PUB8_ARATH
ID PUB8_ARATH Reviewed; 374 AA.
AC O81902; A3RCC8; A7Y5W2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=U-box domain-containing protein 8;
DE EC=2.3.2.27;
DE AltName: Full=Plant U-box protein 8;
DE AltName: Full=RING-type E3 ubiquitin transferase PUB8 {ECO:0000305};
GN Name=PUB8; Synonyms=B80; OrderedLocusNames=At4g21350; ORFNames=T6K22.80;
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], AND VARIANTS SER-58; PRO-77; ARG-104;
RP VAL-179; ALA-184; LYS-308 AND ASN-366.
RC STRAIN=cv. C24;
RX PubMed=17237349; DOI=10.1105/tpc.106.048199;
RA Sherman-Broyles S., Boggs N., Farkas A., Liu P., Vrebalov J.,
RA Nasrallah M.E., Nasrallah J.B.;
RT "S locus genes and the evolution of self-fertility in Arabidopsis
RT thaliana.";
RL Plant Cell 19:94-106(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-58; SER-70; PRO-77;
RP GLN-91; ARG-104; ALA-184; ALA-191; SER-311; ARG-330 AND ASN-366.
RC STRAIN=cv. Cvi-0;
RX PubMed=17656687; DOI=10.1126/science.1143153;
RA Tang C., Toomajian C., Sherman-Broyles S., Plagnol V., Guo Y.-L., Hu T.T.,
RA Clark R.M., Nasrallah J.B., Weigel D., Nordborg M.;
RT "The evolution of selfing in Arabidopsis thaliana.";
RL Science 317:1070-1072(2007).
RN [3]
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 [4]
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 [5]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=11495788; DOI=10.1016/s1360-1385(01)01960-4;
RA Azevedo C., Santos-Rosa M.J., Shirasu K.;
RT "The U-box protein family in plants.";
RL Trends Plant Sci. 6:354-358(2001).
RN [6]
RP GENE FAMILY ORGANIZATION.
RX PubMed=14657406; DOI=10.1104/pp.103.029553;
RA Mudgil Y., Shiu S.-H., Stone S.L., Salt J.N., Goring D.R.;
RT "A large complement of the predicted Arabidopsis ARM repeat proteins are
RT members of the U-box E3 ubiquitin ligase family.";
RL Plant Physiol. 134:59-66(2004).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17412590; DOI=10.1016/j.cub.2007.03.022;
RA Liu P., Sherman-Broyles S., Nasrallah M.E., Nasrallah J.B.;
RT "A cryptic modifier causing transient self-incompatibility in Arabidopsis
RT thaliana.";
RL Curr. Biol. 17:734-740(2007).
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase (By similarity). Involved
CC in the age-dependent pseudo-self-compatibility process. {ECO:0000250,
CC ECO:0000269|PubMed:17412590}.
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.
CC -!- TISSUE SPECIFICITY: Expressed in the whole plant.
CC {ECO:0000269|PubMed:17412590}.
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DR EMBL; EF182720; ABN05290.1; -; Genomic_DNA.
DR EMBL; EF637083; ABV21211.1; -; Genomic_DNA.
DR EMBL; AL031187; CAA20200.1; -; Genomic_DNA.
DR EMBL; AL161554; CAB79134.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84444.1; -; Genomic_DNA.
DR PIR; T05177; T05177.
DR RefSeq; NP_193866.1; NM_118255.1.
DR AlphaFoldDB; O81902; -.
DR SMR; O81902; -.
DR STRING; 3702.AT4G21350.1; -.
DR iPTMnet; O81902; -.
DR PaxDb; O81902; -.
DR PRIDE; O81902; -.
DR EnsemblPlants; AT4G21350.1; AT4G21350.1; AT4G21350.
DR GeneID; 827885; -.
DR Gramene; AT4G21350.1; AT4G21350.1; AT4G21350.
DR KEGG; ath:AT4G21350; -.
DR Araport; AT4G21350; -.
