CKI4_ORYSJ
ID CKI4_ORYSJ Reviewed; 901 AA.
AC Q75J39; Q948R7;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Serine/threonine-protein kinase-like protein CR4 {ECO:0000250|UniProtKB:Q9LX29};
DE EC=2.7.11.1 {ECO:0000269|PubMed:22899082};
DE AltName: Full=Protein CRINKLY 4 {ECO:0000303|Ref.1};
DE Short=OsCR4 {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=CR4 {ECO:0000303|Ref.1};
GN OrderedLocusNames=LOC_Os03g43670 {ECO:0000312|EMBL:ABF97796.1},
GN Os03g0637800 {ECO:0000312|EMBL:BAF12640.1};
GN ORFNames=OSJNBa0066H15.11 {ECO:0000312|EMBL:AAR01745.1},
GN OSNPB_030637800 {ECO:0000312|EMBL:BAS85402.1};
OS Oryza sativa subsp. japonica (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=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kawata M., Oikawa T., Matsumura Y., Fukumoto F., Kawasaki S., Takaiwa F.,
RA Kuroda S.;
RT "OsCR4.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP IDENTIFICATION.
RX PubMed=15549374; DOI=10.1007/s00425-004-1378-3;
RA Cao X., Li K., Suh S.-G., Guo T., Becraft P.W.;
RT "Molecular analysis of the CRINKLY4 gene family in Arabidopsis thaliana.";
RL Planta 220:645-657(2005).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=22332708; DOI=10.1111/j.1365-313x.2012.04925.x;
RA Pu C.-X., Ma Y., Wang J., Zhang Y.-C., Jiao X.-W., Hu Y.-H., Wang L.-L.,
RA Zhu Z.-G., Sun D., Sun Y.;
RT "Crinkly4 receptor-like kinase is required to maintain the interlocking of
RT the palea and lemma, and fertility in rice, by promoting epidermal cell
RT differentiation.";
RL Plant J. 70:940-953(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-532, CATALYTIC ACTIVITY,
RP AND AUTOPHOSPHORYLATION.
RX PubMed=22899082; DOI=10.4161/psb.21106;
RA Pu C.-X., Sun Y.;
RT "Rice Crinkly4 receptor-like kinase positively regulates culm elongation
RT and amino acid K532 is not essential for its kinase activity.";
RL Plant Signal. Behav. 7:1062-1064(2012).
RN [9]
RP INDUCTION BY GRF10 AND GRF6.
RC STRAIN=cv. Zhonghua 10;
RX PubMed=24596329; DOI=10.1104/pp.114.235564;
RA Liu H., Guo S., Xu Y., Li C., Zhang Z., Zhang D., Xu S., Zhang C.,
RA Chong K.;
RT "OsmiR396d-regulated OsGRFs function in floral organogenesis in rice
RT through binding to their targets OsJMJ706 and OsCR4.";
RL Plant Physiol. 165:160-174(2014).
CC -!- FUNCTION: Receptor protein kinase (PubMed:22899082). Could play a role
CC in a differentiation signal (By similarity). Controls formative cell
CC division in meristems (By similarity). Regulates epidermal cell
CC differentiation in many organs (PubMed:22332708, PubMed:22899082).
CC During floral organogenesis, required to maintain the interlocking of
CC the palea and lemma, and fertility (PubMed:22332708). Triggers culm
CC elongation (PubMed:22899082). {ECO:0000250|UniProtKB:O24585,
CC ECO:0000250|UniProtKB:Q9LX29, ECO:0000269|PubMed:22332708,
CC ECO:0000269|PubMed:22899082}.
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 Evidence={ECO:0000269|PubMed:22899082};
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; Evidence={ECO:0000269|PubMed:22899082};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9LX29}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9LX29};
CC Single-pass type I membrane protein {ECO:0000255}. Endosome,
CC multivesicular body membrane {ECO:0000250|UniProtKB:Q9LX29}; Single-
CC pass type I membrane protein {ECO:0000255}. Note=Also localized into
CC protein export bodies. {ECO:0000250|UniProtKB:Q9LX29}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the epidermal cells of
CC paleas and lemmas. {ECO:0000269|PubMed:22332708}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in young vegetative and
CC reproductive tissues, including calli, roots, seedlings, internodes,
CC leaf blades and coleoptiles as well as young panicles and kernels. But
CC low levels in 3-week-old sheaths and reproductive organs. During early
CC spikelet development, accumulates in inflorescences, especially in the
CC outermost cell layers. Present strongly in the palea and lemma
CC epidermal cell layers, mostly at the position of the interlock. Also
CC observed in reproductive organs, such as stigmas, stamens, lodicules,
CC young kernels and seed coats. {ECO:0000269|PubMed:22332708}.
CC -!- INDUCTION: Regulated by GRF10 and GRF6 at the transcription level in
CC floral organs during floret development. {ECO:0000269|PubMed:24596329}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:22899082}.
CC -!- DISRUPTION PHENOTYPE: Abnormal epidermis cells walls with discontinuous
CC cuticles, leading to irregular architecture and organ self-fusion
CC resulting in distorted interlocking structures of the palea and lemma
CC which accumulates abnormal levels of anthocyanin after heading. Delayed
CC separation of the palea and lemma at later spikelet stages. Severe
CC interruption of pistil pollination and damage to the development of
CC embryo and endosperm, with defects in aleurone and reduced seed
CC fertility (PubMed:22332708). Reduced stature due to shorter primary and
CC lateral tillers (PubMed:22899082). {ECO:0000269|PubMed:22332708,
CC ECO:0000269|PubMed:22899082}.
