CKX2_ORYSJ
ID CKX2_ORYSJ Reviewed; 565 AA.
AC Q4ADV8; A0A0P0UZJ1; B9ETN0; Q94IV9;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cytokinin dehydrogenase 2 {ECO:0000305};
DE EC=1.5.99.12 {ECO:0000269|PubMed:15976269};
DE AltName: Full=Cytokinin oxidase 2 {ECO:0000303|PubMed:15976269};
DE Short=OsCKX2 {ECO:0000303|PubMed:15976269};
DE AltName: Full=QTL grain number 1a {ECO:0000303|PubMed:15976269};
DE Short=Gn1a {ECO:0000303|PubMed:15976269};
DE Flags: Precursor;
GN Name=CKX2 {ECO:0000303|PubMed:15976269};
GN OrderedLocusNames=Os01g0197700 {ECO:0000312|EMBL:BAS70876.1},
GN LOC_Os01g10110 {ECO:0000305};
GN ORFNames=B1046G12.8 {ECO:0000312|EMBL:BAB89407.1},
GN OsJ_00744 {ECO:0000312|EMBL:EEE54051.1},
GN P0419B01.20 {ECO:0000312|EMBL:BAB56095.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Koshihikari;
RX PubMed=15976269; DOI=10.1126/science.1113373;
RA Ashikari M., Sakakibara H., Lin S., Yamamoto T., Takashi T., Nishimura A.,
RA Angeles E.R., Qian Q., Kitano H., Matsuoka M.;
RT "Cytokinin oxidase regulates rice grain production.";
RL Science 309:741-745(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare; TISSUE=Seedling root;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP REVIEW.
RX PubMed=12721786; DOI=10.1007/s10265-003-0096-4;
RA Schmuelling T., Werner T., Riefler M., Krupkova E., Bartrina y Manns I.;
RT "Structure and function of cytokinin oxidase/dehydrogenase genes of maize,
RT rice, Arabidopsis and other species.";
RL J. Plant Res. 116:241-252(2003).
RN [8]
RP FUNCTION.
RX PubMed=28337744; DOI=10.1111/pce.12947;
RA Joshi R., Sahoo K.K., Tripathi A.K., Kumar R., Gupta B.K., Pareek A.,
RA Singla-Pareek S.L.;
RT "Knockdown of an inflorescence meristem-specific cytokinin oxidase - OsCKX2
RT in rice reduces yield penalty under salinity stress condition.";
RL Plant Cell Environ. 41:936-946(2018).
CC -!- FUNCTION: Catalyzes the oxidation of cytokinins, a family of N(6)-
CC substituted adenine derivatives that are plant hormones, where the
CC substituent is an isopentenyl group (PubMed:15976269). Is a major QTL
CC involved in grain yield (PubMed:15976269). Modulates the number of
CC reproductive organs by regulating the cytokinin accumulation in
CC inflorescence meristems (PubMed:15976269, PubMed:28337744). Acts as
CC negative regulator of panicle branching (PubMed:15976269,
CC PubMed:28337744). {ECO:0000269|PubMed:15976269,
CC ECO:0000269|PubMed:28337744}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H2O + N(6)-dimethylallyladenine = 3-methyl-2-butenal +
CC adenine + AH2; Xref=Rhea:RHEA:13625, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15825, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:17660; EC=1.5.99.12;
CC Evidence={ECO:0000269|PubMed:15976269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13626;
CC Evidence={ECO:0000269|PubMed:15976269};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9FUJ1};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:Q9FUJ3}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves, culms, inflorescence
CC meristems, and flowers, especially in vascular tissues.
CC {ECO:0000269|PubMed:15976269}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Enhanced grain production and higher cytokinin
CC levels in inflorescence meristems. {ECO:0000269|PubMed:15976269}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB56095.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB89407.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EEE54051.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EEE54051.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB205193; BAE16612.1; -; mRNA.
DR EMBL; AP003200; BAB89407.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP003244; BAB56095.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014957; BAS70876.1; -; Genomic_DNA.
DR EMBL; CM000138; EEE54051.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK243684; BAH01708.1; -; mRNA.
DR RefSeq; XP_015629416.1; XM_015773930.1.
DR AlphaFoldDB; Q4ADV8; -.
DR SMR; Q4ADV8; -.
DR STRING; 4530.OS01T0197700-01; -.
DR PaxDb; Q4ADV8; -.
DR PRIDE; Q4ADV8; -.
DR EnsemblPlants; Os01t0197700-01; Os01t0197700-01; Os01g0197700.
DR GeneID; 4327333; -.
DR Gramene; Os01t0197700-01; Os01t0197700-01; Os01g0197700.
DR KEGG; osa:4327333; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_024955_1_0_1; -.
DR InParanoid; Q4ADV8; -.
DR OMA; MANKRRN; -.
DR OrthoDB; 733611at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q4ADV8; OS.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0019139; F:cytokinin dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009690; P:cytokinin metabolic process; IEA:InterPro.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010229; P:inflorescence development; IMP:UniProtKB.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; -; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR015345; Cytokinin_DH_FAD/cytokin-bd.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF09265; Cytokin-bind; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW Cytokinin signaling pathway; Developmental protein; FAD; Flavoprotein;
KW Glycoprotein; Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..565
FT /note="Cytokinin dehydrogenase 2"
FT /id="PRO_0000394205"
FT DOMAIN 74..255
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 108..112
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT BINDING 113..114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT BINDING 118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT BINDING 179
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT BINDING 184
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT BINDING 190..194
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT BINDING 245
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT BINDING 517
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT BINDING 554..557
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT MOD_RES 113
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 565 AA; 60021 MW; 8932F516467E1CFF CRC64;
MKQEQVRMAV LLMLNCFVKA TAPPPWPPSA SSASFLDDLG DLGIAPLIRA DEAGTARASA
DFGNLSVAGV GAPRLAAAAA VLYPSRPADI AALLRASCAR PAPFAVSARG CGHSVHGQAS
APDGVVVDMA SLGRLQGGGA RRLAVSVEGR YVDAGGEQLW VDVLRASMAH GLTPVSWTDY
LHLTVGGTLS NAGISGQAFR HGPQISNVLE LDVITGVGEM VTCSKEKAPD LFDAVLGGLG
QFGVITRARI PLAPAPARAR WVRFVYTTAA AMTADQERLI AVDRAGGAGA VGGLMDYVEG
SVHLNQGLVE TWRTQPQPPS PSSSSSSSFF SDADEARVAA LAKEAGGVLY FLEGAIYFGG
AAGPSAADVD KRMDVLRREL RHERGFVFAQ DVAYAGFLDR VHDGELKLRA AGLWDVPHPW
LNLFLPRSGV LAFADGVFHG ILSRTPAMGP VLIYPMNRNK WDSNMSAVIT DDDGDEVFYT
VGILRSAAAA GDVGRLEEQN DEILGFCEVA GIAYKQYLPY YGSQAEWQKR HFGANLWPRF
VQRKSKYDPK AILSRGQGIF TSPLA
