NCRK_ARATH
ID NCRK_ARATH Reviewed; 565 AA.
AC Q8VYY5; Q0WWT1; Q9SL30;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Receptor-like serine/threonine-protein kinase NCRK;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=NCRK; OrderedLocusNames=At2g28250; ORFNames=T3B23.8;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-565.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH ARAC5, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18088316; DOI=10.1111/j.1365-313x.2007.03384.x;
RA Molendijk A.J., Ruperti B., Singh M.K., Dovzhenko A., Ditengou F.A.,
RA Milia M., Westphal L., Rosahl S., Soellick T.R., Uhrig J., Weingarten L.,
RA Huber M., Palme K.;
RT "A cysteine-rich receptor-like kinase NCRK and a pathogen-induced protein
RT kinase RBK1 are Rop GTPase interactors.";
RL Plant J. 53:909-923(2008).
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 -!- SUBUNIT: Interacts with ARAC5. {ECO:0000269|PubMed:18088316}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18088316};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:18088316}.
CC Prevacuolar compartment membrane {ECO:0000269|PubMed:18088316}.
CC Endosome {ECO:0000269|PubMed:18088316}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaf primordia, root and shoot
CC apical meristems, lateral root primordia, and stele of older roots and
CC hypocotyls. In leaves and cotyledons, highest levels observed in
CC trichomes, vasculatures, and hydathode endothem.
CC {ECO:0000269|PubMed:18088316}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:18088316}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD29828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006202; AAD29828.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08095.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08096.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61520.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61521.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61522.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61523.1; -; Genomic_DNA.
DR EMBL; AY065457; AAL38898.1; -; mRNA.
DR EMBL; BT004417; AAO42411.1; -; mRNA.
DR EMBL; AK226256; BAE98417.1; -; mRNA.
DR PIR; F84682; F84682.
DR RefSeq; NP_001031435.1; NM_001036358.2.
DR RefSeq; NP_001323735.1; NM_001336153.1.
DR RefSeq; NP_001323736.1; NM_001336154.1.
DR RefSeq; NP_001323737.1; NM_001336155.1.
DR RefSeq; NP_001323738.1; NM_001336156.1.
DR RefSeq; NP_850115.1; NM_179784.2.
DR AlphaFoldDB; Q8VYY5; -.
DR SMR; Q8VYY5; -.
DR BioGRID; 2721; 2.
DR IntAct; Q8VYY5; 1.
DR STRING; 3702.AT2G28250.1; -.
DR iPTMnet; Q8VYY5; -.
DR PaxDb; Q8VYY5; -.
DR PRIDE; Q8VYY5; -.
DR ProteomicsDB; 251051; -.
DR EnsemblPlants; AT2G28250.1; AT2G28250.1; AT2G28250.
DR EnsemblPlants; AT2G28250.2; AT2G28250.2; AT2G28250.
DR EnsemblPlants; AT2G28250.3; AT2G28250.3; AT2G28250.
DR EnsemblPlants; AT2G28250.4; AT2G28250.4; AT2G28250.
DR EnsemblPlants; AT2G28250.5; AT2G28250.5; AT2G28250.
DR EnsemblPlants; AT2G28250.6; AT2G28250.6; AT2G28250.
DR GeneID; 817371; -.
DR Gramene; AT2G28250.1; AT2G28250.1; AT2G28250.
DR Gramene; AT2G28250.2; AT2G28250.2; AT2G28250.
DR Gramene; AT2G28250.3; AT2G28250.3; AT2G28250.
DR Gramene; AT2G28250.4; AT2G28250.4; AT2G28250.
DR Gramene; AT2G28250.5; AT2G28250.5; AT2G28250.
DR Gramene; AT2G28250.6; AT2G28250.6; AT2G28250.
DR KEGG; ath:AT2G28250; -.
DR Araport; AT2G28250; -.
DR TAIR; locus:2062824; AT2G28250.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_161_1_1; -.
DR InParanoid; Q8VYY5; -.
DR OMA; TGSWNCT; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q8VYY5; -.
DR PRO; PR:Q8VYY5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VYY5; baseline and differential.
DR Genevisible; Q8VYY5; AT.
DR GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0010089; P:xylem development; IDA:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; 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; Endosome; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..565
FT /note="Receptor-like serine/threonine-protein kinase NCRK"
FT /id="PRO_0000403329"
FT TOPO_DOM 24..103
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 210..495
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 216..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 378
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 383
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 391
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
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 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 565 AA; 62192 MW; 0927B7D0C3F91596 CRC64;
MKMRVETALA ILLVLISIQQ CYGGVSNYTC TCFSSGNRSD ILESNCSTSC NCRPDRDQWV
CLCPANGFPV IAIGGSNSSC FTSCNCSAGA TKSSKKQYLS RKLVIVILLF CGVLISLAFL
ASMICYICRK DKFSGQTPSV SSDRESSWHS SANLINRKSS VSQSKISISS SVAGCFFQNA
SLFCVSKPET IHGAIFQFSY TELEQATNKF SSNSVIGHGG SSCVYRGQLK DGKTAAIKRL
NTPKGDDTDT LFSTEVELLS RLHHYHVVPL IGYCSEFHGK HAERLLVFEY MSYGSLRDCL
DGELGEKMTW NIRISVALGA ARGLEYLHEA AAPRILHRDV KSTNILLDEN WHAKITDLGM
AKCLSSDGLQ SGSSSPTTGL QGTFGYFAPE YAIAGCASQM SDVFSFGVVL LELITGRKPI
QKPSNNKGEE SLVIWAVPRL QDSKRVIEEL PDPRLNGKFA EEEMQIMAYL AKECLLLDPE
SRPTMREVVQ ILSTITPDTS SRRRNFPINY LFQSNEKKKE SKVGWSRGGS KSGQEEETVD
LTEPRFESFC LPNVKPVLLE PSAHI
