UPL3_ARATH
ID UPL3_ARATH Reviewed; 1888 AA.
AC Q6WWW4; Q0WN20; Q9SZN9; Q9SZP0;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=E3 ubiquitin-protein ligase UPL3;
DE Short=Ubiquitin-protein ligase 3;
DE EC=2.3.2.26;
DE AltName: Full=HECT ubiquitin-protein ligase 3;
DE AltName: Full=HECT-type E3 ubiquitin transferase UPL3;
DE AltName: Full=Protein KAKTUS;
GN Name=UPL3; Synonyms=KAK; OrderedLocusNames=At4g38600/At4g38610;
GN ORFNames=F20M13.160/F20M13.170;
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 GENE FAMILY ORGANIZATION.
RX PubMed=12969426; DOI=10.1046/j.1365-313x.2003.01844.x;
RA Downes B.P., Stupar R.M., Gingerich D.J., Vierstra R.D.;
RT "The HECT ubiquitin-protein ligase (UPL) family in Arabidopsis: UPL3 has a
RT specific role in trichome development.";
RL Plant J. 35:729-742(2003).
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 1196-1888.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=14530964; DOI=10.1007/s00438-003-0932-1;
RA El Refy A., Perazza D., Zekraoui L., Valay J.-G., Bechtold N., Brown S.,
RA Huelskamp M., Herzog M., Bonneville J.-M.;
RT "The Arabidopsis KAKTUS gene encodes a HECT protein and controls the number
RT of endoreduplication cycles.";
RL Mol. Genet. Genomics 270:403-414(2003).
RN [6]
RP FUNCTION.
RX PubMed=10224275; DOI=10.1093/genetics/152.1.461;
RA Perazza D., Herzog M., Huelskamp M., Brown S., Dorne A.-M.,
RA Bonneville J.-M.;
RT "Trichome cell growth in Arabidopsis thaliana can be derepressed by
RT mutations in at least five genes.";
RL Genetics 152:461-476(1999).
RN [7]
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).
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase which mediates
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Involved in the repression of endoreduplication process and
CC the cell morphogenesis in the trichomes. {ECO:0000269|PubMed:10224275,
CC ECO:0000269|PubMed:14530964}.
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=2.3.2.26;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
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=Q6WWW4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14530964}.
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB37516.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g38600 and At4g38610.; Evidence={ECO:0000305};
CC Sequence=CAB37517.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g38600 and At4g38610.; Evidence={ECO:0000305};
CC Sequence=CAB80524.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g38600 and At4g38610.; Evidence={ECO:0000305};
CC Sequence=CAB80525.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g38600 and At4g38610.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY265959; AAP91821.1; -; mRNA.
DR EMBL; AL035540; CAB37516.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL035540; CAB37517.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161593; CAB80524.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161593; CAB80525.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86954.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67531.1; -; Genomic_DNA.
DR EMBL; AK229635; BAF01480.1; -; mRNA.
DR EMBL; BN000268; CAE30362.1; -; mRNA.
DR PIR; T05688; T05688.
DR PIR; T05689; T05689.
DR RefSeq; NP_001329354.1; NM_001342508.1. [Q6WWW4-1]
DR RefSeq; NP_849567.2; NM_179236.3. [Q6WWW4-1]
DR AlphaFoldDB; Q6WWW4; -.
DR SMR; Q6WWW4; -.
DR BioGRID; 15297; 2.
DR STRING; 3702.AT4G38600.1; -.
DR iPTMnet; Q6WWW4; -.
DR PaxDb; Q6WWW4; -.
DR PRIDE; Q6WWW4; -.
DR ProteomicsDB; 233003; -. [Q6WWW4-1]
DR EnsemblPlants; AT4G38600.1; AT4G38600.1; AT4G38600. [Q6WWW4-1]
DR EnsemblPlants; AT4G38600.3; AT4G38600.3; AT4G38600. [Q6WWW4-1]
DR GeneID; 830017; -.
DR Gramene; AT4G38600.1; AT4G38600.1; AT4G38600. [Q6WWW4-1]
DR Gramene; AT4G38600.3; AT4G38600.3; AT4G38600. [Q6WWW4-1]
DR KEGG; ath:AT4G38600; -.
DR Araport; AT4G38600; -.
DR TAIR; locus:2121224; AT4G38600.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR InParanoid; Q6WWW4; -.
DR OMA; PLECADE; -.
DR OrthoDB; 34110at2759; -.
DR PhylomeDB; Q6WWW4; -.
DR BRENDA; 2.3.2.26; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6WWW4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q6WWW4; baseline and differential.
