PWP2_ARATH
ID PWP2_ARATH Reviewed; 900 AA.
AC Q8VYZ5; F4HZM8; Q9XI24;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Periodic tryptophan protein 2 {ECO:0000303|PubMed:19929880};
DE Short=AtPWP2 {ECO:0000303|PubMed:19929880, ECO:0000303|PubMed:23382868};
GN Name=PWP2 {ECO:0000303|PubMed:19929880};
GN OrderedLocusNames=At1g15440 {ECO:0000312|Araport:AT1G15440};
GN ORFNames=F9L1.40 {ECO:0000312|EMBL:AAD39674.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 1).
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 GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP INTERACTION WITH TBP1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=19929880; DOI=10.1111/j.1365-313x.2009.04081.x;
RA Matsui K., Ohme-Takagi M.;
RT "Detection of protein-protein interactions in plants using the
RT transrepressive activity of the EAR motif repression domain.";
RL Plant J. 61:570-578(2010).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY SUCROSE.
RC STRAIN=cv. Columbia;
RX PubMed=23185391; DOI=10.1371/journal.pone.0049641;
RA Bates G.W., Rosenthal D.M., Sun J., Chattopadhyay M., Peffer E., Yang J.,
RA Ort D.R., Jones A.M.;
RT "A comparative study of the Arabidopsis thaliana guard-cell transcriptome
RT and its modulation by sucrose.";
RL PLoS ONE 7:E49641-E49641(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=23382868; DOI=10.1371/journal.pone.0054084;
RA Missbach S., Weis B.L., Martin R., Simm S., Bohnsack M.T., Schleiff E.;
RT "40S ribosome biogenesis co-factors are essential for gametophyte and
RT embryo development.";
RL PLoS ONE 8:E54084-E54084(2013).
CC -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC Plays a role early in ribosome biogenesis, especially in the maturation
CC of 5.8S rRNA (PubMed:23382868). Required for guard cell functions
CC (PubMed:23185391). {ECO:0000269|PubMed:23185391,
CC ECO:0000269|PubMed:23382868}.
CC -!- SUBUNIT: Component of the ribosomal small subunit (SSU) processome (By
CC similarity). Interacts with TBP1 in the nucleus (PubMed:19929880).
CC {ECO:0000250|UniProtKB:P25635, ECO:0000269|PubMed:19929880}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:23382868}.
CC Nucleus {ECO:0000269|PubMed:19929880}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VYZ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VYZ5-2; Sequence=VSP_058979;
CC -!- TISSUE SPECIFICITY: Expressed constitutively and ubiquitously; observed
CC in seeds, seedlings, roots, leaves, stems, flowers and siliques.
CC {ECO:0000269|PubMed:23382868}.
CC -!- INDUCTION: Induced by sucrose in guard cells.
CC {ECO:0000269|PubMed:23185391}.
CC -!- DISRUPTION PHENOTYPE: Impaired maturation of 5.8S rRNA, especially the
CC processing at the 5' end. Reduced siliques size due to defects in
CC embryo and female gametophyte development (PubMed:23382868). Defects in
CC guard cell function leading to reduced stomatal conductance and
CC impaired water-use efficiency (PubMed:23185391).
CC {ECO:0000269|PubMed:23185391, ECO:0000269|PubMed:23382868}.
CC -!- SIMILARITY: Belongs to the WD repeat PWP2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39674.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007591; AAD39674.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29324.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29325.1; -; Genomic_DNA.
DR EMBL; AY065425; AAL38866.1; -; mRNA.
DR EMBL; AY133789; AAM91723.1; -; mRNA.
DR RefSeq; NP_172998.1; NM_101414.4. [Q8VYZ5-1]
DR RefSeq; NP_973836.1; NM_202107.1. [Q8VYZ5-2]
DR AlphaFoldDB; Q8VYZ5; -.
DR SMR; Q8VYZ5; -.
DR STRING; 3702.AT1G15440.1; -.
DR iPTMnet; Q8VYZ5; -.
DR PaxDb; Q8VYZ5; -.
DR PRIDE; Q8VYZ5; -.
DR ProteomicsDB; 226131; -. [Q8VYZ5-1]
DR EnsemblPlants; AT1G15440.1; AT1G15440.1; AT1G15440. [Q8VYZ5-1]
DR EnsemblPlants; AT1G15440.2; AT1G15440.2; AT1G15440. [Q8VYZ5-2]
DR GeneID; 838115; -.