DR TAIR; locus:2141226; AT4G21350.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_006348_0_0_1; -.
DR InParanoid; O81902; -.
DR OMA; TIGAYPY; -.
DR OrthoDB; 1280814at2759; -.
DR PhylomeDB; O81902; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O81902; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81902; baseline and differential.
DR Genevisible; O81902; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; NAS:TAIR.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 4.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway.
FT CHAIN 1..374
FT /note="U-box domain-containing protein 8"
FT /id="PRO_0000322153"
FT DOMAIN 4..79
FT /note="U-box"
FT REPEAT 126..165
FT /note="ARM 1"
FT REPEAT 167..206
FT /note="ARM 2"
FT REPEAT 208..248
FT /note="ARM 3"
FT REPEAT 250..288
FT /note="ARM 4"
FT REPEAT 289..327
FT /note="ARM 5"
FT VARIANT 58
FT /note="Y -> S (in strain: cv. C24 and cv. Cvi-0)"
FT /evidence="ECO:0000269|PubMed:17237349,
FT ECO:0000269|PubMed:17656687"
FT VARIANT 70
FT /note="L -> S (in strain: cv. Cvi-0)"
FT /evidence="ECO:0000269|PubMed:17656687"
FT VARIANT 77
FT /note="L -> P (in strain: cv. C24 and cv. Cvi-0)"
FT /evidence="ECO:0000269|PubMed:17237349,
FT ECO:0000269|PubMed:17656687"
FT VARIANT 91
FT /note="H -> Q (in strain: cv. Cvi-0)"
FT /evidence="ECO:0000269|PubMed:17656687"
FT VARIANT 104
FT /note="Q -> R (in strain: cv. C24 and cv. Cvi-0)"
FT /evidence="ECO:0000269|PubMed:17237349,
FT ECO:0000269|PubMed:17656687"
FT VARIANT 179
FT /note="I -> V (in strain: cv. C24)"
FT /evidence="ECO:0000269|PubMed:17237349"
FT VARIANT 184
FT /note="T -> A (in strain: cv. C24 and cv. Cvi-0)"
FT /evidence="ECO:0000269|PubMed:17237349,
FT ECO:0000269|PubMed:17656687"
FT VARIANT 191
FT /note="P -> A (in strain: cv. Cvi-0)"
FT /evidence="ECO:0000269|PubMed:17656687"
FT VARIANT 308
FT /note="R -> K (in strain: cv. C24)"
FT /evidence="ECO:0000269|PubMed:17237349"
FT VARIANT 311
FT /note="N -> S (in strain: cv. Cvi-0)"
FT /evidence="ECO:0000269|PubMed:17656687"
FT VARIANT 330
FT /note="G -> R (in strain: cv. Cvi-0)"
FT /evidence="ECO:0000269|PubMed:17656687"
FT VARIANT 366
FT /note="T -> N (in strain: cv. C24 and cv. Cvi-0)"
FT /evidence="ECO:0000269|PubMed:17237349,
FT ECO:0000269|PubMed:17656687"
SQ SEQUENCE 374 AA; 40875 MW; DD137FE6C19264EF CRC64;
MAFDLPNDFR CPISLEIMSD PVILQSGHTF DRVSIQQWID SGNRTCPITK LPLSETPYLI
PNHALRSLIL NFAHVSLKES SRPRTQQEHS HSQSQALIST LVSQSSSNAS KLESLTRLVR
LTKRDSSIRR KVTESGAVRA ALDCVDSCNQ VLQEKSLSLL LNLSLEDDNK VGLVADGVIR
RIVTVLRVGS PDCKAIAATL LTSLAVVEVN KATIGSYPDA ISALVSLLRV GNDRERKESA
TALYALCSFP DNRKRVVDCG SVPILVEAAD SGLERAVEVL GLLVKCRGGR EEMSKVSGFV
EVLVNVLRNG NLKGIQYSLF ILNCLCCCSG EIVDEVKREG VVEICFGFED NESEKIRRNA
TILVHTLLGI PMSS
