PSMD4_ARATH
ID PSMD4_ARATH Reviewed; 386 AA.
AC P55034; Q8L9G3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 4 homolog;
DE AltName: Full=26S proteasome regulatory subunit RPN10;
DE Short=AtRPN10;
DE AltName: Full=26S proteasome regulatory subunit S5A homolog;
DE AltName: Full=Multiubiquitin chain-binding protein 1;
DE Short=AtMCB1;
GN Name=RPN10; Synonyms=MBP1, MCB1; OrderedLocusNames=At4g38630;
GN ORFNames=F20M13.190, T9A14.7;
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], AND FUNCTION.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8570648; DOI=10.1073/pnas.93.2.856;
RA van Nocker S., Deveraux Q., Rechsteiner M., Vierstra R.D.;
RT "Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component
RT of the 26S proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:856-860(1996).
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].
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.
RX PubMed=8530351; DOI=10.1074/jbc.270.50.29660;
RA Deveraux Q., van Nocker S., Mahaffey D., Vierstra R.D., Rechsteiner M.;
RT "Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26 S
RT protease subunit S5a.";
RL J. Biol. Chem. 270:29660-29663(1995).
RN [7]
RP SUBUNIT, AND FUNCTION.
RX PubMed=9741626; DOI=10.1016/s0092-8674(00)81603-7;
RA Glickman M.H., Rubin D.M., Coux O., Wefes I., Pfeifer G., Cjeka Z.,
RA Baumeister W., Fried V.A., Finley D.;
RT "A subcomplex of the proteasome regulatory particle required for ubiquitin-
RT conjugate degradation and related to the COP9-signalosome and eIF3.";
RL Cell 94:615-623(1998).
RN [8]
RP POLYUBIQUITIN BINDING, AND FUNCTION.
RX PubMed=9442033; DOI=10.1074/jbc.273.4.1970;
RA Fu H., Sadis S., Rubin D.M., Glickman M., van Nocker S., Finley D.,
RA Vierstra R.D.;
RT "Multiubiquitin chain binding and protein degradation are mediated by
RT distinct domains within the 26 S proteasome subunit Mcb1.";
RL J. Biol. Chem. 273:1970-1981(1998).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12671091; DOI=10.1105/tpc.009217;
RA Smalle J., Kurepa J., Yang P., Emborg T.J., Babiychuk E., Kushnir S.,
RA Vierstra R.D.;
RT "The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis
RT growth and development supports a substrate-specific function in abscisic
RT acid signaling.";
RL Plant Cell 15:965-980(2003).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=14623884; DOI=10.1074/jbc.m311977200;
RA Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., Vierstra R.D.;
RT "Purification of the Arabidopsis 26 S proteasome: biochemical and molecular
RT analyses revealed the presence of multiple isoforms.";
RL J. Biol. Chem. 279:6401-6413(2004).
RN [11]
RP INTERACTION WITH PI4KG4, AND PHOSPHORYLATION BY PI4KG4.
RX PubMed=17880284; DOI=10.1042/bj20070959;
RA Galvao R.M., Kota U., Soderblom E.J., Goshe M.B., Boss W.F.;
RT "Characterization of a new family of protein kinases from Arabidopsis
RT containing phosphoinositide 3/4-kinase and ubiquitin-like domains.";
RL Biochem. J. 409:117-127(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP 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 [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17971041; DOI=10.1111/j.1365-313x.2007.03322.x;
RA Kurepa J., Toh-E A., Smalle J.A.;
RT "26S proteasome regulatory particle mutants have increased oxidative stress
RT tolerance.";
RL Plant J. 53:102-114(2008).
RN [14]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19321709; DOI=10.1104/pp.109.135970;
RA Kurepa J., Wang S., Li Y., Zaitlin D., Pierce A.J., Smalle J.A.;
RT "Loss of 26S proteasome function leads to increased cell size and decreased
RT cell number in Arabidopsis shoot organs.";
RL Plant Physiol. 150:178-189(2009).
RN [15]
RP 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 [16]
RP FUNCTION, INTERACTION WITH RAD23B; RAD23C; RAD23D AND DSK2A, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20059542; DOI=10.1111/j.1742-4658.2009.07531.x;
RA Fatimababy A.S., Lin Y.L., Usharani R., Radjacommare R., Wang H.T.,
RA Tsai H.L., Lee Y., Fu H.;
RT "Cross-species divergence of the major recognition pathways of
RT ubiquitylated substrates for ubiquitin/26S proteasome-mediated
RT proteolysis.";
RL FEBS J. 277:796-816(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, AND SUBUNIT.
