KPRO_MAIZE
ID KPRO_MAIZE Reviewed; 817 AA.
AC P17801;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Putative receptor protein kinase ZmPK1;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=PK1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. B73; TISSUE=Root;
RX PubMed=2163028; DOI=10.1038/345743a0;
RA Walker J.C., Zhang R.;
RT "Relationship of a putative receptor protein kinase from maize to the S-
RT locus glycoproteins of Brassica.";
RL Nature 345:743-746(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=8490135; DOI=10.1007/bf00023612;
RA Zhang R., Walker J.C.;
RT "Structure and expression of the S locus-related genes of maize.";
RL Plant Mol. Biol. 21:1171-1174(1993).
CC -!- FUNCTION: Probable receptor. Interaction with a ligand in the
CC extracellular domain triggers the protein kinase activity of the
CC cytoplasmic domain.
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 -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the shoots and roots of
CC young maize seedlings, and to a lesser extent in the silks.
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; X52384; CAA36611.1; -; mRNA.
DR EMBL; X67733; CAA47962.1; -; Genomic_DNA.
DR PIR; S10930; S10930.
DR RefSeq; NP_001105424.1; NM_001111954.1.
DR AlphaFoldDB; P17801; -.
DR SMR; P17801; -.
DR STRING; 4577.GRMZM2G328785_P01; -.
DR PaxDb; P17801; -.
DR PRIDE; P17801; -.
DR EnsemblPlants; Zm00001eb284380_T002; Zm00001eb284380_P002; Zm00001eb284380.
DR GeneID; 542378; -.
DR Gramene; Zm00001eb284380_T002; Zm00001eb284380_P002; Zm00001eb284380.
DR KEGG; zma:542378; -.
DR MaizeGDB; 65910; -.
DR eggNOG; ENOG502QRH4; Eukaryota.
DR HOGENOM; CLU_000288_116_2_1; -.
DR OMA; SWVAISQ; -.
DR OrthoDB; 253383at2759; -.
DR Proteomes; UP000007305; Chromosome 6.
DR ExpressionAtlas; P17801; baseline and differential.
DR Genevisible; P17801; ZM.
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-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 1.
DR Gene3D; 2.90.10.10; -; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; SSF51110; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Disulfide bond; EGF-like domain; Glycoprotein; Kinase;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT CHAIN 29..817
FT /note="Putative receptor protein kinase ZmPK1"
FT /id="PRO_0000024339"
FT TOPO_DOM 29..472
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..817
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..158
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 292..328
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 342..424
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 534..817
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 658
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 540..548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 296..308
FT /evidence="ECO:0000250"
FT DISULFID 302..316
FT /evidence="ECO:0000250"
FT DISULFID 376..398
FT /evidence="ECO:0000250"
FT DISULFID 384..386
FT /evidence="ECO:0000250"
SQ SEQUENCE 817 AA; 91120 MW; F164B44719922E67 CRC64;
MPRPLAALLS TACILSFFIA LFPRAASSRD ILPLGSSLVV ESYESSTLQS SDGTFSSGFY
EVYTHAFTFS VWYSKTEAAA ANNKTIVWSA NPDRPVHARR SALTLQKDGN MVLTDYDGAA
VWRADGNNFT GVQRARLLDT GNLVIEDSGG NTVWQSFDSP TDTFLPTQLI TAATRLVPTT
QSRSPGNYIF RFSDLSVLSL IYHVPQVSDI YWPDPDQNLY QDGRNQYNST RLGMLTDSGV
LASSDFADGQ ALVASDVGPG VKRRLTLDPD GNLRLYSMND SDGSWSVSMV AMTQPCNIHG
LCGPNGICHY SPTPTCSCPP GYATRNPGNW TEGCMAIVNT TCDRYDKRSM RFVRLPNTDF
WGSDQQHLLS VSLRTCRDIC ISDCTCKGFQ YQEGTGSCYP KAYLFSGRTY PTSDVRTIYL
KLPTGVSVSN ALIPRSDVFD SVPRRLDCDR MNKSIREPFP DVHKTGGGES KWFYFYGFIA
AFFVVEVSFI SFAWFFVLKR ELRPSELWAS EKGYKAMTSN FRRYSYRELV KATRKFKVEL
GRGESGTVYK GVLEDDRHVA VKKLENVRQG KEVFQAELSV IGRINHMNLV RIWGFCSEGS
HRLLVSEYVE NGSLANILFS EGGNILLDWE GRFNIALGVA KGLAYLHHEC LEWVIHCDVK
PENILLDQAF EPKITDFGLV KLLNRGGSTQ NVSHVRGTLG YIAPEWVSSL PITAKVDVYS
YGVVLLELLT GTRVSELVGG TDEVHSMLRK LVRMLSAKLE GEEQSWIDGY LDSKLNRPVN
YVQARTLIKL AVSCLEEDRS KRPTMEHAVQ TLLSADD
