ID PSKR2_ARATH Reviewed; 1036 AA.
AC Q9FN37;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 161.
DE RecName: Full=Phytosulfokine receptor 2;
DE Short=AtPSKR2;
DE EC=2.7.11.1;
DE AltName: Full=Phytosulfokine LRR receptor kinase 2;
DE Flags: Precursor;
GN Name=PSKR2; OrderedLocusNames=At5g53890; ORFNames=K19P17.5;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17989228; DOI=10.1073/pnas.0706403104;
RA Amano Y., Tsubouchi H., Shinohara H., Ogawa M., Matsubayashi Y.;
RT "Tyrosine-sulfated glycopeptide involved in cellular proliferation and
RT expansion in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18333-18338(2007).
CC -!- FUNCTION: Phytosulfokine receptor with a serine/threonine-protein
CC kinase activity. {ECO:0000269|PubMed:17989228}.
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 -!- 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;
CC -!- INTERACTION:
CC Q9FN37; Q9SH71: At1g64210; NbExp=2; IntAct=EBI-16902047, EBI-20651385;
CC Q9FN37; Q9M9C5: At1g68400; NbExp=3; IntAct=EBI-16902047, EBI-1238661;
CC Q9FN37; C0LGK4: At2g16250; NbExp=2; IntAct=EBI-16902047, EBI-16943030;
CC Q9FN37; Q9M8T0: At3g02880; NbExp=2; IntAct=EBI-16902047, EBI-1238677;
CC Q9FN37; Q9FL63: At5g24100; NbExp=2; IntAct=EBI-16902047, EBI-20657062;
CC Q9FN37; C0LGU5: At5g45780; NbExp=3; IntAct=EBI-16902047, EBI-16964970;
CC Q9FN37; A0A178UFM8: At5g51560; NbExp=2; IntAct=EBI-16902047, EBI-20653342;
CC Q9FN37; Q8W4S5: At5g63710; NbExp=2; IntAct=EBI-16902047, EBI-16934827;
CC Q9FN37; Q9LJY0: PRK4; NbExp=2; IntAct=EBI-16902047, EBI-16914444;
CC Q9FN37; Q9C9E4: PRK8; NbExp=3; IntAct=EBI-16902047, EBI-20654777;
CC Q9FN37; Q9LVI6: RLK902; NbExp=2; IntAct=EBI-16902047, EBI-1626936;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17989228}.
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; AB007644; BAB10719.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96423.1; -; Genomic_DNA.
DR EMBL; AY064019; AAL36375.1; -; mRNA.
DR EMBL; AY091180; AAM14119.1; -; mRNA.
DR RefSeq; NP_200200.1; NM_124768.4.
DR AlphaFoldDB; Q9FN37; -.
DR SMR; Q9FN37; -.
DR BioGRID; 20714; 31.
DR IntAct; Q9FN37; 42.
DR STRING; 3702.Q9FN37; -.
DR GlyCosmos; Q9FN37; 18 sites, No reported glycans.
DR iPTMnet; Q9FN37; -.
DR PaxDb; 3702-AT5G53890-1; -.
DR ProteomicsDB; 248895; -.
DR EnsemblPlants; AT5G53890.1; AT5G53890.1; AT5G53890.
DR GeneID; 835470; -.
DR Gramene; AT5G53890.1; AT5G53890.1; AT5G53890.
DR KEGG; ath:AT5G53890; -.
DR Araport; AT5G53890; -.
DR TAIR; AT5G53890; PSKR2.
DR eggNOG; ENOG502QT4D; Eukaryota.
DR HOGENOM; CLU_000288_22_9_1; -.
DR InParanoid; Q9FN37; -.
DR OMA; CKCLDQD; -.
DR OrthoDB; 377080at2759; -.
DR PhylomeDB; Q9FN37; -.
DR PRO; PR:Q9FN37; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN37; baseline and differential.
DR Genevisible; Q9FN37; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0001653; F:peptide receptor activity; IMP:TAIR.
