PUB9_ARATH
ID PUB9_ARATH Reviewed; 460 AA.
AC Q9SRT0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=U-box domain-containing protein 9;
DE EC=2.3.2.27;
DE AltName: Full=Plant U-box protein 9;
DE AltName: Full=RING-type E3 ubiquitin transferase PUB9 {ECO:0000305};
GN Name=PUB9; OrderedLocusNames=At3g07360; ORFNames=F21O3.7;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP INTERACTION WITH SD11; SD16; SD17; SD18; SD113; SD129 AND SD25, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18552232; DOI=10.1104/pp.108.123380;
RA Samuel M.A., Mudgil Y., Salt J.N., Delmas F., Ramachandran S., Chilelli A.,
RA Goring D.R.;
RT "Interactions between the S-domain receptor kinases and AtPUB-ARM E3
RT ubiquitin ligases suggest a conserved signaling pathway in Arabidopsis.";
RL Plant Physiol. 147:2084-2095(2008).
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase (By similarity). May be
CC involved in the abscisic acid-mediated signaling pathway, at least
CC during germination. {ECO:0000250, ECO:0000269|PubMed:18552232}.
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 -!- SUBUNIT: Binds to SD11, SD16, SD17, SD18, SD113, SD129 and SD25.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18552232}. Cell
CC membrane {ECO:0000269|PubMed:18552232}. Note=Relocates from nucleus to
CC plasma membrane when phosphorylated.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SRT0-1; Sequence=Displayed;
CC -!- PTM: Phosphorylated by SD1-6 and SD1-7. {ECO:0000269|PubMed:18552232}.
CC -!- DISRUPTION PHENOTYPE: Reduced abscisic acid (ABA) sensitivity during
CC seed germination. {ECO:0000269|PubMed:18552232}.
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DR EMBL; AC009853; AAF02146.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74532.1; -; Genomic_DNA.
DR EMBL; AY075636; AAL91644.1; -; mRNA.
DR RefSeq; NP_566304.1; NM_111615.4. [Q9SRT0-1]
DR AlphaFoldDB; Q9SRT0; -.
DR SMR; Q9SRT0; -.
DR BioGRID; 5259; 3.
DR STRING; 3702.AT3G07360.1; -.
DR iPTMnet; Q9SRT0; -.
DR PaxDb; Q9SRT0; -.
DR PRIDE; Q9SRT0; -.
DR ProteomicsDB; 226264; -. [Q9SRT0-1]
DR EnsemblPlants; AT3G07360.1; AT3G07360.1; AT3G07360. [Q9SRT0-1]
DR GeneID; 819924; -.
DR Gramene; AT3G07360.1; AT3G07360.1; AT3G07360. [Q9SRT0-1]
DR KEGG; ath:AT3G07360; -.
DR Araport; AT3G07360; -.
DR TAIR; locus:2079706; AT3G07360.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_006348_0_0_1; -.
DR InParanoid; Q9SRT0; -.
DR OMA; DQCKRNK; -.
DR PhylomeDB; Q9SRT0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SRT0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRT0; baseline and differential.
DR Genevisible; Q9SRT0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0070696; F:transmembrane receptor protein serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IMP:UniProtKB.
DR GO; GO:0048527; P:lateral root development; IGI:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA: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; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Cell membrane;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..460
FT /note="U-box domain-containing protein 9"
FT /id="PRO_0000322154"
FT DOMAIN 73..147
FT /note="U-box"
FT REPEAT 201..244
FT /note="ARM 1"
FT REPEAT 248..287
FT /note="ARM 2"
FT REPEAT 289..328
FT /note="ARM 3"
SQ SEQUENCE 460 AA; 51279 MW; FE35CC691CE75450 CRC64;
MAKTGVFDSD PTAIAKAKEL KREMKKLLIK IDDEDDLGVQ TIDQLQDALS ALREATMRKM
AKSSSLEMLE TVSCPEEFRC PLSNELMRDP VVLASGQTYD KLFIQKWLSS GNRTCPKTQQ
VLPHTALTPN LLIREMISKW CKKNGLETKS QYHPNLVNED ETVTRSDREI FNSLLCKVSS
SNLQDQKSAA KELRLLTRKG TEFRALFGES PDEITRLVNP LLHGSNPDEK LQEDVVTTLL
NISIHDDSNK KLVCENPNVI PLLIDALRRG TVATRSNAAA AIFTLSALDS NKVLIGKSGI
LKPLIDLLEE GNPLAIKDVA AAIFTLCIAH ENRSRAVRDG AVRVLGKKIS NGLYVDELLA
ILAMLVTHWK AVEELGELGG VSWLLKITRE SECKRNKENA IVILHTICFS DRTKWKEIKE
EENAHGTITK LSREGTSRAQ RKANGILDRL RKAMNLTHTA
