UPL5_ARATH
ID UPL5_ARATH Reviewed; 873 AA.
AC Q9SU29;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=E3 ubiquitin-protein ligase UPL5;
DE Short=Ubiquitin-protein ligase 5;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase UPL5;
GN Name=UPL5; OrderedLocusNames=At4g12570; ORFNames=T1P17.160;
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=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 [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;
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 [4]
RP FUNCTION, INTERACTION WITH WRKY53, SUBCELLULAR LOCATION, INDUCTION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-839.
RX PubMed=20409006; DOI=10.1111/j.1365-313x.2010.04233.x;
RA Miao Y., Zentgraf U.;
RT "A HECT E3 ubiquitin ligase negatively regulates Arabidopsis leaf
RT senescence through degradation of the transcription factor WRKY53.";
RL Plant J. 63:179-188(2010).
CC -!- FUNCTION: E3 ubiquitin protein ligase that regulates leaf senescence
CC through ubiquitination and subsequent degradation of WRKY53.
CC {ECO:0000269|PubMed:20409006}.
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 -!- SUBUNIT: Interacts with WRKY53. {ECO:0000269|PubMed:20409006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20409006}.
CC -!- INDUCTION: By jasmonate. Down-regulated by hydrogen peroxide.
CC {ECO:0000269|PubMed:20409006}.
CC -!- DISRUPTION PHENOTYPE: Accelerated senescence.
CC {ECO:0000269|PubMed:20409006}.
CC -!- SIMILARITY: Belongs to the UPL family. {ECO:0000305}.
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DR EMBL; AL049730; CAB41727.2; -; Genomic_DNA.
DR EMBL; AL161534; CAB78300.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83149.1; -; Genomic_DNA.
DR EMBL; AK229227; BAF01094.1; -; mRNA.
DR PIR; H85134; H85134.
DR PIR; T07649; T07649.
DR RefSeq; NP_192994.1; NM_117327.3.
DR AlphaFoldDB; Q9SU29; -.
DR SMR; Q9SU29; -.
DR STRING; 3702.AT4G12570.1; -.
DR PaxDb; Q9SU29; -.
DR PRIDE; Q9SU29; -.
DR ProteomicsDB; 234119; -.
DR EnsemblPlants; AT4G12570.1; AT4G12570.1; AT4G12570.
DR GeneID; 826870; -.
DR Gramene; AT4G12570.1; AT4G12570.1; AT4G12570.
DR KEGG; ath:AT4G12570; -.
DR Araport; AT4G12570; -.
DR TAIR; locus:2135630; AT4G12570.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_002173_8_1_1; -.
DR InParanoid; Q9SU29; -.
DR OMA; KEFILCA; -.
DR OrthoDB; 287399at2759; -.
DR PhylomeDB; Q9SU29; -.
DR BRENDA; 2.3.2.26; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SU29; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SU29; baseline and differential.
DR Genevisible; Q9SU29; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0010150; P:leaf senescence; 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:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR CDD; cd00078; HECTc; 1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lectin; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..873
FT /note="E3 ubiquitin-protein ligase UPL5"
FT /id="PRO_0000312023"
FT DOMAIN 95..171
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 272..296
FT /note="C-type lectin"
FT DOMAIN 532..873
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 839
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MUTAGEN 839
FT /note="C->S: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:20409006"
SQ SEQUENCE 873 AA; 100365 MW; 162A86F13CD7BB0F CRC64;
MTLSRSSADD STNNANRSYS AVAGTDNKRK RDEDSSDYVG VAESLEMLKK QEIDADHMAA
SAQQTLISWR SGENSRSLSS SGECSSSNRP ESTRLQIFVR MMSGGKTIVI HAEKYDTVEK
LHQRIEWKTK IPALEQRVIY KGKQLQRENS LTYYSIEQDA SLQLVARMQS TEHPVAWQTI
DDIMYTISRM YKGENLQSNI NEKIVTFFAM IPVESDESIA KYLNIFSNSS VPAALVMLYA
SSLERNKSCA KSSVKLFLSN CVALPKNQKN YCLPIVLEFC KLLRKVCPDQ KLYVTCRNTL
GSMLETFDNP HGVYNDQYET FGVEIFPFFT ELTGLLLNEL AQNSGPSFCD FQKVSSFWQQ
LRKVIELKVA FPIPIVLPMQ STALEAEIRH LHRLFGSLLT TMDLCMCRVE SSLADKEVGN
SETMSSSWSQ YLSILKIINS MSNIYQGAKG QLAVMLNKNK VSFSALVVKF AKRGDDHQWI
FEYKEATNFE ARRHLAMLLF PDVKEDFEEM HEMLIDRSNL LSESFEYIVG ASPEALHGGL
FMEFKNEEAT GPGVLREWFY LVCQEIFNPK NTLFLRSADD FRRFSPNPAS KVDPLHPDFF
EFTGRVIALA LMHKVQVGVL FDRVFFLQLA GLKISLEDIK DTDRIMYNSC KQILEMDPEF
FDSNAGLGLT FVLETEELGK RDTIELCPDG KLKAVNSKNR KQYVDLLIER RFATPILEQV
KQFSRGFTDM LSHSVPPRSF FKRLYLEDLD GMLRGGENPI SIDDWKAHTE YNGFKETDRQ
IDWFWKILKK MTEEEQRSIL FFWTSNKFVP VEGFRGLSSK LYIYRLYEAN DRLPLSHTCF
YRLCIPRYPT ITLMEQRLRL IAQDHVSSSF GKW