DR Genevisible; Q6WWW4; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:TAIR.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:TAIR.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0010091; P:trichome branching; IMP:TAIR.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR PANTHER; PTHR45670; PTHR45670; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00185; ARM; 3.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..1888
FT /note="E3 ubiquitin-protein ligase UPL3"
FT /id="PRO_0000312021"
FT REPEAT 227..267
FT /note="ARM 1"
FT REPEAT 270..310
FT /note="ARM 2"
FT REPEAT 312..349
FT /note="ARM 3"
FT REPEAT 351..390
FT /note="ARM 4"
FT DOMAIN 1490..1888
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1451
FT /note="K-box"
FT COMPBIAS 32..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1113
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1855
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1888 AA; 202928 MW; AFB582F4E2510441 CRC64;
METRSRKRAE ATSAAPSSSS SSPPPPPSAS GPTTRSKRAR LSSSSSSSLA PTPPSSSTTT
RSRSSRSAAA AAPMDTSTDS SGFRRGGRGN RGNNNDNSDK GKEKEHDVRI RERERERDRA
REQLNMDAAA AAARSADEDD DNDSEDGNGG FMHPNMSSAS SALQGLLRKL GAGLDDLLPS
SGIGSASSSH LNGRMKKILS GLRAEGEEGK QVEALTQLCE MLSIGTEDSL STFSVDSFVP
VLVGLLNHES NPDIMLLAAR ALTHLCDVLP SSCAAVVHYG AVSCLVARLL TIEYMDLAEQ
SLQALKKISQ EHPTACLRAG ALMAVLSYLD FFSTGVQRVA LSTAANMCKK LPSDASDYVM
EAVPLLTNLL QYHDSKVLEY ASICLTRIAE AFAPYPEKLD ELCNHGLVTQ AASLISTSNS
GGGQASLSVS TYTGLIRLLS TCASGSPLGF RTLLLLGISS ILKDILLGSG VSANASVSPA
LSRPADQIYE IVNLANELLP PLPEGVISLP TSTNALVKGS CQKKSSPSTS GKQEDILKIS
PREKLLGDQP ELLQQFGLDL LPVLVQIYGS SVNGTIRHKC LSVIGKLMYF SSSEMIQSLI
GDTNISSFLA GVLAWKDPQV LVPALQVAEI LMEKLPETFS KVFVREGVVH AVDQLVLVGK
PSHASPTDKD NDCVPGSARS RRYRRRSSNA NSDGNQSEEP KNPASLTIGA NHNSLDTPTA
SFMLRETVSS CAKAFKDKYF PSDGGDVDVG VTDDLLHLKN LCTKLTAGID DHKVKGKGKS
KASGPFLGDF SASKEEYLIG VISEILGEIS KGDGVSTFEF IGSGVVAALL NYFSCGYFSK
EKISELNLPK LRQEGLRRFK AFLEVALPFD GNEGKVPPMT VLIQKLQNAL SSLERFPVVL
SHPSRSLSGS ARLSSGLSAL AHPLKLRLCR ASGEKTLRDY SSNIVLIDPL ASLAAVEEFL
WPRVQRSESA LKPAAPIGNT EPGTLPSGAG VSSPSSSTPA STTRRHSSRS RSAINIGDTS
KKDPVHEKGT SSSKGKGKGV MKPAQADKGP QTRSNAQKRA VLDKDTQMKP ASGDSSSEDE
ELEISPVDID DALVIEEDDI SDDEDDDNED VLDDSLPMCT PDKVHDVKLA DSVDDDGLAT
SGRQMNPASG GTSGAAAARA SDSIDTGIGN SYGSRGALSF AAAAMAGLGA ASGRGIRGSR
DLHGRTLNRS SDEPSKLIFT AAGKQLSRHL TIYQAVQRQL MLDEDDDDRF GGSDLVSSDG
SRFNDIYTIM YQRPDSQVNR LSVGGASSTT PSKSTKSATT NSSVESQSHR ASLLDSILQG
ELPCDLEKSN STYNVLALLR VLEGLNQLCP RLRAQTLSDR FAEGKITSLD DLSTTAAKVP
LDEFVNSKLT PKLARQIQDA LALCSGSLPS WCYQLTRACP FLFPFQTRRQ YFYSTAFGLS
RALNRLQQQQ GADGSGSTNE REMRIGRLQR QKVRVSRNRI LDSAAKVMEM YSSQKAVLEV
EYFGEVGTGL GPTLEFYTLL SHDLQKASLG MWRSSSGDKV SMQIGRDEIE DGKPSAANRD
IVLAPLGLFP RPWPSTADIS EGGQFHKVIE YFRLLGRVMA KALQDGRLLD VPLSTAFYKL
ILGQELDLHD IVLFDAELGK TLQELRVVVA RKHYLEGVGG DNSSTISDLC LRGCRIEDLS
LEFTLPGYPE YILRSGDEIV DITNLEEYIS LVVDATVKRG VTRQIEAFRS GFNQVFDITS
LQIFTPSELD YLLCGRRELW EVETLAEHIK FDHGYNAKSP AIINLLEIMG ELTADQQRAF
CQFVTGAPRL PPGGLAVLNP KLTIVRKHSS TSSAAANGAG ASETADDDLP SVMTCANYLK
LPPYSTKEIM YKKLLYAINE GQGSFDLS
