CWZF7_ORYSJ
ID CWZF7_ORYSJ Reviewed; 1600 AA.
AC A0A0P0X9Z7; Q0D3R9;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Cysteine-tryptophan domain-containing zinc finger protein 7 {ECO:0000303|PubMed:28818372};
DE Short=OsCW-ZF7 {ECO:0000303|PubMed:28818372};
DE AltName: Full=Protein WIDE GRAIN 7 {ECO:0000303|PubMed:31830332};
GN Name=CWZF7 {ECO:0000303|PubMed:28818372};
GN Synonyms=WG7 {ECO:0000303|PubMed:31830332};
GN OrderedLocusNames=Os07g0669800 {ECO:0000312|EMBL:BAT03144.1},
GN LOC_Os07g47360 {ECO:0000305};
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, INTERACTION WITH TBP2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DOMAIN, AND MUTAGENESIS OF TRP-653; TRP-662 AND TRP-678.
RX PubMed=28818372; DOI=10.1016/j.plantsci.2017.06.013;
RA Zhang Z., Zhang F., Cheng Z.J., Liu L.L., Lin Q.B., Wu F.Q., Zhang H.,
RA Wang J.L., Wang J., Guo X.P., Zhang X., Lei C.L., Zhao Z.C., Zhu S.S.,
RA Wan J.M.;
RT "Functional characterization of rice CW-domain containing zinc finger
RT proteins involved in histone recognition.";
RL Plant Sci. 263:168-176(2017).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=31830332; DOI=10.1111/tpj.14646;
RA Huang Y., Bai X., Cheng N., Xiao J., Li X., Xing Y.;
RT "Wide Grain 7 increases grain width by enhancing H3K4me3 enrichment in the
RT OsMADS1 promoter in rice (Oryza sativa L.).";
RL Plant J. 102:517-528(2020).
CC -!- FUNCTION: Transcriptional activator that acts as a positive regulator
CC of grain size (PubMed:31830332). Binds directly to the DNA core
CC sequence 5'-CATTTC-3' found in the promoter of MADS1, and activates
CC MADS1 transcription (PubMed:31830332). Increases grain width via direct
CC up-regulation of MADS1 expression (PubMed:31830332). Promotes active
CC chromatin modification at the MADS1 locus by increasing its level of
CC histone H3K4me3 (PubMed:31830332). In GST pull-down assay, binds
CC specifically to histone H3K4me3, but not to H3K4me1 or H3K4me2
CC (PubMed:28818372). May facilitate the recruitment of effectors to
CC mediate gene expression (PubMed:28818372).
CC {ECO:0000269|PubMed:28818372, ECO:0000269|PubMed:31830332}.
CC -!- SUBUNIT: Interacts with TBP2, a subunit of the transcription initiation
CC factor TFIID. {ECO:0000269|PubMed:28818372}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28818372}.
CC Note=Exhibits a speckle-like distribution in the nucleus.
CC {ECO:0000269|PubMed:28818372}.
CC -!- TISSUE SPECIFICITY: Highly expressed in young panicles
CC (PubMed:28818372, PubMed:31830332). Highly expressed in axillary buds
CC (PubMed:28818372). Expressed in leaf sheaths, flag leaves, nodes and
CC internodes (PubMed:28818372). Expressed in roots, culms, leaf sheaths
CC and leaf blades (PubMed:31830332). {ECO:0000269|PubMed:28818372,
CC ECO:0000269|PubMed:31830332}.
CC -!- DOMAIN: The CW-type zinc finger domain is not required for nuclear
CC localization. {ECO:0000269|PubMed:28818372}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant size and grain size.
CC {ECO:0000269|PubMed:31830332}.
CC -!- MISCELLANEOUS: Plants silencing CWZF7 exhibit defective development of
CC awns in grains. {ECO:0000269|PubMed:28818372}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF22504.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAT03144.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP008213; BAF22504.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014963; BAT03144.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015646825.1; XM_015791339.1.
DR RefSeq; XP_015646826.1; XM_015791340.1.
DR RefSeq; XP_015646827.1; XM_015791341.1.
DR AlphaFoldDB; A0A0P0X9Z7; -.
DR SMR; A0A0P0X9Z7; -.
DR PaxDb; A0A0P0X9Z7; -.
DR EnsemblPlants; Os07t0669800-01; Os07t0669800-01; Os07g0669800.
DR GeneID; 4344236; -.
DR Gramene; Os07t0669800-01; Os07t0669800-01; Os07g0669800.
DR KEGG; osa:4344236; -.
DR eggNOG; ENOG502QS65; Eukaryota.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0080113; P:regulation of seed growth; IMP:UniProtKB.
DR InterPro; IPR011124; Znf_CW.