RX PubMed=20516081; DOI=10.1074/jbc.m110.136622;
RA Book A.J., Gladman N.P., Lee S.S., Scalf M., Smith L.M., Vierstra R.D.;
RT "Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse
RT array of plant proteolytic complexes.";
RL J. Biol. Chem. 285:25554-25569(2010).
RN [18]
RP INTERACTION WITH RAD23B, AND POLYUBIQUITIN BINDING.
RX PubMed=20086187; DOI=10.1105/tpc.109.072660;
RA Farmer L.M., Book A.J., Lee K.H., Lin Y.L., Fu H., Vierstra R.D.;
RT "The RAD23 family provides an essential connection between the 26S
RT proteasome and ubiquitylated proteins in Arabidopsis.";
RL Plant Cell 22:124-142(2010).
RN [19]
RP REVIEW.
RX PubMed=20399133; DOI=10.1016/j.tplants.2010.03.004;
RA Fu H., Lin Y.L., Fatimababy A.S.;
RT "Proteasomal recognition of ubiquitylated substrates.";
RL Trends Plant Sci. 15:375-386(2010).
RN [20]
RP FUNCTION, DISRUPTION PHENOTYPE, POLYUBIQUITIN BINDING, AND INTERACTION WITH
RP RAD23B; RAD23C; RAD23D AND DSK2B.
RX PubMed=21764993; DOI=10.1105/tpc.111.086702;
RA Lin Y.-L., Sung S.-C., Tsai H.-L., Yu T.-T., Radjacommare R., Usharani R.,
RA Fatimababy A.S., Lin H.-Y., Wang Y.-Y., Fu H.;
RT "The defective proteasome but not substrate recognition function is
RT responsible for the null phenotypes of the Arabidopsis proteasome subunit
RT RPN10.";
RL Plant Cell 23:2754-2773(2011).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22751321; DOI=10.4161/psb.20360;
RA Lin Y.L., Fu H.;
RT "In vivo relevance of substrate recognition function of major Arabidopsis
RT ubiquitin receptors.";
RL Plant Signal. Behav. 7:722-727(2012).
CC -!- FUNCTION: Plays a role in maintaining the structural integrity of the
CC 19S regulatory particle (RP), subcomplex of the 26S proteasome. Plays a
CC major role in both the direct and indirect recognition of ubiquitinated
CC substrates of ubiquitin/26S proteasome-mediated proteolysis (UPP).
CC Binds and presumably selects ubiquitin-conjugates for destruction.
CC Prefers multiubiquitin chains rather than single ubiquitins, with a
CC binding affinity for 'Lys-48'-linked ubiquitin chains. Acts as a
CC potential docking subunit for both ubiquitin receptors RAD23s and
CC DSK2s. Plays a role in the growth and development via the proteasome-
CC dependent degradation of the ABA-signaling protein ABI5/DPBF1. Plays an
CC important role for balancing cell expansion with cell proliferation
CC rates during shoot development. {ECO:0000269|PubMed:12671091,
CC ECO:0000269|PubMed:17971041, ECO:0000269|PubMed:19321709,
CC ECO:0000269|PubMed:20059542, ECO:0000269|PubMed:21764993,
CC ECO:0000269|PubMed:22751321, ECO:0000269|PubMed:8530351,
CC ECO:0000269|PubMed:8570648, ECO:0000269|PubMed:9442033,
CC ECO:0000269|PubMed:9741626}.
CC -!- SUBUNIT: Component of the 19S regulatory particle (RP/PA700) base
CC subcomplex of the 26S proteasome. The 26S proteasome is composed of a
CC core protease (CP), known as the 20S proteasome, capped at one or both
CC ends by the 19S regulatory particle (RP/PA700). The RP/PA700 complex is
CC composed of at least 17 different subunits in two subcomplexes, the
CC base and the lid, which form the portions proximal and distal to the
CC 20S proteolytic core, respectively. Interacts with PI4KG4. Interacts
CC with RAD23s and DSK2s via its UIM3 and UIM1 motif, respectively.
CC Interacts with 'Lys-48'-linked polyubiquitin chains via its UIM1 motif.
CC {ECO:0000269|PubMed:17880284, ECO:0000269|PubMed:20059542,
CC ECO:0000269|PubMed:20086187, ECO:0000269|PubMed:20516081,
CC ECO:0000269|PubMed:21764993, ECO:0000269|PubMed:9741626}.
CC -!- INTERACTION:
CC P55034; Q9SII8: DSK2B; NbExp=2; IntAct=EBI-2620423, EBI-4433040;
CC P55034; Q9SFT9: T1B9.26; NbExp=3; IntAct=EBI-2620423, EBI-4460083;
CC P55034; P0CG48: UBC; Xeno; NbExp=2; IntAct=EBI-2620423, EBI-3390054;
CC -!- TISSUE SPECIFICITY: Ubiquitous with highest expression in flowers.
