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CWZF3_ORYSJ
ID   CWZF3_ORYSJ             Reviewed;         902 AA.
AC   Q0DRX6; A0A0P0VY74; Q10LI9;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2020, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Cysteine-tryptophan domain-containing zinc finger protein 3 {ECO:0000303|PubMed:28818372};
DE            Short=OsCW-ZF3 {ECO:0000303|PubMed:28818372};
GN   Name=CWZF3 {ECO:0000303|PubMed:28818372};
GN   OrderedLocusNames=Os03g0347300 {ECO:0000312|EMBL:BAF12012.1},
GN   LOC_Os03g22580 {ECO:0000312|EMBL:ABF95911.1};
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 [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   [2]
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   [3]
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   [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   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, AND MUTAGENESIS
RP   OF TRP-27; TRP-36 AND TRP-52.
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).
CC   -!- FUNCTION: Binds to histones H3K4me1, H3K4me2 and H3K4me3 in GST pull-
CC       down assay (PubMed:28818372). May facilitate the recruitment of
CC       effectors to mediate gene expression (By similarity).
CC       {ECO:0000250|UniProtKB:A0A0P0X9Z7, ECO:0000269|PubMed:28818372}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28818372}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaf sheaths, flag leaves, nodes,
CC       internodes and panicles. {ECO:0000269|PubMed:28818372}.
CC   -!- DOMAIN: The CW-type zinc finger domain is not required for nuclear
CC       localization. {ECO:0000269|PubMed:28818372}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAS84173.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DP000009; ABF95911.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF12012.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS84173.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q0DRX6; -.
DR   SMR; Q0DRX6; -.
DR   STRING; 4530.OS03T0347300-01; -.
DR   EnsemblPlants; Os03t0347300-01; Os03t0347300-01; Os03g0347300.
DR   Gramene; Os03t0347300-01; Os03t0347300-01; Os03g0347300.
DR   eggNOG; ENOG502SC6K; Eukaryota.
DR   HOGENOM; CLU_014232_0_0_1; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR011124; Znf_CW.
DR   Pfam; PF07496; zf-CW; 1.
DR   PROSITE; PS51050; ZF_CW; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..902
FT                   /note="Cysteine-tryptophan domain-containing zinc finger
FT                   protein 3"
FT                   /id="PRO_0000450711"
FT   ZN_FING         21..74
FT                   /note="CW-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   REGION          131..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..206
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..600
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..629
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..648
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   MUTAGEN         27
FT                   /note="W->A: Abolishes binding to histone H3K4me1/2/3."
FT                   /evidence="ECO:0000269|PubMed:28818372"
FT   MUTAGEN         36
FT                   /note="W->A: Abolishes binding to histone H3K4me1/2/3."
FT                   /evidence="ECO:0000269|PubMed:28818372"
FT   MUTAGEN         52
FT                   /note="W->A: Abolishes binding to histone H3K4me1/2/3."
FT                   /evidence="ECO:0000269|PubMed:28818372"
SQ   SEQUENCE   902 AA;  99539 MW;  7087E83C790849F4 CRC64;
     MPSNGGIIPG PANAASLPAP VLIEDNWVCC DMCHKWRLLP YGTNTSMLPK KWICSMLDWL
     PGMNKCDISE DETTNALNAL YVTQIPAAGV SSGGPHTAHA SVAASSTYNI SGQLGQSRKR
     KNALKDENCY EHDQQAPAKM TLTSNQQAPA KNREVVDSEH YTNDRDPVST HDLVPQSKSA
     SERHKSKHKS RSSHSDGGDL TEKSKKHSKS KNRRGIDRDE HKTSKKTKKE DRHYFNKDWK
     NEYDLAGNKV RDETKALSAK AKMSKDSCEQ DEFSLRKEKA SRFDILEKTK RINDDDVAFH
     EKMKEHRAGI ETLDLSGKKK TVKEWEDNRL SSMDHTSKGG DNENLNERLS KIKKSEARPE
     EVQDANALFS SAGRRQDNEL VADNKFVTCK EGPSELWDNQ PPRQVLNLAE PTRRDVACLQ
     SSTVATSSSS KVSSSRRNKN SREAKGSPVE SVSSSPLKNS NTDKISKARK TGKDGELNAD
     SSILHTPMKY PTHEVGLLHT GQQAVGEAIL RGSTNNSGMG RVDNQLYPGD KKILDMHGPT
     LQPDQQDCFN PRATADSTGH KSKNSAPSRQ GRNGSSNLIS EGNKQIEMSS RKEKLRPSID
     NQDMQKSIGQ DNHSHMKEGK SEVHTTRVKP GASKNHTQLR SNVENGDSAS PIRRDGNMIA
     FALKEARDLK HKANHLKEKG LELESMGLYF EAALKFLHVA SLWETPNLDN SRSGDVAQSM
     KMYSETAKLC SFCAHAYERC NKMASAALAY KCVEVAYLKA AYYKHPSASK DRQELQSVVQ
     IAPGESPSSS ASDIDNLNSH GLSKALSTKG GNSPQVAGNH LPLAVRNQAH LLRLLAYTND
     VNCAFDATRK SQVAIASAAS SQERGKTVDD GLASVRTVLD FNFNNVNELL RLVRLSMELI
     NT
 
 
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