PUX1_ARATH
ID PUX1_ARATH Reviewed; 251 AA.
AC Q9LK22;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Plant UBX domain-containing protein 1 {ECO:0000303|Ref.7};
DE Short=PUX1 {ECO:0000303|Ref.7};
DE AltName: Full=CDC48-interacting UBX-domain protein 1 {ECO:0000312|EMBL:AAS78923.1};
GN Name=PUX1 {ECO:0000312|EMBL:AAS78923.1};
GN OrderedLocusNames=At3g27310 {ECO:0000312|Araport:AT3G27310};
GN ORFNames=K17E12.13 {ECO:0000312|EMBL:BAB02126.1};
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 [MRNA], INTERACTION WITH CDC48A, DISRUPTION PHENOTYPE,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=15498773; DOI=10.1074/jbc.m405498200;
RA Rancour D.M., Park S., Knight S.D., Bednarek S.Y.;
RT "Plant UBX domain-containing protein 1, PUX1, regulates the oligomeric
RT structure and activity of arabidopsis CDC48.";
RL J. Biol. Chem. 279:54264-54274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
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 [7]
RP GENE FAMILY, INTERACTION WITH CDC48A, AND FUNCTION.
RA Posthuma R., Rancour D., Park S., Bates B., Bednarek S.;
RT "The plant UBX-domain containing (PUX) protein family regulates the
RT function of Arabidopsis CDC48, a conserved essential AAA-ATPase.";
RL (In) Proceedings of the 16th international conference on Arabidopsis
RL research, abstract#116, Madison (2005).
RN [8]
RP INTERACTION WITH CDC48A, AND FUNCTION.
RX PubMed=17190830; DOI=10.1074/jbc.m609042200;
RA Park S., Rancour D.M., Bednarek S.Y.;
RT "Protein domain-domain interactions and requirements for the negative
RT regulation of Arabidopsis CDC48/p97 by the plant ubiquitin regulatory X
RT (UBX) domain-containing protein, PUX1.";
RL J. Biol. Chem. 282:5217-5224(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND IDENTIFICATION
RP BY MASS 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).
CC -!- FUNCTION: Regulates CDC48A by inhibiting its ATPase activity and by
CC promoting the disassembly of the active hexamer.
CC {ECO:0000269|PubMed:15498773, ECO:0000269|PubMed:17190830,
CC ECO:0000269|Ref.7}.
CC -!- SUBUNIT: Interacts with CDC48A (non-hexameric) via its UBX-containing
CC C-terminal domain. {ECO:0000269|PubMed:15498773,
CC ECO:0000269|PubMed:17190830, ECO:0000269|Ref.7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15498773}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LK22-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LK22-2; Sequence=VSP_059337;
CC -!- DISRUPTION PHENOTYPE: Accelerated growth of various plant organs
CC including roots and inflorescence shoots.
CC {ECO:0000269|PubMed:15498773}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-
CC 22 of isoform 1. {ECO:0000305}.
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DR EMBL; AY572781; AAS78923.1; -; mRNA.
DR EMBL; AP000381; BAB02126.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77293.1; -; Genomic_DNA.
DR EMBL; AK175284; BAD43047.1; -; mRNA.
DR EMBL; BT024476; ABD19657.1; -; mRNA.
DR EMBL; AY085053; AAM61610.1; -; mRNA.
DR RefSeq; NP_566815.1; NM_113645.3. [Q9LK22-1]
DR PDB; 6HD0; X-ray; 3.73 A; D/E/F/G/I/K=1-251.
DR PDBsum; 6HD0; -.
DR AlphaFoldDB; Q9LK22; -.
DR SMR; Q9LK22; -.
DR STRING; 3702.AT3G27310.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR iPTMnet; Q9LK22; -.
DR MetOSite; Q9LK22; -.
DR PaxDb; Q9LK22; -.
DR PRIDE; Q9LK22; -.
DR ProteomicsDB; 224818; -. [Q9LK22-1]
DR EnsemblPlants; AT3G27310.1; AT3G27310.1; AT3G27310. [Q9LK22-1]
DR GeneID; 822350; -.
DR Gramene; AT3G27310.1; AT3G27310.1; AT3G27310. [Q9LK22-1]
DR KEGG; ath:AT3G27310; -.
DR Araport; AT3G27310; -.
DR TAIR; locus:2086493; AT3G27310.
DR eggNOG; KOG2699; Eukaryota.
DR HOGENOM; CLU_062119_0_0_1; -.
DR InParanoid; Q9LK22; -.
DR OMA; AQPDIPF; -.
DR OrthoDB; 1295079at2759; -.
DR PhylomeDB; Q9LK22; -.
DR PRO; PR:Q9LK22; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK22; baseline and differential.
DR Genevisible; Q9LK22; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0035265; P:organ growth; IMP:TAIR.
DR GO; GO:0032984; P:protein-containing complex disassembly; IDA:UniProtKB.
DR InterPro; IPR044232; PUX1.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR PANTHER; PTHR47557; PTHR47557; 1.
DR Pfam; PF00789; UBX; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Cytoplasm;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..251
FT /note="Plant UBX domain-containing protein 1"
FT /id="PRO_0000432600"
FT DOMAIN 104..180
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 212..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_059337"
FT MOD_RES Q9LK22-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 251 AA; 28502 MW; 32FE78BD14054578 CRC64;
MFVDDPSLHT LKRRRLEITD SMEASSSAQA KIADMREKLG REVRVFETSS ISQRPSQVSS
ADDESDDFYE FTPADFYRLL ATKKEDKSLK TRKIREAEEA ARRSKLTKAV IRVRFPDNHT
LEATFHPSEK IQGLIDLVKR VVAHPDVPFY LYTTPPKKQI KDFSQDFYSA GFVPGAIVYF
SNDQPKDDGG SSTPYLNEEI LSLKDLEAMT KAVEPVESSS EPATVDSSAV PVEHERKSTE
KKTTKPKWFK M
