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WDR12_ARATH
ID   WDR12_ARATH             Reviewed;         433 AA.
AC   Q9LF27;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Ribosome biogenesis protein WDR12 homolog {ECO:0000255|HAMAP-Rule:MF_03029};
DE   AltName: Full=Pescadillo-interacting protein 2 {ECO:0000305};
DE            Short=AtPEIP2 {ECO:0000303|PubMed:25443833};
GN   Name=WDR12 {ECO:0000305}; Synonyms=PEIP2 {ECO:0000303|PubMed:25443833};
GN   OrderedLocusNames=At5g15550 {ECO:0000312|Araport:AT5G15550};
GN   ORFNames=T20K14_160 {ECO:0000312|EMBL:CAC01754.1};
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
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   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [5]
RP   INTERACTION WITH PES AND BOP1, 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   [6]
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).
CC   -!- FUNCTION: Required for maturation of ribosomal RNAs and formation of
CC       the large ribosomal subunit. {ECO:0000255|HAMAP-Rule:MF_03029}.
CC   -!- SUBUNIT: Interacts with PES (PubMed:23909681, PubMed:25443833).
CC       Interacts with BOP1 (PubMed:23909681). {ECO:0000269|PubMed:23909681,
CC       ECO:0000269|PubMed:25443833}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC       Rule:MF_03029, ECO:0000269|PubMed:23909681,
CC       ECO:0000269|PubMed:25443833}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC       Rule:MF_03029}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC       Name=1;
CC         IsoId=Q9LF27-1; Sequence=Displayed;
CC   -!- MISCELLANEOUS: [Isoform 1]: A number of isoforms are produced.
CC       According to EST sequences. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the WD repeat WDR12/YTM1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03029}.
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DR   EMBL; AL391143; CAC01754.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92176.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM71061.1; -; Genomic_DNA.
DR   EMBL; AY064011; AAL36367.1; -; mRNA.
DR   EMBL; AY091257; AAM14196.1; -; mRNA.
DR   PIR; T51533; T51533.
DR   RefSeq; NP_001332618.1; NM_001343408.1. [Q9LF27-1]
DR   RefSeq; NP_197059.1; NM_121559.3. [Q9LF27-1]
DR   AlphaFoldDB; Q9LF27; -.
DR   SMR; Q9LF27; -.
DR   STRING; 3702.AT5G15550.1; -.
DR   iPTMnet; Q9LF27; -.
DR   PaxDb; Q9LF27; -.
DR   PRIDE; Q9LF27; -.
DR   ProteomicsDB; 242783; -. [Q9LF27-1]
DR   EnsemblPlants; AT5G15550.1; AT5G15550.1; AT5G15550. [Q9LF27-1]
DR   EnsemblPlants; AT5G15550.3; AT5G15550.3; AT5G15550. [Q9LF27-1]
DR   GeneID; 831408; -.
DR   Gramene; AT5G15550.1; AT5G15550.1; AT5G15550. [Q9LF27-1]
DR   Gramene; AT5G15550.3; AT5G15550.3; AT5G15550. [Q9LF27-1]
DR   KEGG; ath:AT5G15550; -.
DR   Araport; AT5G15550; -.
DR   TAIR; locus:2180952; AT5G15550.
DR   eggNOG; KOG0313; Eukaryota.
DR   HOGENOM; CLU_000288_57_0_1; -.
DR   InParanoid; Q9LF27; -.
DR   OMA; VDCTRTK; -.
DR   PhylomeDB; Q9LF27; -.
DR   PRO; PR:Q9LF27; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LF27; baseline and differential.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR   GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IEA:UniProtKB-UniRule.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
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); IEA:UniProtKB-UniRule.
DR   Gene3D; 2.130.10.10; -; 1.
DR   HAMAP; MF_03029; WDR12; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR012972; NLE.
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   InterPro; IPR028599; WDR12/Ytm1.
DR   Pfam; PF08154; NLE; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Nucleus; Reference proteome; Repeat;
KW   Ribosome biogenesis; rRNA processing; WD repeat.
FT   CHAIN           1..433
FT                   /note="Ribosome biogenesis protein WDR12 homolog"
FT                   /id="PRO_0000437496"
FT   REPEAT          108..146
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT   REPEAT          148..191
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT   REPEAT          203..242
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT   REPEAT          270..308
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT   REPEAT          310..350
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT   REPEAT          356..396
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT   REPEAT          399..433
FT                   /note="WD 7"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT   REGION          12..96
FT                   /note="Ubiquitin-like (UBL) domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT   REGION          238..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   433 AA;  47338 MW;  8DC768ACCEB4D3B8 CRC64;
     MDIDGEDVSR RLHVKFVTKL DSPFKVPVNS VAIPSNVTRL GLSSIVNSII ESENPEWKTE
     PFDFLIDGEL IRMSLEEFLL AKGISAERTL EIEYIRAVTP RKEEEPSLHD DWVSAVNGSS
     PRFILTGCYD GLGRVWSSAG SCSHILEGHS GAISSVALVN SNDAETVTVA TASKDRTLRL
     FKFDPAESVD STTKVRAYKI LRGHKASVQS VSAQKSGNMV CSSSWDCTIN LWNTNESTSE
     GESVSVKKRK GNNQAEESQS EGEAVTSLVG HTQCVSSVVW PEHDVIYSSS WDHSVRRWDV
     ETGKDSLNLF CGKALNTVDV GGESSALIAA GGSDPILRVW DPRKPGTSAP VFQFSSHSSW
     ISACKWHKSS WFHLLSASYD GKIMLWDLRT AWPLSVIDTH NDKVLSADWW KGESVVSGGA
     DSNLRISSGI AIS
 
 
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