PRT1_ARATH
ID PRT1_ARATH Reviewed; 410 AA.
AC Q8LBL5; O82767;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=E3 ubiquitin-protein ligase PRT1;
DE EC=2.3.2.27;
DE AltName: Full=Proteolysis 1 protein;
DE AltName: Full=RING-type E3 ubiquitin transferase PRT1 {ECO:0000305};
GN Name=PRT1; OrderedLocusNames=At3g24800; ORFNames=K7P8.9;
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 [GENOMIC DNA / MRNA], AND FUNCTION.
RX PubMed=9653113; DOI=10.1073/pnas.95.14.7904;
RA Potuschak T., Stary S., Schloegelhofer P., Becker F., Nejinskaia V.,
RA Bachmair A.;
RT "PRT1 of Arabidopsis thaliana encodes a component of the plant N-end rule
RT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7904-7908(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND MUTANTS PRT1.
RX PubMed=11607348; DOI=10.1073/pnas.90.2.418;
RA Bachmair A., Becker F., Schell J.;
RT "Use of a reporter transgene to generate Arabidopsis mutants in ubiquitin-
RT dependent protein degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:418-421(1993).
RN [7]
RP FUNCTION.
RX PubMed=14551326; DOI=10.1104/pp.103.029272;
RA Stary S., Yin X.-J., Potuschak T., Schloegelhofer P., Nizhynska V.,
RA Bachmair A.;
RT "PRT1 of Arabidopsis is a ubiquitin protein ligase of the plant N-end rule
RT pathway with specificity for aromatic amino-terminal residues.";
RL Plant Physiol. 133:1360-1366(2003).
RN [8]
RP FUNCTION.
RX PubMed=17572409; DOI=10.1016/j.febslet.2007.06.005;
RA Garzon M., Eifler K., Faust A., Scheel H., Hofmann K., Koncz C.,
RA Yephremov A., Bachmair A.;
RT "PRT6/At5g02310 encodes an Arabidopsis ubiquitin ligase of the N-end rule
RT pathway with arginine specificity and is not the CER3 locus.";
RL FEBS Lett. 581:3189-3196(2007).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins. Functions in the
CC N-end rule pathway of protein degradation, where it specifically
CC recognizes and ubiquitinates proteins with a N-terminal bulky aromatic
CC amino acid (Phe). Does not act on aliphatic hydrophobic and basic N-
CC terminal residues (Arg or Leu) containing proteins.
CC {ECO:0000269|PubMed:11607348, ECO:0000269|PubMed:14551326,
CC ECO:0000269|PubMed:17572409, ECO:0000269|PubMed:9653113}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM64697.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ224306; CAA11891.1; -; Genomic_DNA.
DR EMBL; AJ224307; CAA11892.1; -; mRNA.
DR EMBL; AB028609; BAB02890.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76948.1; -; Genomic_DNA.
DR EMBL; AY080799; AAL87280.1; -; mRNA.
DR EMBL; AY114077; AAM45125.1; -; mRNA.
DR EMBL; AY087139; AAM64697.1; ALT_INIT; mRNA.
DR PIR; T52193; T52193.
DR RefSeq; NP_189124.1; NM_113392.3.
DR AlphaFoldDB; Q8LBL5; -.
DR SMR; Q8LBL5; -.
DR BioGRID; 7409; 1.
DR STRING; 3702.AT3G24800.1; -.
DR iPTMnet; Q8LBL5; -.
DR PaxDb; Q8LBL5; -.
DR PRIDE; Q8LBL5; -.
DR ProteomicsDB; 226479; -.
DR EnsemblPlants; AT3G24800.1; AT3G24800.1; AT3G24800.
DR GeneID; 822078; -.
DR Gramene; AT3G24800.1; AT3G24800.1; AT3G24800.
DR KEGG; ath:AT3G24800; -.
DR Araport; AT3G24800; -.
DR TAIR; locus:2087278; AT3G24800.
DR eggNOG; KOG4159; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR HOGENOM; CLU_039458_1_0_1; -.
DR InParanoid; Q8LBL5; -.
DR OMA; HSADHEV; -.
DR OrthoDB; 990568at2759; -.
DR PhylomeDB; Q8LBL5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8LBL5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LBL5; baseline and differential.
DR Genevisible; Q8LBL5; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00184; RING; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..410
FT /note="E3 ubiquitin-protein ligase PRT1"
FT /id="PRO_0000056003"
FT ZN_FING 26..66
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 192..232
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 306..370
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 385..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT CONFLICT 394
FT /note="E -> D (in Ref. 5; AAM64697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 45937 MW; 17463F96CB6DBF54 CRC64;
MAETMKDITM KNDESQEEEI PDQFLCCVCL ELLYKPIVLS CGHLSCFWCV HKSMNGFRES
HCPICRDPYV HFPSVCQKLY FLLKKMYPLA HKKREEQVLK EEQERECFSP QIDLVLDLSV
CSGDSLNVSD KQKVEECSNA ANLLSSSSSR GDIPCIPKNQ EPTDAKALNV HENELLKDNK
VSKQISKDDL LCSACKELLV RPVVLNCGHV YCEGCVVDMA EESEKIKCQE CNVCDPRGFP
KVCLILEQLL EENFPEEYNS RSSKVQKTLA HNSKGNIQSY LKEGPSLSND NNNDDPWLAN
PGSNVHFGAG CDSCGVYPII GDRYRCKDCK EEIGYDLCKD CYETPSKVPG RFNQQHTPDH
RLELARSPQV LINFNSIGIL LGPVISNEGM DTDEGEEGPP GSSNESSSTE
