKSSNVLL SETYEPLISD YAFLPLLQPS
NASQALFAFK TPEFAQTQQV SHKSDVYCLG IIILEILTGK FPSQYLNNGK GGTDIVQWVQ
SSVAEQKEEE LIDPEIVNNT ESMRQMVELL RVGAACIASN PDERLDMREA VRRIEQVKT
