PRK2_ARATH
ID PRK2_ARATH Reviewed; 647 AA.
AC Q84JQ4; Q9ZVV7;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Pollen receptor-like kinase 2 {ECO:0000303|PubMed:23024212};
DE Short=AtPRK2 {ECO:0000303|PubMed:23024212};
DE EC=2.7.11.1 {ECO:0000305};
DE Flags: Precursor;
GN Name=PRK2 {ECO:0000303|PubMed:23024212};
GN Synonyms=PRK2A {ECO:0000303|PubMed:18000057},
GN PRKC {ECO:0000303|PubMed:12139002};
GN OrderedLocusNames=At2g07040 {ECO:0000312|Araport:AT2G07040};
GN ORFNames=T4E14.15 {ECO:0000312|EMBL:AAC67207.1};
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|EMBL:AAO41982.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=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 [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 FUNCTION, INTERACTION WITH ROPGEF12, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18000057; DOI=10.1073/pnas.0705874104;
RA Zhang Y., McCormick S.;
RT "A distinct mechanism regulating a pollen-specific guanine nucleotide
RT exchange factor for the small GTPase Rop in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18830-18835(2007).
RN [7]
RP FUNCTION, MUTAGENESIS OF LYS-366, AND DOMAIN.
RX PubMed=24136420; DOI=10.1093/jxb/ert323;
RA Zhao X.Y., Wang Q., Li S., Ge F.R., Zhou L.Z., McCormick S., Zhang Y.;
RT "The juxtamembrane and carboxy-terminal domains of Arabidopsis PRK2 are
RT critical for ROP-induced growth in pollen tubes.";
RL J. Exp. Bot. 64:5599-5610(2013).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ROPGEF1, GENE FAMILY,
RP NOMENCLATURE, AND ACTIVITY REGULATION.
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 PubMed:24136420). Phosphorylates ROPGEF1 in its C-terminal region,
CC releasing its auto-inhibition, and thereby activating the ROP1
CC signaling pathway (PubMed:23024212). May act as a scaffolding protein,
CC recruiting ROPGEF12 to the plasma membrane by binding to its C-terminal
CC domain (PubMed:18000057). Phosphorylates ROPGEF12, releasing its auto-
CC inhibition (PubMed:18000057). {ECO:0000269|PubMed:18000057,
CC ECO:0000269|PubMed:23024212, ECO:0000269|PubMed:24136420}.
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 -!- ACTIVITY REGULATION: The phosphorylation activity is calcium-
CC independent. {ECO:0000269|PubMed:23024212}.
CC -!- SUBUNIT: Part of a complex containing ROPGEF1 and ARAC11/ROP1
CC (PubMed:23024212). The interaction between PRK2, ROPGEF1 and
CC ARAC11/ROP1 is phosphorylation-independent (PubMed:23024212). Interacts
CC with ROPGEF12 (via C-terminus)(PubMed:18000057). Interacts with ROPGEF1
CC (via PRONE domain)(PubMed:23024212). {ECO:0000269|PubMed:18000057,
CC ECO:0000269|PubMed:23024212}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18000057};
CC Single-pass membrane protein {ECO:0000255}. Note=ROPGEF12 colocalizes
CC with PRK2 at the apical plasma membrane of pollen tube.
CC {ECO:0000269|PubMed:18000057}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen and/or in flowers, but not in
CC leaves (PubMed:12139002). Expressed in pollen tube (PubMed:18000057).
CC {ECO:0000269|PubMed:12139002, ECO:0000269|PubMed:18000057}.
CC -!- DOMAIN: The protein kinase domain may be catalytically impaired due to
CC the lack of the conserved Asp active site at position 466, which is
CC replaced by a His residue. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DOMAIN: The juxtamembrane domain (274-319) is necessary for a
CC relatively uniform plasma membrane localization. The C-terminal domain
CC (614-647) is required for the induction of pollen tube depolarization.
CC Both domains are required for the interaction of PRK2 with ROPGEF12.
CC {ECO:0000269|PubMed:24136420}.