CC {ECO:0000269|PubMed:14623884}.
CC -!- PTM: Phosphorylated by PI4KG4 in vitro. {ECO:0000269|PubMed:17880284}.
CC -!- DISRUPTION PHENOTYPE: Displays reduced seed germination, growth rate,
CC stamen number, genetic transmission through the male gamete, hormone-
CC induced cell division and increased oxidative stress tolerance. Is also
CC more sensitive to abscisic acid (ABA), salt, sucrose stress, heat shock
CC and DNA-damaging agents and shows a decreased sensitivity to cytokinin
CC and auxin. In flowers, epidermal cells in petals were larger than those
CC in the wild type. {ECO:0000269|PubMed:12671091,
CC ECO:0000269|PubMed:17971041, ECO:0000269|PubMed:19321709,
CC ECO:0000269|PubMed:20059542, ECO:0000269|PubMed:21764993,
CC ECO:0000269|PubMed:22751321}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S5A family.
CC {ECO:0000305}.
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DR EMBL; U33269; AAA85583.1; -; mRNA.
DR EMBL; AL035540; CAB37519.1; -; Genomic_DNA.
DR EMBL; AL035656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161593; CAB80527.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86956.1; -; Genomic_DNA.
DR EMBL; AF360319; AAK26029.1; -; mRNA.
DR EMBL; AY113889; AAM44937.1; -; mRNA.
DR EMBL; AY088449; AAM65985.1; -; mRNA.
DR PIR; T05691; T05691.
DR RefSeq; NP_195575.1; NM_120024.3.
DR AlphaFoldDB; P55034; -.
DR SMR; P55034; -.
DR BioGRID; 15299; 47.
DR IntAct; P55034; 11.
DR MINT; P55034; -.
DR STRING; 3702.AT4G38630.1; -.
DR iPTMnet; P55034; -.
DR PaxDb; P55034; -.
DR PRIDE; P55034; -.
DR ProteomicsDB; 224827; -.
DR EnsemblPlants; AT4G38630.1; AT4G38630.1; AT4G38630.
DR GeneID; 830019; -.
DR Gramene; AT4G38630.1; AT4G38630.1; AT4G38630.
DR KEGG; ath:AT4G38630; -.
DR Araport; AT4G38630; -.
DR TAIR; locus:2121269; AT4G38630.
DR eggNOG; KOG2884; Eukaryota.
DR HOGENOM; CLU_033293_0_0_1; -.
DR InParanoid; P55034; -.
DR OMA; MTDQANV; -.
DR OrthoDB; 1244685at2759; -.
DR PhylomeDB; P55034; -.
DR PRO; PR:P55034; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P55034; baseline and differential.
DR Genevisible; P55034; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0001653; F:peptide receptor activity; IDA:TAIR.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0048528; P:post-embryonic root development; IMP:TAIR.
DR GO; GO:0043248; P:proteasome assembly; IMP:TAIR.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:TAIR.
DR GO; GO:0030163; P:protein catabolic process; TAS:TAIR.
DR GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0051788; P:response to misfolded protein; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IMP:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR GO; GO:0048455; P:stamen formation; IMP:TAIR.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF02809; UIM; 2.
DR Pfam; PF13519; VWA_2; 1.
DR SMART; SM00726; UIM; 3.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50330; UIM; 3.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Proteasome; Reference proteome; Repeat.
FT CHAIN 1..386
FT /note="26S proteasome non-ATPase regulatory subunit 4
FT homolog"
FT /id="PRO_0000173832"
FT DOMAIN 5..190
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 221..240
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 282..301
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 305..324
FT /note="UIM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 241..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT CONFLICT 253
FT /note="G -> C (in Ref. 5; AAM65985)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="T -> H (in Ref. 5; AAM65985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 40757 MW; 2F5C89D9FACB4550 CRC64;
MVLEATMICI DNSEWMRNGD YSPSRLQAQT EAVNLLCGAK TQSNPENTVG ILTMAGKGVR
VLTTPTSDLG KILACMHGLD VGGEINLTAA IQIAQLALKH RQNKNQRQRI IVFAGSPIKY
EKKALEIVGK RLKKNSVSLD IVNFGEDDDE EKPQKLEALL TAVNNNDGSH IVHVPSGANA
LSDVLLSTPV FTGDEGASGY VSAAAAAAAA GGDFDFGVDP NIDPELALAL RVSMEEERAR
QEAAAKKAAD EAGQKDKDGD TASASQETVA RTTDKNAEPM DEDSALLDQA IAMSVGDVNM
SEAADEDQDL ALALQMSMSG EESSEATGAG NNLLGNQAFI SSVLSSLPGV DPNDPAVKEL
LASLPDESKR TEEEESSSKK GEDEKK
