PUX2_ARATH
ID PUX2_ARATH Reviewed; 458 AA.
AC Q9ZU93; Q8LGE5;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Plant UBX domain-containing protein 2 {ECO:0000303|Ref.8};
DE Short=PUX2 {ECO:0000303|Ref.8};
DE AltName: Full=AtPUB3 {ECO:0000303|PubMed:11587532};
DE AltName: Full=CDC48-interacting UBX-domain protein 2 {ECO:0000312|EMBL:AAS78924.1};
GN Name=PUX2 {ECO:0000312|EMBL:AAS78924.1};
GN Synonyms=PUB3 {ECO:0000303|PubMed:11587532};
GN OrderedLocusNames=At2g01650 {ECO:0000312|Araport:AT2G01650};
GN ORFNames=T8O11.18 {ECO:0000312|EMBL:AAD12706.2};
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].
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
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 [7]
RP PUB DOMAIN.
RX PubMed=11587532; DOI=10.1006/bbrc.2001.5688;
RA Suzuki T., Park H., Till E.A., Lennarz W.J.;
RT "The PUB domain: a putative protein-protein interaction domain implicated
RT in the ubiquitin-proteasome pathway.";
RL Biochem. Biophys. Res. Commun. 287:1083-1087(2001).
RN [8]
RP GENE FAMILY, SUBCELLULAR LOCATION, INTERACTION WITH CDC48A, FUNCTION, AND
RP PUB DOMAIN.
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 [9]
RP DISRUPTION PHENOTYPE, INDUCTION, AND FUNCTION.
RX PubMed=19176722; DOI=10.1104/pp.108.132985;
RA Chandran D., Tai Y.C., Hather G., Dewdney J., Denoux C., Burgess D.G.,
RA Ausubel F.M., Speed T.P., Wildermuth M.C.;
RT "Temporal global expression data reveal known and novel salicylate-impacted
RT processes and regulators mediating powdery mildew growth and reproduction
RT on Arabidopsis.";
RL Plant Physiol. 149:1435-1451(2009).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=23301616; DOI=10.1094/mpmi-10-12-0254-r;
RA Chandran D., Rickert J., Cherk C., Dotson B.R., Wildermuth M.C.;
RT "Host cell ploidy underlying the fungal feeding site is a determinant of
RT powdery mildew growth and reproduction.";
RL Mol. Plant Microbe Interact. 26:537-545(2013).
CC -!- FUNCTION: Facilitates the interaction of SYP31 and CDC48A, thereby
CC regulating an CDC48A membrane-associated function (Ref.8). Appears to
CC act as a negative regulator mediating the powdery mildew-plant
CC interaction (PubMed:19176722, PubMed:23301616).
CC {ECO:0000269|PubMed:19176722, ECO:0000269|PubMed:23301616,
CC ECO:0000269|Ref.8}.
CC -!- SUBUNIT: Interacts with CDC48A in vitro and co-fractionates with
CC membrane-associated but not soluble CDC48A in vivo.
CC {ECO:0000269|Ref.8}.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein
CC {ECO:0000269|Ref.8}.
CC -!- INDUCTION: Induced in response to powdery mildew and by
CC benzothiadiazole (BTH) treatment. {ECO:0000269|PubMed:19176722}.
CC -!- DOMAIN: PUB (PUG) domain is required for the interaction with CDC48A
CC (Ref.8). PUB domain may serve as a protein-protein interaction domain
CC implicated in the ubiquitin-proteasome pathway (PubMed:11587532).
CC {ECO:0000269|PubMed:11587532, ECO:0000269|Ref.8}.
CC -!- DISRUPTION PHENOTYPE: Enhanced resistance to powdery mildew with a
CC reduced fungus reproduction. {ECO:0000269|PubMed:19176722,
CC ECO:0000269|PubMed:23301616}.
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DR EMBL; AY572782; AAS78924.1; -; mRNA.
DR EMBL; AC006069; AAD12706.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC05479.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61337.1; -; Genomic_DNA.
DR EMBL; AK118911; BAC43494.1; -; mRNA.
DR EMBL; BT005408; AAO63828.1; -; mRNA.
DR EMBL; AY084317; AAM60904.1; -; mRNA.
DR PIR; D84427; D84427.
DR RefSeq; NP_001318177.1; NM_001335070.1.
DR RefSeq; NP_565271.1; NM_126226.4.
DR AlphaFoldDB; Q9ZU93; -.
DR SMR; Q9ZU93; -.
DR IntAct; Q9ZU93; 2.
DR STRING; 3702.AT2G01650.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR iPTMnet; Q9ZU93; -.
DR PaxDb; Q9ZU93; -.
DR PRIDE; Q9ZU93; -.
DR ProteomicsDB; 225933; -.
DR EnsemblPlants; AT2G01650.1; AT2G01650.1; AT2G01650.
DR EnsemblPlants; AT2G01650.2; AT2G01650.2; AT2G01650.
DR GeneID; 814694; -.
DR Gramene; AT2G01650.1; AT2G01650.1; AT2G01650.
DR Gramene; AT2G01650.2; AT2G01650.2; AT2G01650.
DR KEGG; ath:AT2G01650; -.
DR Araport; AT2G01650; -.
DR TAIR; locus:2065363; AT2G01650.
DR eggNOG; KOG2699; Eukaryota.
DR HOGENOM; CLU_610277_0_0_1; -.
DR InParanoid; Q9ZU93; -.
DR OMA; RRIRMSN; -.
DR OrthoDB; 1288120at2759; -.
DR PhylomeDB; Q9ZU93; -.
DR PRO; PR:Q9ZU93; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZU93; baseline and differential.
DR Genevisible; Q9ZU93; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0009620; P:response to fungus; IEP:UniProtKB.
DR InterPro; IPR036339; PUB-like_dom_sf.
DR InterPro; IPR018997; PUB_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF09409; PUB; 1.
DR SUPFAM; SSF143503; SSF143503; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Reference proteome; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..458
FT /note="Plant UBX domain-containing protein 2"
FT /id="PRO_0000432601"
FT DOMAIN 181..248
FT /note="PUB"
FT /evidence="ECO:0000255"
FT DOMAIN 349..433
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT ZN_FING 121..143
FT /note="C2H2-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 51064 MW; D2FFD9F7B200BD60 CRC64;
MDDVKDKLKG FMKKVNLSSS SGKFKGQGRV LGSSSSSSAP PVNPIQNRFN SSQAPNPTPR
PKPNPNPLPE KPLSSSDQKI SGSTRNPDHD PVRAPQDGFD PYGAFITSSN RSQNGYSLSM
FECPICKNPF TSEEEVSVHV ESCLGDTNGD ESSFEKDNND NDKSEMEKLV VVYLSGKPSE
SSIDVLLRLF KNIVKEPENA KFRKVRMSNA KIKEAIGDVA GGVELLELVG FELKEENDEI
WAVMDVPSEE QSILINKVVG YLEKRKTESS GSSAQVMEPV APKKIDREIR VFFSVSENVA
SRIEVPDSFY SLSADEIKRE ADLRRKKIAE SQLLIPRSYK EKQAKAARKR YKRSMIRVQF
PDGVVLQGVF APWEPTFALY EFVSSALKEP SLQFELLDPV LVKRRVIPHT PAPGQKPITL
EDEELVPSAL IRFRPIETDS LVFTGLRNEL LEISEPLS
