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PUB24_ORYSJ
ID   PUB24_ORYSJ             Reviewed;         824 AA.
AC   Q10FT0; Q7Y097;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=U-box domain-containing protein 24 {ECO:0000305};
DE            EC=2.3.2.27 {ECO:0000269|PubMed:30920691};
DE   AltName: Full=Plant U-box protein 24 {ECO:0000303|PubMed:30920691};
DE            Short=OsPUB24 {ECO:0000303|PubMed:30920691};
DE   AltName: Full=RING-type E3 ubiquitin transferase PUB24 {ECO:0000305};
GN   Name=PUB24 {ECO:0000303|PubMed:30920691};
GN   OrderedLocusNames=Os03g0657100 {ECO:0000312|EMBL:BAF12727.1},
GN   LOC_Os03g45420 {ECO:0000312|EMBL:ABF97977.1};
GN   ORFNames=OSJNBa0075A22.19 {ECO:0000312|EMBL:AAP50990.1};
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, CATALYTIC ACTIVITY, INTERACTION WITH BZR1; BZR2; BZR3 AND GSK2,
RP   SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AUTOUBIQUITINATION,
RP   PHOSPHORYLATION, AND MUTAGENESIS OF CYS-20.
RX   PubMed=30920691; DOI=10.1111/tpj.14332;
RA   Min H.J., Cui L.H., Oh T.R., Kim J.H., Kim T.W., Kim W.T.;
RT   "OsBZR1 turnover mediated by OsSK22-regulated U-box E3 ligase OsPUB24 in
RT   rice BR response.";
RL   Plant J. 99:426-438(2019).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that functions as a negative
CC       regulator of brassinosteroid (BR) signaling (PubMed:30920691). Targets
CC       BZR1, a positive regulator of BR signaling pathway, and promotes its
CC       degradation via the ubiquitin-26S proteasome pathway (PubMed:30920691).
CC       {ECO:0000269|PubMed:30920691}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000269|PubMed:30920691};
CC   -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC   -!- SUBUNIT: Interacts with BZR1, BZR2, BZR3 and GSK2.
CC       {ECO:0000269|PubMed:30920691}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30920691}.
CC       Nucleus {ECO:0000269|PubMed:30920691}.
CC   -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:30920691}.
CC   -!- PTM: Phosproylated by GSK2 (PubMed:30920691). Phosphorylation of PUB24
CC       increases its cellular stability (PubMed:30920691).
CC       {ECO:0000269|PubMed:30920691}.
CC   -!- DISRUPTION PHENOTYPE: Pleiotropic phenotypes, such as reduced height,
CC       enlarged lamina joint angles, increased tiller number, decreased
CC       panicle length and reduced primary branches per panicle, due to
CC       hypersensitivity to brassinosteroid. {ECO:0000269|PubMed:30920691}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP50990.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC133859; AAP50990.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000009; ABF97977.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF12727.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS85568.1; -; Genomic_DNA.
DR   RefSeq; XP_015631680.1; XM_015776194.1.
DR   AlphaFoldDB; Q10FT0; -.
DR   SMR; Q10FT0; -.
DR   STRING; 4530.OS03T0657100-01; -.
DR   PaxDb; Q10FT0; -.
DR   PRIDE; Q10FT0; -.
DR   EnsemblPlants; Os03t0657100-01; Os03t0657100-01; Os03g0657100.
DR   GeneID; 4333620; -.
DR   Gramene; Os03t0657100-01; Os03t0657100-01; Os03g0657100.
DR   KEGG; osa:4333620; -.
DR   eggNOG; KOG0167; Eukaryota.
DR   HOGENOM; CLU_004912_0_0_1; -.
DR   InParanoid; Q10FT0; -.
DR   OMA; ECRENGQ; -.
DR   OrthoDB; 268677at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   ExpressionAtlas; Q10FT0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd16664; RING-Ubox_PUB; 1.
DR   Gene3D; 1.25.10.10; -; 3.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR045210; RING-Ubox_PUB.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00185; ARM; 9.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF48371; SSF48371; 2.
DR   PROSITE; PS51698; U_BOX; 1.
PE   1: Evidence at protein level;
KW   Brassinosteroid signaling pathway; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..824
FT                   /note="U-box domain-containing protein 24"
FT                   /id="PRO_0000448266"
FT   DOMAIN          13..92
FT                   /note="U-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01034"
FT   REPEAT          133..172
FT                   /note="ARM 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          175..214
FT                   /note="ARM 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          217..258
FT                   /note="ARM 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          260..299
FT                   /note="ARM 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          300..339
FT                   /note="ARM 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          341..385
FT                   /note="ARM 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          396..435
FT                   /note="ARM 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          441..481
FT                   /note="ARM 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          486..525
FT                   /note="ARM 9"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         20
FT                   /note="C->Y: Loss of E3 ubiquitin-protein ligase activity."
FT                   /evidence="ECO:0000269|PubMed:30920691"
SQ   SEQUENCE   824 AA;  88483 MW;  B08D77AF82B1D039 CRC64;
     MAGEGVEMSE EEGAFEAFVC PLTKQVMRDP VTIETGQTFE REAILKWFRE CRDNGRRPTC
     PLTQRELRDT EVSPSVALRS VIHEWRARNE EKDLDRACAS LVGGFAGHAG DEEEEESALR
     ALVHVSQICQ RSAASKDLVR RRGVLRAVAE MLKSGSRRLR LKSLQVLRVL VEDNDDNKEE
     LGKGDTIRTI IKFLSNEHVQ ERELAVSLLH ELSGHEPTCE RIGAVYGAIL LLVGMGSSKS
     ESAVAVDKAE STLRNLDRFD ANVKQMADNG RLQPLLTRLL RGEPDTRVAM ADYLGELALA
     NDDKAAVAEQ AGPLLVGMLR TGATPAKEAT LKALREISSS EASAKLLLQR AGVLPPLVND
     VLFSTGHLPM KLKELAATIL ANLVASGADF RSIPLDDDED DDGGGGGRGR RRTLLSEDVV
     HSQLHLISNT GPAIGCRLLS VLAGLTSSRA TVADVVAAVK SSGATISLIQ FIEAAHRDIR
     VESLKLLRNL APYMGAELAD ALGGSLSSLL RAISSDGGGV TEEQAAAVGL LGDLPEGDSS
     LTRQLFDLGA FRALAPKLAE LRRGTIRGGN RYVTPLTEGV VKVMYRVTCA LEEDAEYVEF
     AREAGLAPLF VELLHTNGMD TVQLYSAMAL EKLSLQSSHL TAIPAPPSPP AGFGCACLGR
     RPAAAAVPAG VCRVHGGFCS LRETFCLAQA DGGKAVERLV ACLDHLDGRV VEAALAALST
     LVCDGVDARE GVVVLGEADG LRPVVDIMVE SRTEALQRRA VWAVERILRV EEIAGEVAAD
     QTVASALVEA YRNGDPRTRQ TAERALRHLD RIPNFSAAFQ SKRS
 
 
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