DR Gramene; AT1G15440.1; AT1G15440.1; AT1G15440. [Q8VYZ5-1]
DR Gramene; AT1G15440.2; AT1G15440.2; AT1G15440. [Q8VYZ5-2]
DR KEGG; ath:AT1G15440; -.
DR Araport; AT1G15440; -.
DR TAIR; locus:2037798; AT1G15440.
DR eggNOG; KOG0291; Eukaryota.
DR InParanoid; Q8VYZ5; -.
DR OMA; QSEQYIM; -.
DR OrthoDB; 290630at2759; -.
DR PhylomeDB; Q8VYZ5; -.
DR PRO; PR:Q8VYZ5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VYZ5; baseline and differential.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0034388; C:Pwp2p-containing subcomplex of 90S preribosome; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IMP:TAIR.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR027145; PWP2.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR007148; SSU_processome_Utp12.
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; PTHR19858; PTHR19858; 1.
DR Pfam; PF04003; Utp12; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 10.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosome biogenesis;
KW rRNA processing; WD repeat.
FT CHAIN 1..900
FT /note="Periodic tryptophan protein 2"
FT /id="PRO_0000440648"
FT REPEAT 10..47
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 50..89
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 91..129
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 139..178
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 185..229
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 302..341
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 344..384
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 387..426
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REPEAT 429..468
FT /note="WD 9"
FT /evidence="ECO:0000255"
FT REPEAT 472..512
FT /note="WD 10"
FT /evidence="ECO:0000255"
FT REPEAT 515..554
FT /note="WD 11"
FT /evidence="ECO:0000255"
FT REPEAT 557..596
FT /note="WD 12"
FT /evidence="ECO:0000255"
FT REPEAT 619..658
FT /note="WD 13"
FT /evidence="ECO:0000255"
FT REPEAT 720..759
FT /note="WD 14"
FT /evidence="ECO:0000255"
FT REGION 228..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT VAR_SEQ 166..205
FT /note="Missing (in isoform 2)"
FT /id="VSP_058979"
SQ SEQUENCE 900 AA; 100471 MW; EEC29D5F106F5624 CRC64;
MEFRFENLLG APYRGGNAVI TKNTQLISPV GNRVSVTDLS KNHSVTLPLE TSTNICRLAS
SPDGTFLLAV DEQNRCLFIN LPRRVVLHRI TFKDKVGALK FSPNGKFIAV GIGKLVEIWR
SPGFRRAVLP FERVRTFANS DDKVVSLEWS LDSDYLLVGS RDLAARLFCV RKLKGVLNKP
FLFLGHRDSV VGCFFGVDKM TNKVNRAFTI ARDGYIFSWG YTEKDVKMDE SEDGHSEPPS
PVTPDRADEV MVENGGGVGT ELKKRKEYDG KGLESDEEGD DDDEEYMHRG KWVLLRKDGC
NQASAKVTAC DYHQGLDMVV VGFSNGVFGL YQMPDFICIH LLSISRQKLT TAVFNERGNW
LTFGCAKLGQ LLVWDWRTET YILKQQGHYF DVNCVTYSPD SQLLATGADD NKVKVWNVMS
GTCFITFTEH TNAVTALHFM ADNHSLLSAS LDGTVRAWDF KRYKNYKTYT TPTPRQFVSL
TADPSGDVVC AGTLDSFEIF VWSKKTGQIK DILSGHEAPV HGLMFSPLTQ LLASSSWDYT
VRLWDVFASK GTVETFRHNH DVLTVAFRPD GKQLASSTLD GQINFWDTIE GVLMYTIEGR
RDIAGGRVMT DRRSAANSSS GKCFTTLCYS ADGGYILAAG TSRYICMYDI ADQVLLRRFQ
ISHNLSLDGV LDFLHSKKMT EAGPIDLIDD DNSDEEGGID KQSRGNLGYD LPGSRPNRGR
PIIRTKSLSI APTGRSFAAA TTEGVLIFSI DDTFIFDPTD LDIDVTPEAV EAAIEEDEVS
RALALSMRLN EDSLIKKCIF AVAPADIKAV AISVRQKYLE RLMEALVDLL ENCPHLEFIL
HWCQEICKAH GSSIQRNYRT LLPALRSLQK AITRAHQDLA DMCSSNEYTL RYLCSVPNNH
