PQT3L_ARATH
ID PQT3L_ARATH Reviewed; 892 AA.
AC B9DFV2; A8MRK5; F4JX50; Q8L7L2; Q9FHH9;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=E3 ubiquitin ligase PQT3-like;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:F4JP52};
GN OrderedLocusNames=At5g47430 {ECO:0000312|Araport:AT5G47430};
GN ORFNames=MQL5.29 {ECO:0000312|EMBL:BAB11612.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-462 (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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-404, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-866, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:F4JP52};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:F4JP52,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=B9DFV2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B9DFV2-2; Sequence=VSP_058684;
CC Name=3;
CC IsoId=B9DFV2-3; Sequence=VSP_058685;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11612.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB018117; BAB11612.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB025628; BAB11612.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED95508.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95509.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95510.1; -; Genomic_DNA.
DR EMBL; AK316913; BAH19619.1; -; mRNA.
DR EMBL; AY128390; AAM91593.1; -; mRNA.
DR RefSeq; NP_001078725.1; NM_001085256.1. [B9DFV2-2]
DR RefSeq; NP_001190484.1; NM_001203555.1. [B9DFV2-3]
DR RefSeq; NP_199554.2; NM_124114.4. [B9DFV2-1]
DR AlphaFoldDB; B9DFV2; -.
DR SMR; B9DFV2; -.
DR STRING; 3702.AT5G47430.1; -.
DR iPTMnet; B9DFV2; -.
DR PaxDb; B9DFV2; -.
DR PRIDE; B9DFV2; -.
DR EnsemblPlants; AT5G47430.1; AT5G47430.1; AT5G47430. [B9DFV2-1]
DR EnsemblPlants; AT5G47430.2; AT5G47430.2; AT5G47430. [B9DFV2-2]
DR EnsemblPlants; AT5G47430.3; AT5G47430.3; AT5G47430. [B9DFV2-3]
DR GeneID; 834790; -.
DR Gramene; AT5G47430.1; AT5G47430.1; AT5G47430. [B9DFV2-1]
DR Gramene; AT5G47430.2; AT5G47430.2; AT5G47430. [B9DFV2-2]
DR Gramene; AT5G47430.3; AT5G47430.3; AT5G47430. [B9DFV2-3]
DR KEGG; ath:AT5G47430; -.
DR Araport; AT5G47430; -.
DR TAIR; locus:2171569; AT5G47430.
DR eggNOG; KOG0314; Eukaryota.
DR HOGENOM; CLU_015100_2_0_1; -.
DR InParanoid; B9DFV2; -.
DR OMA; YQDFGAE; -.
DR PhylomeDB; B9DFV2; -.
DR PRO; PR:B9DFV2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B9DFV2; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR014891; DWNN_domain.
DR InterPro; IPR033489; RBBP6.
DR InterPro; IPR025829; Zn_knuckle_CX2CX3GHX4C.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15439; PTHR15439; 2.
DR Pfam; PF08783; DWNN; 1.
DR Pfam; PF13696; zf-CCHC_2; 1.
DR SMART; SM01180; DWNN; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS51282; DWNN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..892
FT /note="E3 ubiquitin ligase PQT3-like"
FT /id="PRO_0000438584"
FT DOMAIN 3..76
FT /note="DWNN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00612"
FT ZN_FING 210..224
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 295..333
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 375..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 693..700
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 388..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform 2)"
FT /id="VSP_058684"
FT VAR_SEQ 196..198
FT /note="Missing (in isoform 3)"
FT /id="VSP_058685"
SQ SEQUENCE 892 AA; 99083 MW; 5BB66BD2C7A62C10 CRC64;
MAIYYKFKSA RDYDTIAMDG PFISVGILKD KIFETKHLGT GKDLDIVVSN AQTNEEYLDE
AMLIPKNTSV LIRRVPGRPR ITVITTQEPR IQNKVEDVQA ETTNFPVADP SAAEFPEDEY
DEFGTDLYSI PDTQDAQHII PRPHLATADD KVDEESKIQA LIDTPALDWQ QRQGQDTFGA
GRGYGRGMPG RMNGRGFGME RKTPPPGYVC HRCNIPGHFI QHCPTNGDPN YDVKRVKPPT
GIPKSMLMAT PDGSYSLPSG AVAVLKPNED AFEKEMEGLP STTRSVGELP PELKCPLCKE
VMKDAALTSK CCYKSFCDKC IRDHIISKSM CVCGRSDVLA DDLLPNKTLR DTINRILEAG
NDSTENVGSV GHIPDLESAR CPPPKALSPT TSVASKGEKK PVLSNNNDAS TLKAPMEVAE
ITSAPRASAE VNVEKPVDAC ESTQGSVIVK EATVSKLNTQ APKEEMQQQV AAGEPGKKKK
KKPRVPGNDM QWNPVPDLAG PDYMMQMGPG PQYFNGMQPG FNGVQPGFNG VQPGFNGFHP
GFNGFGGPFP GAMPPFMGYG LNPMDMGFGG GMNMMHPDPF MAQGFGFPNI PPPHRDLAEM
GNRMNLQRAM MGRDEAEARN AEMLRKRENE RRPEGGKMFR DGENSRMMMN NGTSASASSI
NPNKSRQAPP PPIHDYDRRR RPEKRLSPEH PPTRKNISPS RDSKRKSERY PDERDRQRDR
ERSRHQDVDR EHDRTRDRRD EDRSRDHRHH RGETERSQHH HRKRSEPPSS EPPVPATKAE
IENNLKSSVF ARISFPEEET SSGKRRKVPS SSSTSVTDPS ASASAAAAVG TSVHRHSSRK
EIEVADYESS DEDRHFKRKP SRYARSPPVV VSDVSEDKLR YSKRGKGERS RA
