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FZR1_ARATH
ID   FZR1_ARATH              Reviewed;         475 AA.
AC   Q8VZS9; Q9T060;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Protein FIZZY-RELATED 1;
DE   AltName: Full=Cell cycle switch protein CCS52A2;
GN   Name=FZR1; Synonyms=CCS52A2, CDH1-1; OrderedLocusNames=At4g11920;
GN   ORFNames=T26M18.130;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   REVIEW.
RX   PubMed=12597875; DOI=10.1016/s1360-1385(02)00028-6;
RA   Capron A., Okresz L., Genschik P.;
RT   "First glance at the plant APC/C, a highly conserved ubiquitin-protein
RT   ligase.";
RL   Trends Plant Sci. 8:83-89(2003).
RN   [5]
RP   FUNCTION, DEVELOPMENTAL STAGE, ASSOCIATION WITH THE APC/C COMPLEX, AND
RP   INTERACTION WITH CYCA1-1; CYCA1-2; CYCA3-4; CYCB1-1 AND CYCB1-2.
RX   PubMed=15970679;
RA   Fueloep K., Tarayre S., Kelemen Z., Horvath G., Kevei Z., Nikovics K.,
RA   Bako L., Brown S., Kondorosi A., Kondorosi E.;
RT   "Arabidopsis anaphase-promoting complexes: multiple activators and wide
RT   range of substrates might keep APC perpetually busy.";
RL   Cell Cycle 4:1084-1092(2005).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=19553203; DOI=10.1073/pnas.0901193106;
RA   Vanstraelen M., Baloban M., Da Ines O., Cultrone A., Lammens T.,
RA   Boudolf V., Brown S.C., De Veylder L., Mergaert P., Kondorosi E.;
RT   "APC/C-CCS52A complexes control meristem maintenance in the Arabidopsis
RT   root.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:11806-11811(2009).
RN   [7]
RP   REVIEW, AND GENE FAMILY.
RX   PubMed=21087491; DOI=10.1186/1471-2229-10-254;
RA   Lima M.D.F., Eloy N.B., Pegoraro C., Sagit R., Rojas C., Bretz T.,
RA   Vargas L., Elofsson A., de Oliveira A.C., Hemerly A.S., Ferreira P.C.G.;
RT   "Genomic evolution and complexity of the Anaphase-promoting Complex (APC)
RT   in land plants.";
RL   BMC Plant Biol. 10:254-254(2010).
RN   [8]
RP   INTERACTION WITH CDC20-1 AND CDC20-2.
RX   PubMed=21687678; DOI=10.1371/journal.pone.0020618;
RA   Kevei Z., Baloban M., Da Ines O., Tiricz H., Kroll A., Regulski K.,
RA   Mergaert P., Kondorosi E.;
RT   "Conserved CDC20 cell cycle functions are carried out by two of the five
RT   isoforms in Arabidopsis thaliana.";
RL   PLoS ONE 6:E20618-E20618(2011).
RN   [9]
RP   INTERACTION WITH GIG1.
RX   PubMed=22844260; DOI=10.1371/journal.pgen.1002865;
RA   Cromer L., Heyman J., Touati S., Harashima H., Araou E., Girard C.,
RA   Horlow C., Wassmann K., Schnittger A., De Veylder L., Mercier R.;
RT   "OSD1 promotes meiotic progression via APC/C inhibition and forms a
RT   regulatory network with TDM and CYCA1;2/TAM.";
RL   PLoS Genet. 8:E1002865-E1002865(2012).
CC   -!- FUNCTION: Activator protein that regulates the ubiquitin ligase
CC       activity and substrate specificity of the anaphase promoting
CC       complex/cyclosome (APC/C). Required for meristem organization and
CC       maintenance of quiescent center identity and stem cells.
CC       {ECO:0000269|PubMed:15970679, ECO:0000269|PubMed:19553203}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Associates with the APC/C complex. Interacts with CDC20-1,
CC       CDC20-2, CYCA1-1, CYCA1-2, CYCA3-4, CYCB1-1 AND CYCB1-2. Binds to GIG1.
CC       {ECO:0000269|PubMed:15970679, ECO:0000269|PubMed:21687678,
CC       ECO:0000269|PubMed:22844260}.
CC   -!- INTERACTION:
CC       Q8VZS9; Q8LGU6: CDC27B; NbExp=2; IntAct=EBI-1749329, EBI-1668733;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19553203}.
CC   -!- TISSUE SPECIFICITY: Expressed in the root tip, predominantly in the
CC       root cap, quiescent center cells, surrounding stem cells and columella.
CC       {ECO:0000269|PubMed:19553203}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from late M until late S-early G2
CC       phases. {ECO:0000269|PubMed:15970679}.