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; AB057787; BAB68389.1; -; Genomic_DNA.
DR EMBL; AC120505; AAR01745.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF97796.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12640.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS85402.1; -; Genomic_DNA.
DR RefSeq; XP_015628681.1; XM_015773195.1.
DR AlphaFoldDB; Q75J39; -.
DR SMR; Q75J39; -.
DR STRING; 4530.OS03T0637800-01; -.
DR iPTMnet; Q75J39; -.
DR PaxDb; Q75J39; -.
DR PRIDE; Q75J39; -.
DR EnsemblPlants; Os03t0637800-01; Os03t0637800-01; Os03g0637800.
DR GeneID; 4333525; -.
DR Gramene; Os03t0637800-01; Os03t0637800-01; Os03g0637800.
DR KEGG; osa:4333525; -.
DR eggNOG; ENOG502QUN0; Eukaryota.
DR HOGENOM; CLU_009948_0_0_1; -.
DR InParanoid; Q75J39; -.
DR OMA; TPAHFPF; -.
DR OrthoDB; 684563at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0009986; C:cell surface; IEA:EnsemblPlants.
DR GO; GO:0030139; C:endocytic vesicle; IEA:EnsemblPlants.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR GO; GO:0004672; F:protein kinase activity; IDA: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:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
DR GO; GO:0048439; P:flower morphogenesis; IMP:UniProtKB.
DR GO; GO:0010311; P:lateral root formation; IEA:EnsemblPlants.
DR GO; GO:0090627; P:plant epidermal cell differentiation; IMP:UniProtKB.
DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IEA:EnsemblPlants.
DR GO; GO:0048829; P:root cap development; IEA:EnsemblPlants.
DR Gene3D; 2.130.10.30; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00208; TNFR; 1.
DR SUPFAM; SSF50985; SSF50985; 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.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Developmental protein; Disulfide bond;
KW Endosome; Glycoprotein; Kinase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..901
FT /note="Serine/threonine-protein kinase-like protein CR4"
FT /id="PRO_5007710260"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 31..66
FT /note="1"
FT /evidence="ECO:0000250|UniProtKB:O24585"
FT REPEAT 70..105
FT /note="2"
FT /evidence="ECO:0000250|UniProtKB:O24585"
FT REPEAT 123..158
FT /note="3"
FT /evidence="ECO:0000250|UniProtKB:O24585"
FT REPEAT 160..193
FT /note="4"
FT /evidence="ECO:0000250|UniProtKB:O24585"
FT REPEAT 201..234
FT /note="5"
FT /evidence="ECO:0000250|UniProtKB:O24585"
FT REPEAT 251..285
FT /note="6"
FT /evidence="ECO:0000250|UniProtKB:O24585"
FT REPEAT 290..328
FT /note="7"
FT /evidence="ECO:0000250|UniProtKB:O24585"
FT REPEAT 335..389
FT /note="TNFR-Cys"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DOMAIN 504..781
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 31..328
FT /note="7 X 36 AA repeats"
FT /evidence="ECO:0000250|UniProtKB:O24585"
FT REGION 845..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 633
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 510..518
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 336..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 367..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 371..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT MUTAGEN 532
FT /note="K->M: Normal autophosphorylation."
FT /evidence="ECO:0000269|PubMed:22899082"
SQ SEQUENCE 901 AA; 97772 MW; 1D3452E7023D9815 CRC64;
MDIVPVVALC CCLVLLPSWA YGLGSMASIA VSYGEDGPVF CGLNSDGSHL VTCFGADASV
VYGAPSRIPF VGVTAGDGFA CGLLLDTNQP YCWGSNSYVK IGVPQPMVEG AMYSELSAGD
NHLCALRTSV KGFHSVNGDT SVIDCWGYNM TATHTVTGAV SAISAGSVFN CGLFARNRTV
FCWGDESVSG VIGLAPRNVR FQSIGAGGYH VCGVLENAQV FCWGRSLEMQ QMSTPSSTDD
GDVNIVPMDA MVSVVGGRFH ACGIRSLDHQ VACWGFTLQN STLAPKGLRV YAIVAGDYFT
CGVPAETSLK PMCWGHSGPL ALPMAVSPGI CVSDSCSHGY YEYANHGEVG SGSKTCKPAN
SRLCLPCSVG CPDDSYESSP CNATADRVCQ FDCSKCASDE CVSFCLSQKR TKNRKFMAFQ
LRIFVAEIAF AVILVFSVTA IACLYVRYKL RHCQCSKNEL RLAKNTTYSF RKDNMKIQPD
VEDLKIRRAQ EFSYEELEQA TGGFSEDSQV GKGSFSCVFK GILRDGTVVA VKRAIKASDV
KKSSKEFHTE LDLLSRLNHA HLLNLLGYCE DGSERLLVYE FMAHGSLYQH LHGKDPNLKK
RLNWARRVTI AVQAARGIEY LHGYACPPVI HRDIKSSNIL IDEDHNARVA DFGLSILGPA
DSGTPLSELP AGTLGYLDPE YYRLHYLTTK SDVYSFGVVL LEILSGRKAI DMQFEEGNIV
EWAVPLIKAG DISALLDPVL SPPSDLEALK KIAAVACKCV RMRAKDRPSM DKVTTALERA
LALLMGSPCI EQPILPTEVV LGSSRMHKKV SQRSSNHSCS ENDLVDGDDQ RIEYRAPSWI
TFPSVTSSQR RKSSASEADM DGRTTTDGRN VGSSIGDGLR SLEEEISPAS PQENLYLQHN
F
