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PSKR1_DAUCA
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   03-AUG-2022, entry version 108.
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   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:0050832; P:defense response to fungus; IEA:UniProt.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 3.80.10.10; -; 2.
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   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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
 
 
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