CC -!- DISRUPTION PHENOTYPE: No effect on pollen germination and growth. Prk1
CC and prk2 or prk2 and prk5 double mutants have no effect on pollen
CC germination and growth. Prk1, prk2 and prk5 triple mutant shows reduced
CC pollen tube elongation. {ECO:0000269|PubMed:23024212}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC67207.1; Type=Erroneous gene model prediction; Evidence={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; AC005171; AAC67207.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06031.1; -; Genomic_DNA.
DR EMBL; BT003936; AAO41982.1; -; mRNA.
DR EMBL; BT005118; AAO50651.1; -; mRNA.
DR EMBL; FJ708690; ACN59285.1; -; mRNA.
DR PIR; G84481; G84481.
DR RefSeq; NP_178721.3; NM_126680.4.
DR AlphaFoldDB; Q84JQ4; -.
DR SMR; Q84JQ4; -.
DR DIP; DIP-46187N; -.
DR IntAct; Q84JQ4; 29.
DR STRING; 3702.AT2G07040.1; -.
DR PaxDb; Q84JQ4; -.
DR PRIDE; Q84JQ4; -.
DR ProteomicsDB; 226501; -.
DR EnsemblPlants; AT2G07040.1; AT2G07040.1; AT2G07040.
DR GeneID; 815274; -.
DR Gramene; AT2G07040.1; AT2G07040.1; AT2G07040.
DR KEGG; ath:AT2G07040; -.
DR Araport; AT2G07040; -.
DR TAIR; locus:2063621; AT2G07040.
DR eggNOG; ENOG502QUJJ; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR OMA; EWTQELF; -.
DR OrthoDB; 805610at2759; -.
DR PhylomeDB; Q84JQ4; -.
DR PRO; PR:Q84JQ4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84JQ4; baseline and differential.
DR Genevisible; Q84JQ4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0090406; C:pollen tube; 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; IDA:TAIR.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IEP:TAIR.
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; 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; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..647
FT /note="Pollen receptor-like kinase 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431923"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 87..109
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 110..134
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 136..159
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 161..183
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 185..203
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT DOMAIN 338..613
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 620..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 508
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MUTAGEN 366
FT /note="K->R: Reduced affinity for ROPGEF12, but no effect
FT on pollen tube depolarization."
FT /evidence="ECO:0000269|PubMed:24136420"
SQ SEQUENCE 647 AA; 72522 MW; 7CF9F8FFD50088F9 CRC64;
MESKCLMFVS IVSVFFMVVN GVSETETLLK FKNSLVIGRA NALESWNRRN PPCKWTGVLC
DRGFVWGLRL ENLELSGSID IEALMGLNSL RSLSFINNKF KGPFPEFKKL VALKSLYLSN
NQFDLEIPKD AFDGMGWLKK LHLEQNNFIG EIPTSLVKSP KLIELRLDGN RFTGQIPEFR
HHPNMLNLSN NALAGQIPNS FSTMDPKLFE GNKGLCGKPL DTKCSSPYNH SSEPKSSTKK
TSSKFLYIVA AAVAALAASL IIIGVVIFLI RRRKKKQPLL SAEPGPSSLQ MRAGIQESER
GQGSYHSQNR AAKKMIHTTK LSFLRDDKGK FELQDLLKAS AEILGSGCFG ASYKTLLSNG
SVMVVKRFKH MNSAGIDEFQ EHMKRLGRLN HENLLPIVAY YYKKEEKLFV SDFVANGSLA
AHLHGHKSLG QPSLDWPTRF NIVKGVGRGL LYLHKNLPSL MAPHGHLKSS NVLLSEKFEP
LLMDYGLIPM INEESAQELM VAYKSPEYVK QSRVTKKTDV WGLGVLILEI LTGKLLESFS
QVDKESEEDL ASWVRSSFKG EWTQELFDQE MGKTSNCEAH ILNLMRIGLS CCEVDVEKRL
DIREAVEKME DLMKEREQGD DDFYSTYASE ADGRSSRGLS SEGINLS
