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BOP1_ARATH
ID   BOP1_ARATH              Reviewed;         753 AA.
AC   F4IH25; Q9SIY9;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Ribosome biogenesis protein BOP1 homolog {ECO:0000255|HAMAP-Rule:MF_03027};
DE   AltName: Full=Pescadillo-interacting protein 1 {ECO:0000305};
DE            Short=AtPEIP1 {ECO:0000303|PubMed:25443833};
DE   AltName: Full=Protein BLOCK OF CELL PROLIFERATION 1 {ECO:0000305};
GN   Name=BOP1 {ECO:0000305}; Synonyms=PEIP1 {ECO:0000303|PubMed:25443833};
GN   OrderedLocusNames=At2g40360 {ECO:0000312|Araport:AT2G40360};
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=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   [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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
RN   [4]
RP   INTERACTION WITH PES AND WDR12, AND SUBCELLULAR LOCATION.
RX   PubMed=23909681; DOI=10.1111/tpj.12302;
RA   Cho H.K., Ahn C.S., Lee H.S., Kim J.K., Pai H.S.;
RT   "Pescadillo plays an essential role in plant cell growth and survival by
RT   modulating ribosome biogenesis.";
RL   Plant J. 76:393-405(2013).
RN   [5]
RP   INTERACTION WITH PES, AND SUBCELLULAR LOCATION.
RX   PubMed=25443833; DOI=10.1016/j.plantsci.2014.08.012;
RA   Zografidis A., Kapolas G., Podia V., Beri D., Papadopoulou K., Milioni D.,
RA   Haralampidis K.;
RT   "Transcriptional regulation and functional involvement of the Arabidopsis
RT   pescadillo ortholog AtPES in root development.";
RL   Plant Sci. 229:53-65(2014).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26940494; DOI=10.1016/j.plantsci.2016.01.002;
RA   Carvalho S.D., Chatterjee M., Coleman L., Clancy M.A., Folta K.M.;
RT   "Analysis of Block of cell proliferation 1 (BOP1) activity in strawberry
RT   and Arabidopsis.";
RL   Plant Sci. 245:84-93(2016).
CC   -!- FUNCTION: Required for maturation of ribosomal RNAs and formation of
CC       the large ribosomal subunit (By similarity). Plays an essential role in
CC       cell growth and survival through its regulation of ribosome biogenesis
CC       and mitotic progression (PubMed:26940494). {ECO:0000255|HAMAP-
CC       Rule:MF_03027, ECO:0000269|PubMed:26940494}.
CC   -!- SUBUNIT: Interacts with PES (PubMed:23909681, PubMed:25443833).
CC       Interacts with WDR12 (PubMed:23909681). {ECO:0000269|PubMed:23909681,
CC       ECO:0000269|PubMed:25443833}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC       Rule:MF_03027, ECO:0000269|PubMed:23909681,
CC       ECO:0000269|PubMed:25443833}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC       Rule:MF_03027}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC       {ECO:0000269|PubMed:26940494}.
CC   -!- SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03027}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD25679.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC007020; AAD25679.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC09818.1; -; Genomic_DNA.
DR   PIR; E84828; E84828.
DR   RefSeq; NP_181567.3; NM_129596.4.
DR   AlphaFoldDB; F4IH25; -.
DR   SMR; F4IH25; -.
DR   STRING; 3702.AT2G40360.1; -.
DR   PaxDb; F4IH25; -.
DR   PRIDE; F4IH25; -.
DR   EnsemblPlants; AT2G40360.1; AT2G40360.1; AT2G40360.
DR   GeneID; 818629; -.
DR   Gramene; AT2G40360.1; AT2G40360.1; AT2G40360.
DR   KEGG; ath:AT2G40360; -.
DR   Araport; AT2G40360; -.
DR   TAIR; locus:2063099; AT2G40360.
DR   eggNOG; KOG0650; Eukaryota.
DR   HOGENOM; CLU_011390_2_0_1; -.
DR   InParanoid; F4IH25; -.
DR   OMA; MRPAKGE; -.
DR   OrthoDB; 759498at2759; -.
DR   PRO; PR:F4IH25; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; F4IH25; baseline and differential.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070545; C:PeBoW complex; IBA:GO_Central.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central.
DR   GO; GO:0007276; P:gamete generation; IMP:TAIR.
DR   GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:UniProtKB-UniRule.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0051302; P:regulation of cell division; IMP:TAIR.
DR   Gene3D; 2.130.10.10; -; 1.
DR   HAMAP; MF_03027; BOP1; 1.
DR   InterPro; IPR028598; BOP1/Erb1.
DR   InterPro; IPR012953; BOP1_N_dom.
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; PTHR17605; PTHR17605; 1.
DR   Pfam; PF08145; BOP1NT; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM01035; BOP1NT; 1.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Repeat; Ribosome biogenesis; rRNA processing;
KW   WD repeat.
FT   CHAIN           1..753
FT                   /note="Ribosome biogenesis protein BOP1 homolog"
FT                   /id="PRO_0000437494"
FT   REPEAT          421..462
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03027"
FT   REPEAT          464..502
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03027"
FT   REPEAT          539..581
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03027"
FT   REPEAT          626..665
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03027"
FT   REPEAT          669..708
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03027"
FT   REPEAT          722..753
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03027"
FT   REGION          1..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..113
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   753 AA;  85383 MW;  0B11A93D744DCFEC CRC64;
     MTKRSKGANE DKLIETKSKN VSGKSQKQKK PVEAESLKEE DLLQASGTDS DYDGDSLPGS
     LNSDDFDSDF SDSEDDGTHE GTEDGDVEFS DDDDVLEHDG SIDNEDDDGS EHVGSDNNEE
     HGSDEDSERG EAVEESDSSE DEVPSRNTVG NVPLKWYEDE KHIGYDLTGK KITKKEKQDK
     LDSFLATIDD SKTWRKIYDE YNDEDVELTK EESKIVQRIL KGEAPHADFD PYAPYVEWFK
     HDDAIHPLSS APEPKRRFIP SKWEAKKVVK IVRAIRKGWI KFDKPEEEPN VYLLWGDDST
     SDQKSKHLTY IPPPKLKLPG HDESYNPSLE YIPTEEEKAS YELMFEEDRP KFIPTRFTSL
     RSIPAYENAL KESFERCLDL YLCPRVRKKR INIDPESLKP KLPSRKDLRP YPNSCYLEYK
     GHTGAVTSIS TDSSGEWIAS GSTDGSVRMW EVETGRCLKV WQFDEAIMCV AWNPLSRLPV
     LAVAMGRDLF FLNTELGTDE EQEITKERLH SGNIPEPDAS VAAIVTWLPD ELYGGIKIRH
     FKSISSIDWH RKGDYLSTVM ASGETRGVVL HQLSKQKTQR LPFKIRGLPV CTLFHPSLSY
     FFVATRKDVR VYNLLKPGEA TKKLETGLRE ISSMAIHPGG DNLIVGSKEG KMCWFDMDLS
     SKPYKTLKNH PKDITNVAVH RSYPLFASCS EDSTAYVFHG MVYNDLNQNP LIVPLEILRG
     HSSKGGVLDC KFHPRQPWLF TAGADSIIKL YCH
 
 
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