PUX8_ARATH
ID PUX8_ARATH Reviewed; 564 AA.
AC F4JPR7; Q94B82; Q9CB00; Q9T0E1;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Plant UBX domain-containing protein 8 {ECO:0000303|Ref.5};
DE Short=PUX8 {ECO:0000303|Ref.5};
DE AltName: Full=Ara4-interacting protein {ECO:0000312|EMBL:BAB32954.1};
DE AltName: Full=Suppressor of ARA4-induced defect of ypt1 {ECO:0000303|PubMed:10758485};
DE Short=SAY1 {ECO:0000303|PubMed:10758485};
GN Name=PUX8 {ECO:0000303|Ref.5}; Synonyms=SAY1 {ECO:0000312|EMBL:BAB32954.1};
GN OrderedLocusNames=At4g11740 {ECO:0000312|Araport:AT4G11740};
GN ORFNames=T5C23.170 {ECO:0000312|EMBL:CAB39945.1};
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] (ISOFORM 2), AND INTERACTION WITH RABA5C.
RX PubMed=10758485; DOI=10.1046/j.1365-313x.2000.00681.x;
RA Ueda T., Matsuda N., Uchimiya H., Nakano A.;
RT "Modes of interaction between the Arabidopsis Rab protein, Ara4, and its
RT putative regulator molecules revealed by a yeast expression system.";
RL Plant J. 21:341-349(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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] OF 125-564 (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 [5]
RP GENE FAMILY.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-326 AND SER-328, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-324; SER-326 AND
RP SER-328, AND IDENTIFICATION BY 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).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 -!- SUBUNIT: Interacts with RABA5C/ARA-4. {ECO:0000269|PubMed:10758485}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4JPR7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JPR7-2; Sequence=VSP_057530, VSP_057531;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK68728.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB39945.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78217.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB007767; BAB32954.1; -; mRNA.
DR EMBL; AL049500; CAB39945.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161532; CAB78217.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83043.1; -; Genomic_DNA.
DR EMBL; AY042788; AAK68728.1; ALT_INIT; mRNA.
DR EMBL; AY064650; AAL47361.1; -; mRNA.
DR PIR; T04221; T04221.
DR RefSeq; NP_567380.2; NM_117243.4. [F4JPR7-1]
DR AlphaFoldDB; F4JPR7; -.
DR SMR; F4JPR7; -.
DR STRING; 3702.AT4G11740.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR iPTMnet; F4JPR7; -.
DR PaxDb; F4JPR7; -.
DR PRIDE; F4JPR7; -.
DR ProteomicsDB; 224801; -. [F4JPR7-1]
DR EnsemblPlants; AT4G11740.1; AT4G11740.1; AT4G11740. [F4JPR7-1]
DR GeneID; 826779; -.
DR Gramene; AT4G11740.1; AT4G11740.1; AT4G11740. [F4JPR7-1]
DR KEGG; ath:AT4G11740; -.
DR Araport; AT4G11740; -.
DR TAIR; locus:2139787; AT4G11740.
DR eggNOG; KOG1363; Eukaryota.
DR HOGENOM; CLU_035367_0_0_1; -.
DR InParanoid; F4JPR7; -.
DR OMA; QVSHPRE; -.
DR OrthoDB; 677590at2759; -.
DR PRO; PR:F4JPR7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JPR7; baseline and differential.
DR Genevisible; F4JPR7; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:TAIR.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR InterPro; IPR003903; UIM_dom.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00166; UBX; 1.
DR SMART; SM00726; UIM; 2.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
DR PROSITE; PS50330; UIM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..564
FT /note="Plant UBX domain-containing protein 8"
FT /id="PRO_0000432606"
FT DOMAIN 2..44
FT /note="UBA-like"
FT DOMAIN 198..217
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 230..249
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 482..560
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 210..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 412..478
FT /evidence="ECO:0000255"
FT COMPBIAS 267..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT VAR_SEQ 463..467
FT /note="ELERQ -> ASASG (in isoform 2)"
FT /id="VSP_057530"
FT VAR_SEQ 468..564
FT /note="Missing (in isoform 2)"
FT /id="VSP_057531"
SQ SEQUENCE 564 AA; 62350 MW; 902F7EF5484F231F CRC64;
MATPNQEAID TFISITGASD AVALQKLEEH RGDLNQAVNA YFSEGDRNVV REAPVNDDDE
MDIDDVIPAP QSPLSMFNAA RTIGRPPFSL LDSDFARRVF DSDPLMPRPP FVSHPREVRQ
IPIEVKDSSG PSGRSSDAPT IEDVTETAHV QGPVTTQGTV IIDEESDDDI PFAPMGRSRQ
DRPAGSVANN NNQDYNDIEE EMIRAAIEAS KKEAEGSSNP LLEERPLHME DDDDIAIAVT
MSLKSAEEEV LRSQGYKAST SEIGASAVTA AQGPQDTQAL NGRLAAPSSP FDDDSDDVDE
QPLVRHRPRR AASGSLAPPN ADRSRSGSPE EEHASINPAE RGSGFPSEWG GISSEEHDEA
VMLEAAMFGG IPETGYNHLP FLPPQPRAQP RPPSPSLTAQ RLIREQQDDE YVASLQADRD
KEMKSIRDAE ARQLEEETAR KAFLEEEKKK EEEAQRKLEE EQELERQLDA KEASLPKEPQ
ADEENAITLL IRMPDGTRRG RRFLKSDKLQ TLFNFIDIAR VVKPNTYRLV RPYPRHAFGD
GESESTLNDL GLTSKQEALF LELI
