PRK5_ARATH
ID PRK5_ARATH Reviewed; 686 AA.
AC Q9LPT1;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Pollen receptor-like kinase 5 {ECO:0000303|PubMed:23024212};
DE Short=AtPRK5 {ECO:0000303|PubMed:23024212};
DE EC=2.7.11.1 {ECO:0000305};
DE Flags: Precursor;
GN Name=PRK5 {ECO:0000303|PubMed:23024212};
GN Synonyms=PRKB {ECO:0000303|PubMed:12139002};
GN OrderedLocusNames=At1g50610 {ECO:0000312|Araport:AT1G50610};
GN ORFNames=F11F12.7 {ECO:0000312|EMBL:AAF87874.1},
GN F17J6.13 {ECO:0000312|EMBL:AAG51193.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 [6]
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, 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 [8]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY STRESSES, INTERACTION WITH GRI,
RP SUBCELLULAR LOCATION, 3D-STRUCTURE MODELING, AND MUTAGENESIS OF HIS-500 AND
RP ALA-520.
RX PubMed=25398910; DOI=10.15252/embj.201488582;
RA Wrzaczek M., Vainonen J.P., Stael S., Tsiatsiani L., Help-Rinta-Rahko H.,
RA Gauthier A., Kaufholdt D., Bollhoener B., Lamminmaeki A., Staes A.,
RA Gevaert K., Tuominen H., Van Breusegem F., Helariutta Y., Kangasjaervi J.;
RT "GRIM REAPER peptide binds to receptor kinase PRK5 to trigger cell death in
RT Arabidopsis.";
RL EMBO J. 34:55-66(2015).
CC -!- FUNCTION: Receptor-like kinase involved in the control of pollen
CC germination and pollen tube polar growth (PubMed:23024212). The
CC extracellular domain serves as a sensor for peptides derived from GRI
CC (PubMed:25398910). May act as a downstream element for ROS-dependent
CC cell death induced by GRI (PubMed:25398910).
CC {ECO:0000269|PubMed:23024212, ECO:0000269|PubMed:25398910}.
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 with the GRI peptide. {ECO:0000269|PubMed:25398910}.
CC -!- INTERACTION:
CC Q9LPT1; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-16914400, EBI-20651541;
CC Q9LPT1; A0A178UFM8: AXX17_At5g50380; NbExp=2; IntAct=EBI-16914400, EBI-20653342;
CC Q9LPT1; O22138: LRR-RLK; NbExp=2; IntAct=EBI-16914400, EBI-16946020;
CC Q9LPT1; F4I2N7-2: RLK7; NbExp=2; IntAct=EBI-16914400, EBI-20651307;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25398910};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen and/or in flowers
CC (PubMed:12139002). Detected at low levels in leaves (PubMed:25398910).
CC {ECO:0000269|PubMed:12139002, ECO:0000269|PubMed:25398910}.
CC -!- INDUCTION: Up-regulated by biotic and abiotic stresses.
CC {ECO:0000305|PubMed:25398910}.
CC -!- DOMAIN: The protein kinase domain may be catalytically impaired due to
CC the lack of the conserved Asp active site at position 500, which is
CC replaced by a His residue. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: No effect on pollen germination and growth. Prk2
CC and prk5 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}.
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DR EMBL; AC012561; AAF87874.1; -; Genomic_DNA.
DR EMBL; AC079279; AAG51193.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32570.1; -; Genomic_DNA.
DR EMBL; AK117856; BAC42497.1; -; mRNA.
DR EMBL; BT005953; AAO64888.1; -; mRNA.
DR EMBL; FJ708649; ACN59245.1; -; mRNA.
DR PIR; F96542; F96542.
DR RefSeq; NP_175476.2; NM_103943.3.
DR AlphaFoldDB; Q9LPT1; -.
DR SMR; Q9LPT1; -.
DR BioGRID; 26708; 64.
DR IntAct; Q9LPT1; 66.
DR STRING; 3702.AT1G50610.1; -.
DR PaxDb; Q9LPT1; -.
DR PRIDE; Q9LPT1; -.
DR ProteomicsDB; 226167; -.
DR EnsemblPlants; AT1G50610.1; AT1G50610.1; AT1G50610.
DR GeneID; 841483; -.
DR Gramene; AT1G50610.1; AT1G50610.1; AT1G50610.
DR KEGG; ath:AT1G50610; -.
DR Araport; AT1G50610; -.
DR TAIR; locus:2008061; AT1G50610.
DR eggNOG; ENOG502QUJJ; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q9LPT1; -.
DR OMA; WCFGVLI; -.
DR OrthoDB; 805610at2759; -.
DR PhylomeDB; Q9LPT1; -.
DR PRO; PR:Q9LPT1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPT1; baseline and differential.
DR Genevisible; Q9LPT1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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 InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 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..39
FT /evidence="ECO:0000255"
FT CHAIN 40..686
FT /note="Pollen receptor-like kinase 5"
FT /id="PRO_0000389465"
FT TOPO_DOM 40..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 112..135
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 136..159
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 161..184
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 185..208
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 210..230
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT DOMAIN 375..648
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 328..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 381..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 472
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 542
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 500
FT /note="H->D: Restored in-vitro kinase activity; when
FT associated with G-520."
FT /evidence="ECO:0000269|PubMed:25398910"
FT MUTAGEN 520
FT /note="A->G: Restored in-vitro kinase activity; when
FT associated with D-500."
FT /evidence="ECO:0000269|PubMed:25398910"
SQ SEQUENCE 686 AA; 76861 MW; E7F599BE13B04718 CRC64;
MRNWEDPFTL ACNTALKKNL PSCIFIIIFI SVLCPVAMSQ VVVPDSDADC LLRFKDTLAN
GSEFRSWDPL SSPCQGNTAN WFGVLCSNYV WGLQLEGMGL TGKLNLDPLV PMKNLRTISF
MNNNFNGPMP QVKRFTSLKS LYLSNNRFSG EIPADAFLGM PLLKKILLAN NAFRGTIPSS
LASLPMLLEL RLNGNQFQGQ IPSFQQKDLK LASFENNDLD GPIPESLRNM DPGSFAGNKG
LCDAPLSPCS SSSPGVPVVP VSPVDPKSTS PPTGKKAGSF YTLAIILIVI GIILVIIALV
FCFVQSRRRN FLSAYPSSAG KERIESYNYH QSTNKNNKPA ESVNHTRRGS MPDPGGRLLF
VRDDIQRFDL QDLLRASAEV LGSGTFGASY KAAISSGQTL VVKRYKHMNN VGRDEFHEHM
RRLGRLNHPN ILPLVAYYYR REEKLLVTEF MPNSSLASHL HANNSAGLDW ITRLKIIKGV
AKGLSYLFDE LPTLTIPHGH MKSSNIVLDD SFEPLLTDYA LRPMMSSEHA HNFMTAYKSP
EYRPSKGQII TKKTDVWCFG VLILEVLTGR FPENYLTQGY DSNMSLVTWV NDMVKEKKTG
DVFDKEMKGK KNCKAEMINL LKIGLRCCEE EEERRMDMRE VVEMVEMLRE GESEDDFGSM
DHRGTHNNVY SSMLLDDDDF GFSMNR