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 CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR PANTHER; PTHR48005:SF62; OS02G0116700 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00365; LRR_SD22; 6.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 14.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1036
FT /note="Phytosulfokine receptor 2"
FT /id="PRO_0000365618"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 89..111
FT /note="LRR 1"
FT REPEAT 113..136
FT /note="LRR 2"
FT REPEAT 137..159
FT /note="LRR 3"
FT REPEAT 160..182
FT /note="LRR 4"
FT REPEAT 185..207
FT /note="LRR 5"
FT REPEAT 209..231
FT /note="LRR 6"
FT REPEAT 233..256
FT /note="LRR 7"
FT REPEAT 257..279
FT /note="LRR 8"
FT REPEAT 281..303
FT /note="LRR 9"
FT REPEAT 305..326
FT /note="LRR 10"
FT REPEAT 329..351
FT /note="LRR 11"
FT REPEAT 353..375
FT /note="LRR 12"
FT REPEAT 377..398
FT /note="LRR 13"
FT REPEAT 403..423
FT /note="LRR 14"
FT REPEAT 427..450
FT /note="LRR 15"
FT REPEAT 451..473
FT /note="LRR 16"
FT REPEAT 475..498
FT /note="LRR 17"
FT REPEAT 561..583
FT /note="LRR 18"
FT REPEAT 585..606
FT /note="LRR 19"
FT DOMAIN 754..1025
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 995..1020
FT /note="LRR 20"
FT ACT_SITE 880
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 760..768
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 782
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 751
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 827
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 867
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 922
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1036 AA; 114340 MW; 6DF9511FC2A4E261 CRC64;
MVIILLLVFF VGSSVSQPCH PNDLSALREL AGALKNKSVT ESWLNGSRCC EWDGVFCEGS
DVSGRVTKLV LPEKGLEGVI SKSLGELTEL RVLDLSRNQL KGEVPAEISK LEQLQVLDLS
HNLLSGSVLG VVSGLKLIQS LNISSNSLSG KLSDVGVFPG LVMLNVSNNL FEGEIHPELC
SSSGGIQVLD LSMNRLVGNL DGLYNCSKSI QQLHIDSNRL TGQLPDYLYS IRELEQLSLS
GNYLSGELSK NLSNLSGLKS LLISENRFSD VIPDVFGNLT QLEHLDVSSN KFSGRFPPSL
SQCSKLRVLD LRNNSLSGSI NLNFTGFTDL CVLDLASNHF SGPLPDSLGH CPKMKILSLA
KNEFRGKIPD TFKNLQSLLF LSLSNNSFVD FSETMNVLQH CRNLSTLILS KNFIGEEIPN
NVTGFDNLAI LALGNCGLRG QIPSWLLNCK KLEVLDLSWN HFYGTIPHWI GKMESLFYID
FSNNTLTGAI PVAITELKNL IRLNGTASQM TDSSGIPLYV KRNKSSNGLP YNQVSRFPPS
IYLNNNRLNG TILPEIGRLK ELHMLDLSRN NFTGTIPDSI SGLDNLEVLD LSYNHLYGSI
PLSFQSLTFL SRFSVAYNRL TGAIPSGGQF YSFPHSSFEG NLGLCRAIDS PCDVLMSNML
NPKGSSRRNN NGGKFGRSSI VVLTISLAIG ITLLLSVILL RISRKDVDDR INDVDEETIS
GVSKALGPSK IVLFHSCGCK DLSVEELLKS TNNFSQANII GCGGFGLVYK ANFPDGSKAA
VKRLSGDCGQ MEREFQAEVE ALSRAEHKNL VSLQGYCKHG NDRLLIYSFM ENGSLDYWLH
ERVDGNMTLI WDVRLKIAQG AARGLAYLHK VCEPNVIHRD VKSSNILLDE KFEAHLADFG
LARLLRPYDT HVTTDLVGTL GYIPPEYSQS LIATCRGDVY SFGVVLLELV TGRRPVEVCK
GKSCRDLVSR VFQMKAEKRE AELIDTTIRE NVNERTVLEM LEIACKCIDH EPRRRPLIEE
VVTWLEDLPM ESVQQQ
//
