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   27-MAR-2024, entry version 94.
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.C0LGU0; -.
DR   GlyCosmos; C0LGU0; 1 site, No reported glycans.
DR   PaxDb; 3702-AT5G35390-1; -.
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; AT5G35390; PRK1.
DR   eggNOG; ENOG502QUJJ; Eukaryota.
DR   HOGENOM; CLU_000288_92_6_1; -.
DR   InParanoid; C0LGU0; -.
DR   OMA; ELAQDIM; -.
DR   OrthoDB; 1213458at2759; -.
DR   PhylomeDB; C0LGU0; -.
DR   PRO; PR:C0LGU0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; C0LGU0; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; IDA:TAIR.
DR   GO; GO:0016324; C:apical plasma membrane; IDA: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; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR046959; PRK1-6/SRF4-like.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR48007; LEUCINE-RICH REPEAT RECEPTOR-LIKE PROTEIN KINASE PXC1; 1.
DR   PANTHER; PTHR48007:SF64; POLLEN RECEPTOR-LIKE KINASE 1; 1.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   Genevisible; C0LGU0; AT.
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
//