PUB18_ARATH
ID PUB18_ARATH Reviewed; 697 AA.
AC Q9XIJ5; Q8S9I5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=U-box domain-containing protein 18 {ECO:0000303|PubMed:11495788};
DE EC=2.3.2.27 {ECO:0000269|PubMed:27956469};
DE AltName: Full=Plant U-box protein 18 {ECO:0000303|PubMed:11495788};
DE AltName: Full=RING-type E3 ubiquitin transferase PUB18 {ECO:0000303|PubMed:11495788};
GN Name=PUB18 {ECO:0000303|PubMed:11495788};
GN OrderedLocusNames=At1g10560 {ECO:0000312|Araport:AT1G10560};
GN ORFNames=T10O24.19 {ECO:0000312|EMBL:AAD39579.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] OF 443-697.
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 FUNCTION, INTERACTION WITH EXO70B1, DOMAIN UND, MUTAGENESIS OF
RP 23-SER--ILE-210 AND VAL-305, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27956469; DOI=10.1105/tpc.16.00347;
RA Seo D.H., Ahn M.Y., Park K.Y., Kim E.Y., Kim W.T.;
RT "The N-terminal UND motif of the Arabidopsis U-box E3 ligase PUB18 is
RT critical for the negative regulation of ABA-mediated stomatal movement and
RT determines its ubiquitination specificity for exocyst subunit Exo70B1.";
RL Plant Cell 28:2952-2973(2016).
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase (By similarity). Mediates
CC EXO70B1 ubiquitination. Involved in the regulation of abscisic acid
CC (ABA)-mediated stomatal movements (PubMed:27956469). {ECO:0000250,
CC ECO:0000269|PubMed:27956469}.
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; Evidence={ECO:0000269|PubMed:27956469};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:27956469}.
CC -!- SUBUNIT: Interacts with EXO70B1 via its U-box N-terminal domain (UND).
CC {ECO:0000269|PubMed:27956469}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:27956469}. Note=Displays a punctate pattern.
CC Colocalizes with EXO70B1. {ECO:0000269|PubMed:27956469}.
CC -!- DOMAIN: The U-box N-terminal domain (UND) confers binding specificity
CC and subsequent ubiquitination. {ECO:0000269|PubMed:27956469}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL77690.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC007067; AAD39579.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28594.1; -; Genomic_DNA.
DR EMBL; AY075683; AAL77690.1; ALT_INIT; mRNA.
DR PIR; B86239; B86239.
DR RefSeq; NP_172526.1; NM_100931.3.
DR AlphaFoldDB; Q9XIJ5; -.
DR SMR; Q9XIJ5; -.
DR STRING; 3702.AT1G10560.1; -.
DR iPTMnet; Q9XIJ5; -.
DR PaxDb; Q9XIJ5; -.
DR PRIDE; Q9XIJ5; -.
DR EnsemblPlants; AT1G10560.1; AT1G10560.1; AT1G10560.
DR GeneID; 837597; -.
DR Gramene; AT1G10560.1; AT1G10560.1; AT1G10560.
DR KEGG; ath:AT1G10560; -.
DR Araport; AT1G10560; -.
DR TAIR; locus:2194564; AT1G10560.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_006348_5_2_1; -.
DR InParanoid; Q9XIJ5; -.
DR OMA; HDFYERR; -.
DR OrthoDB; 720131at2759; -.
DR PhylomeDB; Q9XIJ5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9XIJ5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XIJ5; baseline and differential.
DR Genevisible; Q9XIJ5; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP: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:0016567; P:protein ubiquitination; IDA:TAIR.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0010029; P:regulation of seed germination; IGI:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:UniProtKB.
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; PF00514; Arm; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 4.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Membrane; Reference proteome; Repeat;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..697
FT /note="U-box domain-containing protein 18"
FT /id="PRO_0000322162"
FT DOMAIN 287..361
FT /note="U-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01034"
FT REPEAT 420..459
FT /note="ARM 1"
FT /evidence="ECO:0000255"
FT REPEAT 461..500
FT /note="ARM 2"
FT /evidence="ECO:0000255"
FT REPEAT 502..544
FT /note="ARM 3"
FT /evidence="ECO:0000255"
FT REPEAT 546..587
FT /note="ARM 4"
FT /evidence="ECO:0000255"
FT REPEAT 589..631
FT /note="ARM 5"
FT /evidence="ECO:0000255"
FT REPEAT 657..696
FT /note="ARM 6"
FT /evidence="ECO:0000255"
FT REGION 23..210
FT /note="U-box N-terminal domain (UND) required for EXO70B1
FT binding and crucial for the negative regulation of ABA-
FT dependent stomatal movement"
FT /evidence="ECO:0000269|PubMed:27956469"
FT MUTAGEN 23..210
FT /note="Missing: Impaired EXO70B1 binding. Altered
FT ubiquitination of EXO70B1, but unusual binding and
FT ubiquitination of EXO70B2. Reduced abscisic acid (ABA)-
FT mediated stomatal movements."
FT /evidence="ECO:0000269|PubMed:27956469"
FT MUTAGEN 305
FT /note="V->I: Abrogated E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:27956469"
FT CONFLICT 648
FT /note="M -> V (in Ref. 3; AAL77690)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="L -> H (in Ref. 3; AAL77690)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 697 AA; 76995 MW; F014FE42FC256F09 CRC64;
MIHTKTGSGR RILTFPTVEP SESISIVTLL DSLIQLAGDI LTFKSKHFST NKQSFRETLR
RIQNLLVVFE EIRIRIRNSR RYFHDSAAAS SLKEIHVGFQ KLKFLLEDCT RDGARLCMMM
NSDQVSDHLR VLTRSISTSL SAFPVASVDL TTEVNELIDL VVRQARKYGV QPETNDKRAV
SSINRILALF VNRVVPDPDE INRILDHVGI RKWGDCVKEI NFLGEEIDAE RLDEKKKKSS
DQVELLSSLM GFICYCRCII LGRIERDDHH NHHEDGIKKD HDLIRGLKVE DLLCPISLEI
MTDPVVIETG HTYDRSSITK WFGSGNITCP ITGKILTSTE LVDNVSVRQV IRKHCKTNGI
VLAGISRRRK SHDDVVPESL AAKGAGKLIA KFLTSELING GEEMIYRAVR EIRVQTKTSS
FNRSCLVKAG AVTPLLKLLS SVDIRIQENA MAGILNLSKH VTGKSKIAGE GLKILVEILN
EGAKTETRLY SASALFYLSS VEDYSRLIGE NPDAIPGLMN IVKGDDYGDS AKRSALLAVM
GLLMQSDNHW RVLAAGAVPI LLDLLRSGEI SGGLTADCLA TLAKLAEYPD GTIGVIRRGG
LKLAVKILSS SEDSPVAVKQ HCVGLILNLC LNGGRDVVGV LVKNSLVMGS LYTVLSNGEY
GGSKKASALI RMIHEFQERK TGSVEPNLQR GRFVHAW
