CD27B_ARATH
ID CD27B_ARATH Reviewed; 744 AA.
AC Q8LGU6; Q8W4M8; Q9SL81;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cell division cycle protein 27 homolog B;
DE Short=CDC27 homolog B;
DE AltName: Full=Protein HOBBIT;
GN Name=CDC27B; Synonyms=HBT; OrderedLocusNames=At2g20000; ORFNames=T2G17.20;
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 [MRNA], AND FUNCTION.
RX PubMed=12368267; DOI=10.1101/gad.237302;
RA Blilou I., Frugier F., Folmer S., Serralbo O., Willemsen V., Wolkenfelt H.,
RA Eloy N.B., Ferreira P.C., Weisbeek P., Scheres B.;
RT "The Arabidopsis HOBBIT gene encodes a CDC27 homolog that links the plant
RT cell cycle to progression of cell differentiation.";
RL Genes Dev. 16:2566-2575(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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 [5]
RP FUNCTION, INTERACTION WITH APC2; APC10; FZR2 AND FZR3, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17944809; DOI=10.1111/j.1365-313x.2007.03312.x;
RA Perez-Perez J.M., Serralbo O., Vanstraelen M., Gonzalez C., Criqui M.C.,
RA Genschik P., Kondorosi E., Scheres B.;
RT "Specialization of CDC27 function in the Arabidopsis thaliana anaphase-
RT promoting complex (APC/C).";
RL Plant J. 53:78-89(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SAMBA.
RX PubMed=22869741; DOI=10.1073/pnas.1211418109;
RA Eloy N.B., Gonzalez N., Van Leene J., Maleux K., Vanhaeren H., De Milde L.,
RA Dhondt S., Vercruysse L., Witters E., Mercier R., Cromer L., Beemster G.T.,
RA Remaut H., Van Montagu M.C., De Jaeger G., Ferreira P.C., Inze D.;
RT "SAMBA, a plant-specific anaphase-promoting complex/cyclosome regulator is
RT involved in early development and A-type cyclin stabilization.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:13853-13858(2012).
RN [7]
RP INTERACTION WITH PANS1.
RX PubMed=24206843; DOI=10.1016/j.cub.2013.08.036;
RA Cromer L., Jolivet S., Horlow C., Chelysheva L., Heyman J., De Jaeger G.,
RA Koncz C., De Veylder L., Mercier R.;
RT "Centromeric cohesion is protected twice at meiosis, by SHUGOSHINs at
RT anaphase I and by PATRONUS at interkinesis.";
RL Curr. Biol. 23:2090-2099(2013).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex
CC that controls progression through mitosis and the G1 phase of the cell
CC cycle. The APC/C complex controls several key steps in the cell cycle
CC by mediating ubiquitination and subsequent degradation of target
CC proteins such as cyclins. The APC/C complex is required for the female
CC gametophyte development and is involved in several aspect of
CC development by controlling cell division and cell elongation. Involved
CC in the control of endoreduplication. Functionally redundant with CDC27A
CC in the control of gametophyte development.
CC {ECO:0000269|PubMed:12368267, ECO:0000269|PubMed:17944809}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The APC/C is composed of at least 10 subunits (By similarity).
CC Can homodimerize (By similarity). Interacts with APC2, APC10, FZR2 and
CC FZR3 (PubMed:17944809). Interacts with PANS1 (PubMed:24206843).
CC Interacts with SAMBA (PubMed:22869741). {ECO:0000250,
CC ECO:0000269|PubMed:17944809, ECO:0000269|PubMed:22869741,
CC ECO:0000269|PubMed:24206843}.
CC -!- INTERACTION:
CC Q8LGU6; Q9ZPW2: APC10; NbExp=3; IntAct=EBI-1668733, EBI-1749354;
CC Q8LGU6; Q8H1U5: APC2; NbExp=3; IntAct=EBI-1668733, EBI-1749410;
CC Q8LGU6; Q9SZA4: CDC20-1; NbExp=2; IntAct=EBI-1668733, EBI-1668707;
CC Q8LGU6; Q8VZS9: FZR1; NbExp=2; IntAct=EBI-1668733, EBI-1749329;
CC Q8LGU6; Q8LPL5: FZR3; NbExp=2; IntAct=EBI-1668733, EBI-1749341;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17944809}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in dividing and elongating
CC cells. {ECO:0000269|PubMed:17944809}.
CC -!- DISRUPTION PHENOTYPE: Dwarf plant with small leaves and stunted growth.
CC Defect in cell division and expansion. Defective endoreduplication.
