WNK1_ORYSI
ID WNK1_ORYSI Reviewed; 704 AA.
AC A2YMV6; O81637; Q0PGM8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Probable serine/threonine-protein kinase WNK1;
DE Short=OsWNK1;
DE EC=2.7.11.1;
DE AltName: Full=Mitogen-activated protein kinase kinase 1;
DE AltName: Full=Protein kinase with no lysine 1;
GN Name=WNK1; Synonyms=MEK1; ORFNames=OsI_025649;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INDUCTION.
RC STRAIN=cv. Milyang 117;
RX PubMed=10755311; DOI=10.1094/mpmi.2000.13.4.470;
RA Kim C.Y., Lee S.-H., Park H.C., Bae C.G., Cheong Y.H., Choi Y.J., Han C.,
RA Lee S.Y., Lim C.O., Cho M.J.;
RT "Identification of rice blast fungal elicitor-responsive genes by
RT differential display analysis.";
RL Mol. Plant Microbe Interact. 13:470-474(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=cv. Pusa Basmati;
RA Kumar K., Sinha A.K.;
RT "Oryza sativa indica group with no lysine kinase 1 mRNA.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2YMV6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2YMV6-2; Sequence=VSP_035534, VSP_035535;
CC -!- INDUCTION: By fungal elicitor. {ECO:0000269|PubMed:10755311}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. WNK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Was named WNK/'with no lysine(K)' because key residues for
CC catalysis, including the lysine involved in ATP binding, are either not
CC conserved or differ compared to the residues described in other kinase
CC family proteins. {ECO:0000250|UniProtKB:Q9H4A3}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC32599.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ABH07431.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EAZ04417.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF080436; AAC32599.1; ALT_INIT; mRNA.
DR EMBL; DQ837532; ABH07431.1; ALT_INIT; mRNA.
DR EMBL; CM000132; EAZ04417.1; ALT_INIT; Genomic_DNA.
DR PIR; T02951; T02951.
DR AlphaFoldDB; A2YMV6; -.
DR SMR; A2YMV6; -.
DR STRING; 39946.A2YMV6; -.
DR PRIDE; A2YMV6; -.
DR HOGENOM; CLU_000288_142_2_1; -.
DR Proteomes; UP000007015; Chromosome 7.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..704
FT /note="Probable serine/threonine-protein kinase WNK1"
FT /id="PRO_0000351671"
FT DOMAIN 27..284
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 499..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT BINDING 107..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT VAR_SEQ 649..654
FT /note="YHSRHP -> PKGPAL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10755311, ECO:0000303|Ref.2"
FT /id="VSP_035534"
FT VAR_SEQ 655..704
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10755311, ECO:0000303|Ref.2"
FT /id="VSP_035535"
FT CONFLICT 278
FT /note="L -> V (in Ref. 1; AAC32599)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="D -> N (in Ref. 1; AAC32599)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="E -> Q (in Ref. 1; AAC32599)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="N -> T (in Ref. 1; AAC32599)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="V -> A (in Ref. 2; ABH07431)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="T -> S (in Ref. 1; AAC32599)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="D -> N (in Ref. 2; ABH07431)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="S -> C (in Ref. 1; AAC32599)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="Q -> H (in Ref. 1; AAC32599)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="E -> D (in Ref. 1; AAC32599)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="E -> D (in Ref. 1; AAC32599)"
FT /evidence="ECO:0000305"
FT CONFLICT 521..522
FT /note="DQ -> NK (in Ref. 3; EAZ04417)"
FT /evidence="ECO:0000305"
FT CONFLICT 535..539
FT /note="RRGPP -> TTRPR (in Ref. 1; AAC32599)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="A -> G (in Ref. 1; AAC32599)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 704 AA; 79761 MW; 53F50DF5CB1FBE42 CRC64;
MMGPKANAAA AGDLPEYAEV DPTGRYGRYN DVLGKGASKT VYRAFDEYQG MEVAWNQVKL
HDFLQSPEDL ERLYCEIHLL KTLKHRNIMK FYTSWVDVSR RNINFITEMF TSGTLRQYRQ
KHMRVNIWAV KHWCRQILSG LLYLHSHDPP IIHRDLKCDN IFVNGNQGEV KIGDLGLAAI
LRKSHAVHCV GTPEFMAPEV YEEEYNELVD IYSFGMCVLE MVTFEYPYSE CTHPVQIYKK
VISGTKPEAL YKVKDPMVRQ FVEKCLATAS RRLSARELLK DPFLQVDDLV FCPGDGDYSL
MNYLRQPYLE HAYSNVSMMS NGLSESIDED TPTEDRWDCE DDDIKADGID LFNGHEDEPL
GNVDITIKGR KSEDGSIFLR LRIADNDGHV RNIYFPFDIE ADTALSVATE MVAELDITDH
EVTRIAEMID GEVSALVPDW RPGPGIEESQ DTTYCHNCGS NVSSCGSLYA YMSSAARGCQ
CAELHGRFEE ITFQANGEQT DLQDSGGSSD DGGGQTQHVK DQEAVHSNGF VQMGRRGPPD
QFCFSSFQEQ SCSPRHYEYD TSLQAKGFDM KHEVKMAKYK ARKMAHLRRA IHPSLDFDNL
NGERRMKSSL NKLQSFHIGK NHNFRIPTCE RSPGARDAEE DPDIFNLAYH SRHPDPGAQR
ARHCEVDAQS SPDLMFTARS YYTGAQLPTN LPRTKSVTLN AVDA
