ID PSKR1_DAUCA Reviewed; 1021 AA.
AC Q8LPB4;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Phytosulfokine receptor 1;
DE Short=DcPSKR1;
DE EC=2.7.11.1;
DE AltName: Full=Phytosulfokine LRR receptor kinase 1;
DE Flags: Precursor;
GN Name=PSKR;
OS Daucus carota (Wild carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=4039;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RX PubMed=12029134; DOI=10.1126/science.1069607;
RA Matsubayashi Y., Ogawa M., Morita A., Sakagami Y.;
RT "An LRR receptor kinase involved in perception of a peptide plant hormone,
RT phytosulfokine.";
RL Science 296:1470-1472(2002).
RN [2]
RP MUTAGENESIS OF 503-GLU--LYS-517 AND 518-LYS--ILE-538, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17092941; DOI=10.1074/jbc.m604558200;
RA Shinohara H., Ogawa M., Sakagami Y., Matsubayashi Y.;
RT "Identification of ligand binding site of phytosulfokine receptor by on-
RT column photoaffinity labeling.";
RL J. Biol. Chem. 282:124-131(2007).
CC -!- FUNCTION: Phytosulfokine receptor with a serine/threonine-protein
CC kinase activity. Regulates, in response to phytosulfokine binding, a
CC signaling cascade involved in plant cell differentiation, organogenesis
CC and somatic embryogenesis. {ECO:0000269|PubMed:12029134}.
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 Q8LPB4; Q9XIC7: SERK2; Xeno; NbExp=4; IntAct=EBI-16172869, EBI-6299033;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in leaf, apical meristem,
CC hypocotyl and root. {ECO:0000269|PubMed:12029134}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12029134}.
CC -!- MISCELLANEOUS: The 36 amino-acid island present in the 18th leucine-
CC rich repeat contains a ligand binding pocket that directly interacts
CC with PSK. An island domain has also been found among the extracellular
CC LRRs of the brassinosteroid receptor BRI1 and has been shown to be
CC critical for its function.
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; AB060167; BAC00995.1; -; mRNA.
DR PDB; 4Z5W; X-ray; 2.20 A; A/B=24-659.
DR PDB; 4Z61; X-ray; 2.75 A; A/B=24-659.
DR PDB; 4Z62; X-ray; 2.90 A; A=24-659.
DR PDBsum; 4Z5W; -.
DR PDBsum; 4Z61; -.
DR PDBsum; 4Z62; -.
DR AlphaFoldDB; Q8LPB4; -.
DR SMR; Q8LPB4; -.
DR DIP; DIP-61782N; -.
DR IntAct; Q8LPB4; 2.
DR GlyCosmos; Q8LPB4; 19 sites, No reported glycans.
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:0006952; P:defense response; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
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; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45974:SF183; PHYTOSULFOKINE RECEPTOR 1; 1.
DR PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR Pfam; PF00560; LRR_1; 7.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51450; LRR; 13.
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 3D-structure; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Receptor; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1021
FT /note="Phytosulfokine receptor 1"
FT /id="PRO_0000024372"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 21..43
FT /note="LRR 1"
FT REPEAT 85..109
FT /note="LRR 2"
FT REPEAT 110..133
FT /note="LRR 3"
FT REPEAT 135..156
FT /note="LRR 4"
FT REPEAT 158..180
FT /note="LRR 5"
FT REPEAT 181..205
FT /note="LRR 6"
FT REPEAT 206..229
FT /note="LRR 7"
FT REPEAT 231..252
FT /note="LRR 8"
FT REPEAT 253..277
FT /note="LRR 9"
FT REPEAT 301..325
FT /note="LRR 10"
FT REPEAT 326..349
FT /note="LRR 11"
FT REPEAT 351..372
FT /note="LRR 12"
FT REPEAT 373..397
FT /note="LRR 13"
FT REPEAT 402..426
FT /note="LRR 14"
FT REPEAT 428..448
FT /note="LRR 15"
FT REPEAT 449..474
FT /note="LRR 16"
FT REPEAT 476..496
FT /note="LRR 17"
FT REPEAT 498..555
FT /note="LRR 18; atypical"
FT REPEAT 556..580
FT /note="LRR 19"
FT REPEAT 581..604
FT /note="LRR 20"
FT REPEAT 606..629
FT /note="LRR 21"
FT DOMAIN 743..1014
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 869
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 749..757
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 771
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 632
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 503..517
FT /note="Missing: Loss of PSK binding activity."