CC Cdc27a and cdc27b double mutant is gametophytic lethal
CC (PubMed:17944809). {ECO:0000269|PubMed:17944809}.
CC -!- SIMILARITY: Belongs to the APC3/CDC27 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD24396.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAL32548.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAM91180.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AJ487669; CAD31951.1; -; mRNA.
DR EMBL; AC006081; AAD24396.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06953.1; -; Genomic_DNA.
DR EMBL; AY062470; AAL32548.1; ALT_SEQ; mRNA.
DR EMBL; AY128780; AAM91180.1; ALT_SEQ; mRNA.
DR PIR; G84583; G84583.
DR RefSeq; NP_849994.1; NM_179663.3.
DR AlphaFoldDB; Q8LGU6; -.
DR SMR; Q8LGU6; -.
DR BioGRID; 1874; 18.
DR ELM; Q8LGU6; -.
DR IntAct; Q8LGU6; 21.
DR STRING; 3702.AT2G20000.1; -.
DR iPTMnet; Q8LGU6; -.
DR PaxDb; Q8LGU6; -.
DR PRIDE; Q8LGU6; -.
DR ProteomicsDB; 223968; -.
DR EnsemblPlants; AT2G20000.1; AT2G20000.1; AT2G20000.
DR GeneID; 816519; -.
DR Gramene; AT2G20000.1; AT2G20000.1; AT2G20000.
DR KEGG; ath:AT2G20000; -.
DR Araport; AT2G20000; -.
DR TAIR; locus:2061649; AT2G20000.
DR eggNOG; KOG1126; Eukaryota.
DR HOGENOM; CLU_008850_1_1_1; -.
DR InParanoid; Q8LGU6; -.
DR OMA; ADKRHYN; -.
DR OrthoDB; 280620at2759; -.
DR PhylomeDB; Q8LGU6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8LGU6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8LGU6; baseline and differential.
DR Genevisible; Q8LGU6; AT.
DR GO; GO:0005680; C:anaphase-promoting complex; IPI:TAIR.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005819; C:spindle; IDA:TAIR.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IMP:TAIR.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0048829; P:root cap development; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0010071; P:root meristem specification; IMP:TAIR.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Mitosis; Nucleus; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..744
FT /note="Cell division cycle protein 27 homolog B"
FT /id="PRO_0000396840"
FT REPEAT 101..134
FT /note="TPR 1"
FT REPEAT 450..483
FT /note="TPR 2"
FT REPEAT 518..551
FT /note="TPR 3"
FT REPEAT 553..585
FT /note="TPR 4"
FT REPEAT 587..619
FT /note="TPR 5"
FT REPEAT 621..653
FT /note="TPR 6"
FT REPEAT 655..687
FT /note="TPR 7"
FT REPEAT 688..721
FT /note="TPR 8"
FT REGION 180..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 83068 MW; 1CB1719C75469861 CRC64;
MEAMLVDCVN NSLRHFVYKN AIFMCERLCA EFPSEVNLQL LATSYLQNNQ AYSAYHLLKG
TQMAQSRYLF ALSCFQMDLL NEAESALCPV NEPGAEIPNG AAGHYLLGLI YKYTDRRKNA
AQQFKQSLTI DPLLWAAYEE LCILGAAEEA TAVFGETAAL SIQKQYMQQL STSLGLNTYN
EERNSTSTKN TSSEDYSPRQ SKHTQSHGLK DISGNFHSHG VNGGVSNMSF YNTPSPVAAQ
LSGIAPPPLF RNFQPAVANP NSLITDSSPK STVNSTLQAP RRKFVDEGKL RKISGRLFSD
SGPRRSSRLS ADSGANINSS VATVSGNVNN ASKYLGGSKL SSLALRSVTL RKGHSWANEN
MDEGVRGEPF DDSRPNTAST TGSMASNDQE DETMSIGGIA MSSQTITIGV SEILNLLRTL
GEGCRLSYMY RCQEALDTYM KLPHKHYNTG WVLSQVGKAY FELIDYLEAE KAFRLARLAS
PYCLEGMDIY STVLYHLKED MKLSYLAQEL ISTDRLAPQS WCAMGNCYSL QKDHETALKN
FLRAVQLNPR FAYAHTLCGH EYTTLEDFEN GMKSYQNALR VDTRHYNAWY GLGMIYLRQE
KLEFSEHHFR MAFLINPSSS VIMSYLGTSL HALKRSEEAL EIMEQAIVAD RKNPLPMYQK
ANILVCLERL DEALEVLEEL KEYAPSESSV YALMGRIYKR RNMHDKAMLH FGLALDMKPP
ATDVAAIKAA MEKLHVPDEI DESP
