ZRK6_ARATH
ID ZRK6_ARATH Reviewed; 378 AA.
AC Q9SVZ0; B9DGQ0; B9DHG2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Non-functional pseudokinase ZRK6 {ECO:0000303|PubMed:26355215, ECO:0000303|PubMed:28499073};
GN Name=ZRK6 {ECO:0000303|PubMed:26355215, ECO:0000303|PubMed:28499073};
GN OrderedLocusNames=At3g57760 {ECO:0000312|Araport:AT3G57760};
GN ORFNames=F15B8.50 {ECO:0000312|EMBL:CAB41179.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP INTERACTION WITH RPP13L4/ZAR1, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=26355215; DOI=10.1016/j.chom.2015.08.004;
RA Wang G., Roux B., Feng F., Guy E., Li L., Li N., Zhang X., Lautier M.,
RA Jardinaud M.-F., Chabannes M., Arlat M., Chen S., He C., Noel L.D.,
RA Zhou J.-M.;
RT "The decoy substrate of a pathogen effector and a pseudokinase specify
RT pathogen-induced modified-self recognition and immunity in plants.";
RL Cell Host Microbe 18:285-295(2015).
RN [6]
RP INDUCTION BY ELEVATED TEMPERATURE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=28499073; DOI=10.1111/nph.14585;
RA Wang Z., Cui D., Liu J., Zhao J., Liu C., Xin W., Li Y., Liu N., Ren D.,
RA Tang D., Hu Y.;
RT "Arabidopsis ZED1-related kinases mediate the temperature-sensitive
RT intersection of immune response and growth homeostasis.";
RL New Phytol. 215:711-724(2017).
CC -!- SUBUNIT: Interacts with RPP13L4/ZAR1. {ECO:0000269|PubMed:26355215}.
CC -!- INDUCTION: Induced by elevated temperature (e.g. at 25 degrees
CC Celsius). {ECO:0000269|PubMed:28499073}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. ZRK subfamily. {ECO:0000305}.
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DR EMBL; AL049660; CAB41179.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79695.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79696.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79697.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63888.1; -; Genomic_DNA.
DR EMBL; AF372966; AAK50103.1; -; mRNA.
DR EMBL; BT002229; AAN72240.1; -; mRNA.
DR EMBL; AK317236; BAH19917.1; -; mRNA.
DR EMBL; AK317514; BAH20179.1; -; mRNA.
DR PIR; T06744; T06744.
DR RefSeq; NP_001030879.1; NM_001035802.1.
DR RefSeq; NP_001030880.1; NM_001035803.1.
DR RefSeq; NP_001319784.1; NM_001339885.1.
DR RefSeq; NP_191335.1; NM_115636.1.
DR AlphaFoldDB; Q9SVZ0; -.
DR SMR; Q9SVZ0; -.
DR STRING; 3702.AT3G57760.2; -.
DR PaxDb; Q9SVZ0; -.
DR PRIDE; Q9SVZ0; -.
DR EnsemblPlants; AT3G57760.1; AT3G57760.1; AT3G57760.
DR EnsemblPlants; AT3G57760.2; AT3G57760.2; AT3G57760.
DR EnsemblPlants; AT3G57760.3; AT3G57760.3; AT3G57760.
DR EnsemblPlants; AT3G57760.4; AT3G57760.4; AT3G57760.
DR GeneID; 824945; -.
DR Gramene; AT3G57760.1; AT3G57760.1; AT3G57760.
DR Gramene; AT3G57760.2; AT3G57760.2; AT3G57760.
DR Gramene; AT3G57760.3; AT3G57760.3; AT3G57760.
DR Gramene; AT3G57760.4; AT3G57760.4; AT3G57760.
DR KEGG; ath:AT3G57760; -.
DR Araport; AT3G57760; -.
DR TAIR; locus:2076631; AT3G57760.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q9SVZ0; -.
DR OMA; CCDGKCN; -.
DR OrthoDB; 778960at2759; -.
DR PhylomeDB; Q9SVZ0; -.
DR PRO; PR:Q9SVZ0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SVZ0; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009266; P:response to temperature stimulus; IEP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR045274; WAK-like.
DR PANTHER; PTHR27005; PTHR27005; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..378
FT /note="Non-functional pseudokinase ZRK6"
FT /id="PRO_0000449493"
FT DOMAIN 34..378
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 55
FT /note="F -> L (in Ref. 4; BAH19917)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="D -> G (in Ref. 4; BAH20179)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="K -> R (in Ref. 4; BAH19917)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 43084 MW; 90A47E31B54F7C30 CRC64;
MDWLRTKRIR AKKRKRNVKE NGEVVLKELI ECCDGKCNPI KNFSYDQIIK ATNNFCQSNR
ASRIDVYYRC YKGMLDDRPV LIKKGKYTLD MKEICRDIAI SSMVSGHKNF LKLLGCCLEF
TPPVLVFEYA EVITLGPLLT SHPGYLRRIK IAREVANALT YLHTAFSRVF IHSNLDPFTI
FLDGNGVAKL GNFCNCITIP EGETFVHDDT LQKYHELRHN TLKGTHGLGV CNLPVIDPDY
KSTGKVTTKT DMHSFGGFML ALVQIREVDD ELSLSSDMLR ALADLFIKPY DDVRYVHFPL
HHHVSKILRK FGYAEVVDSD MSEVAAWPIK AFLRLALRCI GCKLGDPLSS MIQVTKELRL
IEKSAYYPSN NRSQMSSI