FT /evidence="ECO:0000269|PubMed:17092941"
FT MUTAGEN 518..538
FT /note="Missing: Loss of PSK binding activity."
FT /evidence="ECO:0000269|PubMed:17092941"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:4Z5W"
FT TURN 74..78
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:4Z5W"
FT TURN 175..179
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:4Z5W"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 368..372
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 389..396
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 443..447
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 467..471
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:4Z62"
FT HELIX 491..495
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 497..500
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 526..530
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 551..555
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 575..579
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:4Z5W"
FT HELIX 599..603
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 614..620
FT /evidence="ECO:0007829|PDB:4Z61"
FT HELIX 625..628
FT /evidence="ECO:0007829|PDB:4Z61"
FT HELIX 632..635
FT /evidence="ECO:0007829|PDB:4Z5W"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:4Z5W"
SQ SEQUENCE 1021 AA; 112099 MW; B0C7F101B29144C2 CRC64;
MGVLRVYVIL ILVGFCVQIV VVNSQNLTCN SNDLKALEGF MRGLESSIDG WKWNESSSFS
SNCCDWVGIS CKSSVSLGLD DVNESGRVVE LELGRRKLSG KLSESVAKLD QLKVLNLTHN
SLSGSIAASL LNLSNLEVLD LSSNDFSGLF PSLINLPSLR VLNVYENSFH GLIPASLCNN
LPRIREIDLA MNYFDGSIPV GIGNCSSVEY LGLASNNLSG SIPQELFQLS NLSVLALQNN
RLSGALSSKL GKLSNLGRLD ISSNKFSGKI PDVFLELNKL WYFSAQSNLF NGEMPRSLSN
SRSISLLSLR NNTLSGQIYL NCSAMTNLTS LDLASNSFSG SIPSNLPNCL RLKTINFAKI
KFIAQIPESF KNFQSLTSLS FSNSSIQNIS SALEILQHCQ NLKTLVLTLN FQKEELPSVP
SLQFKNLKVL IIASCQLRGT VPQWLSNSPS LQLLDLSWNQ LSGTIPPWLG SLNSLFYLDL
SNNTFIGEIP HSLTSLQSLV SKENAVEEPS PDFPFFKKKN TNAGGLQYNQ PSSFPPMIDL
SYNSLNGSIW PEFGDLRQLH VLNLKNNNLS GNIPANLSGM TSLEVLDLSH NNLSGNIPPS
LVKLSFLSTF SVAYNKLSGP IPTGVQFQTF PNSSFEGNQG LCGEHASPCH ITDQSPHGSA
VKSKKNIRKI VAVAVGTGLG TVFLLTVTLL IILRTTSRGE VDPEKKADAD EIELGSRSVV
LFHNKDSNNE LSLDDILKST SSFNQANIIG CGGFGLVYKA TLPDGTKVAI KRLSGDTGQM
DREFQAEVET LSRAQHPNLV HLLGYCNYKN DKLLIYSYMD NGSLDYWLHE KVDGPPSLDW
KTRLRIARGA AEGLAYLHQS CEPHILHRDI KSSNILLSDT FVAHLADFGL ARLILPYDTH
VTTDLVGTLG YIPPEYGQAS VATYKGDVYS FGVVLLELLT GRRPMDVCKP RGSRDLISWV
LQMKTEKRES EIFDPFIYDK DHAEEMLLVL EIACRCLGEN PKTRPTTQQL VSWLENIDVS
S
//