CC   -!- DISRUPTION PHENOTYPE: Stunted plants. Impaired root growth and smaller
CC       root meristem. {ECO:0000269|PubMed:19553203}.
CC   -!- MISCELLANEOUS: FZR2 controls the induction of early rounds of
CC       endoreduplication while the remaining rounds may be mediated by FZR1
CC       and FZR3.
CC   -!- MISCELLANEOUS: FZR1 and FZR2 are functional homologs, and their
CC       functional divergence in root development arises from the different
CC       expression patterns. {ECO:0000305|PubMed:19553203}.
CC   -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB44330.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78235.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Arabidopsis APC/C subunits;
CC       URL="http://personal.rhul.ac.uk/ujba/110/apc/APC.htm";
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DR   EMBL; AL078606; CAB44330.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161533; CAB78235.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE83070.1; -; Genomic_DNA.
DR   EMBL; AY063875; AAL36231.1; -; mRNA.
DR   EMBL; AY091235; AAM14174.1; -; mRNA.
DR   PIR; T09351; T09351.
DR   RefSeq; NP_192929.2; NM_117262.3.
DR   AlphaFoldDB; Q8VZS9; -.
DR   SMR; Q8VZS9; -.
DR   BioGRID; 12097; 29.
DR   IntAct; Q8VZS9; 22.
DR   STRING; 3702.AT4G11920.1; -.
DR   PaxDb; Q8VZS9; -.
DR   PRIDE; Q8VZS9; -.
DR   ProteomicsDB; 247382; -.
DR   EnsemblPlants; AT4G11920.1; AT4G11920.1; AT4G11920.
DR   GeneID; 826799; -.
DR   Gramene; AT4G11920.1; AT4G11920.1; AT4G11920.
DR   KEGG; ath:AT4G11920; -.
DR   Araport; AT4G11920; -.
DR   TAIR; locus:2137030; AT4G11920.
DR   eggNOG; KOG0305; Eukaryota.
DR   HOGENOM; CLU_014831_4_1_1; -.
DR   InParanoid; Q8VZS9; -.
DR   OMA; WNVFPGP; -.
DR   OrthoDB; 1220675at2759; -.
DR   PhylomeDB; Q8VZS9; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q8VZS9; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8VZS9; baseline and differential.
DR   Genevisible; Q8VZS9; AT.
DR   GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0010997; F:anaphase-promoting complex binding; IBA:GO_Central.
DR   GO; GO:1990757; F:ubiquitin ligase activator activity; IBA:GO_Central.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010492; P:maintenance of shoot apical meristem identity; IMP:TAIR.
DR   GO; GO:1905786; P:positive regulation of anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR   GO; GO:0032877; P:positive regulation of DNA endoreduplication; IMP:TAIR.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008361; P:regulation of cell size; IMP:TAIR.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR033010; Cdc20/Fizzy.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR19918; PTHR19918; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Mitosis; Nucleus; Reference proteome; Repeat;
KW   Ubl conjugation pathway; WD repeat.
FT   CHAIN           1..475
FT                   /note="Protein FIZZY-RELATED 1"
FT                   /id="PRO_0000364435"
FT   REPEAT          166..203
FT                   /note="WD 1"
FT   REPEAT          207..246
FT                   /note="WD 2"
FT   REPEAT          249..289
FT                   /note="WD 3"
FT   REPEAT          290..329
FT                   /note="WD 4"
FT   REPEAT          332..374
FT                   /note="WD 5"
FT   REPEAT          376..417
FT                   /note="WD 6"
FT   REPEAT          420..459
FT                   /note="WD 7"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  52330 MW;  323B3547A52C48DE CRC64;
     MEEDESTTPK KKSDSQLNLP PSMNRPTVSL ESRINRLIDS NHYHSPSKPI YSDRFIPSRS
     GSNFALFDLA SSSPNKKDGK EDGAGSYASL LKTALFGPVT PEKSDVVNGF SPSGNIFRFK
     TETQRSLNLY PPFDSDVVSG VSPSPVKSPR KILRSPYKVL DAPALQDDFY LNLVDWSAQN
     VLAVGLGNCV YLWNACSSKV TKLCDLGVDE TVCSVGWALR GTHLAIGTSS GTVQIWDVLR
     CKNIRTMEGH RLRVGALAWS SSVLSSGSRD KSILQRDIRT QEDHVSKLKG HKSEICGLKW
     SSDNRELASG GNDNKLFVWN QHSTQPVLRF CEHAAAVKAI AWSPHHFGLL ASGGGTADRC
     IRFWNTTTNT HLNCVDTNSQ VCNLVWSKNV NELVSTHGYS QNQIIVWKYP TMSKLATLTG
     HSYRVLYLAV SPDGQTIVTG AGDETLRFWN VFPSPKSQSR ESEIGALSFG RTTIR
 
 
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