ID CRK16_ARATH Reviewed; 662 AA.
AC O65476; F4JNG9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=Putative cysteine-rich receptor-like protein kinase 16;
DE Short=Cysteine-rich RLK16;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=CRK16; OrderedLocusNames=At4g23240; ORFNames=F21P8.130;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=11402176; DOI=10.1104/pp.126.2.473;
RA Chen Z.;
RT "A superfamily of proteins with novel cysteine-rich repeats.";
RL Plant Physiol. 126:473-476(2001).
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;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CRK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18471.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79279.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022347; CAA18471.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161559; CAB79279.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84727.2; -; Genomic_DNA.
DR PIR; T04841; T04841.
DR RefSeq; NP_001320041.1; NM_001341588.1.
DR AlphaFoldDB; O65476; -.
DR SMR; O65476; -.
DR STRING; 3702.O65476; -.
DR GlyCosmos; O65476; 7 sites, No reported glycans.
DR PaxDb; 3702-AT4G23240-1; -.
DR EnsemblPlants; AT4G23240.1; AT4G23240.1; AT4G23240.
DR GeneID; 828423; -.
DR Gramene; AT4G23240.1; AT4G23240.1; AT4G23240.
DR KEGG; ath:AT4G23240; -.
DR Araport; AT4G23240; -.
DR TAIR; AT4G23240; CRK16.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_3_1; -.
DR InParanoid; O65476; -.
DR OrthoDB; 687002at2759; -.
DR PhylomeDB; O65476; -.
DR PRO; PR:O65476; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65476; baseline and differential.
DR Genevisible; O65476; AT.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27002:SF1010; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 16-RELATED; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01657; Stress-antifung; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51473; GNK2; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..662
FT /note="Putative cysteine-rich receptor-like protein kinase
FT 16"
FT /id="PRO_0000295063"
FT TOPO_DOM 27..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..131
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 137..244
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 335..612
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 460
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 341..349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
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 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 662 AA; 74586 MW; A6CFEFFC82DCD5B0 CRC64;
MIFIMKLKNL LPIFCFFLVS FSISSAQKCG KTGLFKPNDK YDINRHLLLS SLASNVSARG
GFYNASIGQG PDRLYASGTC IQGSEPELCS ACIDSAFIRV IKKCHNQTEA LDWSSFNEEY
PCMIRYSNRS FFGLLEMTPF FKNYNATDFQ VNLTEFYQKW EALMLGVIAD AISSPNPKFY
GAGTGKIGIQ TVYAFVLCSK DISPWNCSRC LRGNVDNYKL SCSGKPRGHS FSPSCYMRWD
LYQFYGFIEY RASPTLPREK GRISELSDDG GKISTRNILG ITVALAFFIT VLLVLGYALS
RRRKAYQEFA TENDITTSGS LQFDFKAIEA ATNNFQKSNK LGHGGFGEVF KGTFPNGTEV
AVKRLSKISG QGEEEFKNEV LLVAKLQHRN LVRLLGFSVE GEEKILVYEY MPNKSLDYFL
FDHRRRGQLD WRTRYNIIRG VTRGILYLHQ DSRLTIIHRD LKAGNILLDV DMNPKIADFG
VARNFRVDQT EATTGRVVGT FGYMPPEYVA NGQFSMKSDV YSFGVLILEI IVGKKSSSFH
EIDGSVGNLV TYVWRLWNNE SFLELVDPAM GESYDKDEVI RCIHISLLCV QENPADRPTM
STVFQMLTNT FLTLPVPQLP GFVFRVRSEP NPLAERLEPG PSTTMSFACS IDDASITSVD
LR
//