DR Pfam; PF07496; zf-CW; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 1: Evidence at protein level;
KW Activator; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1600
FT /note="Cysteine-tryptophan domain-containing zinc finger
FT protein 7"
FT /id="PRO_0000450710"
FT ZN_FING 647..700
FT /note="CW-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1481..1517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..824
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 656
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 659
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 680
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 692
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT MUTAGEN 653
FT /note="W->A: Abolishes binding to histone H3K4me3."
FT /evidence="ECO:0000269|PubMed:28818372"
FT MUTAGEN 662
FT /note="W->A: Abolishes binding to histone H3K4me3."
FT /evidence="ECO:0000269|PubMed:28818372"
FT MUTAGEN 678
FT /note="W->A: Abolishes binding to histone H3K4me3."
FT /evidence="ECO:0000269|PubMed:28818372"
SQ SEQUENCE 1600 AA; 175194 MW; 8BF3384B54865BDB CRC64;
MLSVRRRQED ARGVGLRGGA AAGGMEDDAE LEEGEACGDE TAFVDPDVAL SYIDEKIQDV
LGHFQKDFEG AVSAENLGSK FGGYGSFLPT YQRSPLPQTR SPPKAANVSS RSPYHQPTES
MSQNTLAVAA PSVSKHNGSM VPLSDDSSKK EVHQSTKVER ASSTQDSLNG LSKSSDHNRF
KVRIKVGSDN GLARNNAAIY SGLGLDISSP SSIEDSPDGC GSLSPEFNNV PIESPRTILQ
IMTCFSVPGG FLLSPLRDDL VQLTQKVVPT SKKWETNANT ENVQERYEGY AAKRVKSDAK
KKKAVDTKRS KSRNDVSAVM KNEIDIETPA GQKIVLEALN IPLLSNPRTM EAKDGSQFEE
DPMRDTLVEN KDARLKERTI NSDLMAIKYE NVKAEAAECL ENSGPGSSGM DFSAVKGEVK
FKAEKAEIHV EDRNTTSEKD FQSDRKQERK IKTESKCNAT GVNFEGNKVM NERTPVVGRS
IGKVSSKETL LNDINEENVS KSESRRSQKE QNMNASSSSD FLEDDRGVLS SGAVKERKND
SQSKSSHPGR KPKAKSHRDV REHLPEGSYG GKDDTLENGS GLGELRPKKI WKNDSERDSD
MPGTSKREIS SSLKNDRHTP AEEQRMHVPP SVSAPTANAA PMLPAPVVIE EHWVCCDICQ
KWRLLPYKMN PSLLPKKWKC SMLQWLPGMN RCEVSEDETT NALNALYVSP APGNGVASVG
HSHVASSGLT TSNTLNVNGH VEQSRKRKNT LSDGNVSFDV SQQMQGSVYP LSNQHAPIRS
KSAADSIQFP VERDSKSVDH FVEKKRSKSK NHGSSSDGGH LVERSKKHSK VKSKREMDHD
EYRTSKKIKK EERRQRQSGI DSNPGYDLAS GDVPDEAKAL PSKSMALQGS SERSDVPPSK
YKSVSKYNSS EKSKRSKDGD VFLPEDKNKE HSYPSDAQKP DLSSKKRIVK EWEESQHNST
PPVSKMSIVN QSSSSKETCK DQNLKETKSK LTKSEEPFAM TDSKSIKVAH SNQTSRNLNN
ELFEDSTPFA VKSGMSEPPE NRSSEQALDL AEPASSDLAY FQTTAVTSSS SKASGSQRRK
QNFHVAKTSP IESVSSSPPR ISNNDKVSHD KILGKDGSTC ANTNNMQSLV KNTEVIVDNV
RQARKSHESM LASEPVMNGF SQGNSDKDNE LPQLTQGHAS NGIISGRSLD DDLQHASGRK
DSSLKSSNAA RSHNHLHYAN KNNLLTDGSS IQHRMAVLDT KGDSMVHENK RSVTSLQDRN
GSTHYPPDGN PQSEVSFGKE KSHPKSNKHD MQNSKAQMLP SPLKESKVES HSAPLRSNAS
KLTAQLKRGN VENGGQHGIT KQAISNPADT SSPVRKDNNS TGYALKEARD LKHKANRLKE
EGKEQESTRL YFESALKYLH VASTLEPPPS IDGFKQCDAA QNLYSDTAKL CNFVGHAYEK
SKKMAAAALA YKCVEVAYLK AAYYKYPTAS KDRQMLQAIV QNPPGESPSS SASDIDNLNN
NGLSKGPSSK DANSPQVTGN NLLLAARNQP HLTRLLAYTN DVNCAFDATR KSQMAIASAA
SNQENGIDGL SSVKTVLDFN FQSVNDLLRL VRLSMESISC
