PRK4_ARATH
ID PRK4_ARATH Reviewed; 679 AA.
AC Q9LJY0; Q84WQ0;
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 4 {ECO:0000303|PubMed:23024212};
DE Short=AtPRK4 {ECO:0000303|PubMed:23024212};
DE EC=2.7.11.1 {ECO:0000305};
DE Flags: Precursor;
GN Name=PRK4 {ECO:0000303|PubMed:23024212};
GN Synonyms=PRKA {ECO:0000303|PubMed:12139002};
GN OrderedLocusNames=At3g20190 {ECO:0000312|Araport:AT3G20190};
GN ORFNames=MAL21.21 {ECO:0000312|EMBL:BAB01878.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 227-679.
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 [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, GENE FAMILY, NOMENCLATURE, AND INTERACTION 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).
RN [8]
RP INTERACTION WITH GRI.
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). 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 -!- SUBUNIT: Interacts in vitro with ROPGEF1 (via PRONE domain)
CC (PubMed:23024212). Interacts weakly with the GRI peptide
CC (PubMed:25398910). {ECO:0000269|PubMed:23024212,
CC ECO:0000269|PubMed:25398910}.
CC -!- INTERACTION:
CC Q9LJY0; C0LGH8: At1g63430; NbExp=2; IntAct=EBI-16914444, EBI-20657656;
CC Q9LJY0; C0LGJ1: At1g74360; NbExp=2; IntAct=EBI-16914444, EBI-20652666;
CC Q9LJY0; Q9LFG1: At3g53590; NbExp=2; IntAct=EBI-16914444, EBI-20664191;
CC Q9LJY0; Q9LT96: At5g49770; NbExp=2; IntAct=EBI-16914444, EBI-17123993;
CC Q9LJY0; O64794: LRR-RLK; NbExp=2; IntAct=EBI-16914444, EBI-16887796;
CC Q9LJY0; Q93ZS4: NIK3; NbExp=2; IntAct=EBI-16914444, EBI-17121474;
CC Q9LJY0; Q9ZVR7: PSKR1; NbExp=2; IntAct=EBI-16914444, EBI-16172949;
CC Q9LJY0; Q9FN37: PSKR2; NbExp=2; IntAct=EBI-16914444, EBI-16902047;
CC Q9LJY0; C0LGV1: RGI2; NbExp=2; IntAct=EBI-16914444, EBI-20664449;
CC Q9LJY0; C0LGF5: RGI5; NbExp=2; IntAct=EBI-16914444, EBI-16964286;
CC Q9LJY0; Q9SKB2: SOBIR1; NbExp=2; IntAct=EBI-16914444, EBI-16905883;
CC Q9LJY0; Q9FII5: TDR; NbExp=2; IntAct=EBI-16914444, EBI-15730235;
CC Q9LJY0; Q9SIT1: TMK3; NbExp=2; IntAct=EBI-16914444, EBI-16896864;
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 500, which is
CC replaced by a His 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; AP000383; BAB01878.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76345.1; -; Genomic_DNA.
DR EMBL; BT046196; ACI49795.1; -; mRNA.
DR EMBL; FJ708724; ACN59319.1; -; mRNA.
DR EMBL; BT002912; AAO22728.1; -; mRNA.
DR RefSeq; NP_188654.2; NM_112910.5.
DR AlphaFoldDB; Q9LJY0; -.
DR SMR; Q9LJY0; -.
DR IntAct; Q9LJY0; 96.
DR STRING; 3702.AT3G20190.1; -.
DR iPTMnet; Q9LJY0; -.
DR PaxDb; Q9LJY0; -.
DR PRIDE; Q9LJY0; -.
DR ProteomicsDB; 234876; -.
DR EnsemblPlants; AT3G20190.1; AT3G20190.1; AT3G20190.
DR GeneID; 821563; -.
DR Gramene; AT3G20190.1; AT3G20190.1; AT3G20190.
DR KEGG; ath:AT3G20190; -.
DR Araport; AT3G20190; -.
DR TAIR; locus:2087595; AT3G20190.
DR eggNOG; ENOG502QUJJ; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR OMA; FGVSCHG; -.
DR OrthoDB; 805610at2759; -.
DR PhylomeDB; Q9LJY0; -.
DR PRO; PR:Q9LJY0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJY0; baseline and differential.
DR Genevisible; Q9LJY0; AT.
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-EC.
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; -; 2.
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; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..679
FT /note="Pollen receptor-like kinase 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431925"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 118..141
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 142..165
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 167..191
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 193..217
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 234..257
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT DOMAIN 372..646
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 252..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 378..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 455
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"
SQ SEQUENCE 679 AA; 76102 MW; 40256E0CC1F24663 CRC64;
MLTWETPVML ASNTASTKKL AFITTFLIIV LCPVTMVMSQ PQADVLPLPA SDADCLLRFK
DTLVNASFIS SWDPSISPCK RNSENWFGVL CVTGNVWGLQ LEGMGLTGKL DLEPLAAIKN
LRTLSFMNNK FNGSMPSVKN FGALKSLYLS NNRFTGEIPA DAFDGMHHLK KLLLANNAFR
GSIPSSLAYL PMLLELRLNG NQFHGEIPYF KQKDLKLASF ENNDLEGPIP ESLSNMDPVS
FSGNKNLCGP PLSPCSSDSG SSPDLPSSPT EKNKNQSFFI IAIVLIVIGI ILMIISLVVC
ILHTRRRKSL SAYPSAGQDR TEKYNYDQST DKDKAADSVT SYTSRRGAVP DQNKLLFLQD
DIQRFDLQDL LRASAEVLGS GSFGSSYKTG INSGQMLVVK RYKHMNNVGR DEFHEHMRRL
GRLKHPNLLP IVAYYYRREE KLLIAEFMPN RSLASHLHAN HSVDQPGLDW PTRLKIIQGV
AKGLGYLFNE LTTLTIPHGH LKSSNVVLDE SFEPLLTDYA LRPVMNSEQS HNLMISYKSP
EYSLKGHLTK KTDVWCLGVL ILELLTGRFP ENYLSQGYDA NMSLVTWVSN MVKEKKTGDV
FDKEMTGKKN CKAEMLNLLK IGLSCCEEDE ERRMEMRDAV EKIERLKEGE FDNDFASTTH
NVFASRLIDD DDFGFAMNR
