PRK1_ARATH
ID PRK1_ARATH Reviewed; 662 AA.
AC C0LGU0; O65240;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Pollen receptor-like kinase 1 {ECO:0000303|PubMed:23024212};
DE Short=AtPRK1 {ECO:0000303|PubMed:23024212};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=LRR receptor-like serine/threonine-protein kinase RLK;
DE Flags: Precursor;
GN Name=PRK1 {ECO:0000303|PubMed:23024212};
GN Synonyms=PRKD {ECO:0000303|PubMed:12139002}, RLK;
GN OrderedLocusNames=At5g35390 {ECO:0000312|Araport:AT5G35390};
GN ORFNames=T26D22.9 {ECO:0000312|EMBL:AAC13607.1};
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=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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [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 SUBCELLULAR LOCATION.
RX PubMed=18591430; DOI=10.1083/jcb.200801086;
RA Lee Y.J., Szumlanski A., Nielsen E., Yang Z.;
RT "Rho-GTPase-dependent filamentous actin dynamics coordinate vesicle
RT targeting and exocytosis during tip growth.";
RL J. Cell Biol. 181:1155-1168(2008).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, GENE FAMILY, NOMENCLATURE, AND INTERACTION
RP WITH ROPGEF1.
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).
CC -!- FUNCTION: Receptor-like kinase involved in the control of pollen
CC germination and pollen tube polar growth (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 -!- SUBUNIT: Interacts in vitro with ROPGEF1 (via PRONE domain).
CC {ECO:0000269|PubMed:23024212}.
CC -!- INTERACTION:
CC C0LGU0; Q9FK10: At5g53320; NbExp=2; IntAct=EBI-20665360, EBI-20654730;
CC C0LGU0; Q6R2K3: SRF3; NbExp=2; IntAct=EBI-20665360, EBI-20651925;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18591430};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:18591430}.
CC Note=Preferentially localized to the apical region of the pollen tube
CC plasma membrane.
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 485, which is
CC replaced by a His residue. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: No effect on pollen germination and growth. Prk1
CC and prk2 double mutant has no effect on pollen germination and growth.
CC Prk1, prk2 and prk5 triple mutant shows reduced pollen tube elongation.
CC {ECO:0000269|PubMed:23024212}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13607.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB11489.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF058826; AAC13607.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB025636; BAB11489.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93962.1; -; Genomic_DNA.
DR EMBL; FJ708784; ACN59375.1; -; mRNA.
DR PIR; T01183; T01183.
DR RefSeq; NP_198389.2; NM_122930.3.
DR AlphaFoldDB; C0LGU0; -.
DR SMR; C0LGU0; -.
DR BioGRID; 18754; 15.
DR IntAct; C0LGU0; 17.
DR STRING; 3702.AT5G35390.1; -.
DR PaxDb; C0LGU0; -.
DR PRIDE; C0LGU0; -.
DR EnsemblPlants; AT5G35390.1; AT5G35390.1; AT5G35390.
DR GeneID; 833500; -.
DR Gramene; AT5G35390.1; AT5G35390.1; AT5G35390.
DR KEGG; ath:AT5G35390; -.
DR Araport; AT5G35390; -.
DR TAIR; locus:2182623; AT5G35390.
DR eggNOG; ENOG502QUJJ; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; C0LGU0; -.
DR OMA; ACCEANV; -.
DR OrthoDB; 805610at2759; -.
DR PhylomeDB; C0LGU0; -.
DR PRO; PR:C0LGU0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C0LGU0; baseline and differential.
DR Genevisible; C0LGU0; AT.
DR GO; GO:0045177; C:apical part of cell; IDA:TAIR.
DR GO; GO:0016324; C:apical plasma membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..662
FT /note="Pollen receptor-like kinase 1"
FT /id="PRO_0000387521"
FT TOPO_DOM 32..256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 79..98
FT /note="LRR 1"
FT REPEAT 99..121
FT /note="LRR 2"
FT REPEAT 122..144
FT /note="LRR 3"
FT REPEAT 147..169
FT /note="LRR 4"
FT REPEAT 171..191
FT /note="LRR 5"
FT REPEAT 192..214
FT /note="LRR 6"
FT DOMAIN 357..639
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 233..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 363..371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 457
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 527
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 662 AA; 73483 MW; 1F441F0B84D9CE8C CRC64;
MPPMQARTLS VYNVMVPLVC LLLFFSTPTH GLSDSEAILK FKESLVVGQE NALASWNAKS
PPCTWSGVLC NGGSVWRLQM ENLELSGSID IEALSGLTSL RTLSFMNNKF EGPFPDFKKL
AALKSLYLSN NQFGGDIPGD AFEGMGWLKK VHLAQNKFTG QIPSSVAKLP KLLELRLDGN
QFTGEIPEFE HQLHLLNLSN NALTGPIPES LSMTDPKVFE GNKGLYGKPL ETECDSPYIE
HPPQSEARPK SSSRGPLVIT AIVAALTILI ILGVIFLLNR SYKNKKPRLA VETGPSSLQK
KTGIREADQS RRDRKKADHR KGSGTTKRMG AAAGVENTKL SFLREDREKF DLQDLLKASA
EILGSGCFGA SYKAVLSSGQ MMVVKRFKQM NNAGRDEFQE HMKRLGRLMH HNLLSIVAYY
YRKEEKLLVC DFAERGSLAI NLHSNQSLGK PSLDWPTRLK IVKGVAKGLF YLHQDLPSLM
APHGHLKSSN VLLTKTFEPL LTDYGLIPLI NQEKAQMHMA AYRSPEYLQH RRITKKTDVW
GLGILILEIL TGKFPANFSQ SSEEDLASWV NSGFHGVWAP SLFDKGMGKT SHCEGQILKL
LTIGLNCCEP DVEKRLDIGQ AVEKIEELKE REGDDDDFYS TYVSETDGRS SKGESCESIS
FA
