UPL7_ARATH
ID UPL7_ARATH Reviewed; 1142 AA.
AC Q9SCQ2; Q0WUM3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=E3 ubiquitin-protein ligase UPL7;
DE Short=Ubiquitin-protein ligase 7;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase UPL7;
GN Name=UPL7; OrderedLocusNames=At3g53090; ORFNames=T4D2.20;
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;
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.
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase which mediates
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the UPL family. {ECO:0000305}.
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DR EMBL; AL132958; CAB64212.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79035.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79036.1; -; Genomic_DNA.
DR EMBL; AK227125; BAE99175.1; -; mRNA.
DR PIR; T46155; T46155.
DR RefSeq; NP_001030850.1; NM_001035773.2.
DR RefSeq; NP_190877.1; NM_115169.3.
DR AlphaFoldDB; Q9SCQ2; -.
DR SMR; Q9SCQ2; -.
DR STRING; 3702.AT3G53090.1; -.
DR PaxDb; Q9SCQ2; -.
DR PRIDE; Q9SCQ2; -.
DR ProteomicsDB; 245282; -.
DR EnsemblPlants; AT3G53090.1; AT3G53090.1; AT3G53090.
DR EnsemblPlants; AT3G53090.2; AT3G53090.2; AT3G53090.
DR GeneID; 824475; -.
DR Gramene; AT3G53090.1; AT3G53090.1; AT3G53090.
DR Gramene; AT3G53090.2; AT3G53090.2; AT3G53090.
DR KEGG; ath:AT3G53090; -.
DR Araport; AT3G53090; -.
DR TAIR; locus:2101973; AT3G53090.
DR eggNOG; KOG4427; Eukaryota.
DR HOGENOM; CLU_002173_2_6_1; -.
DR InParanoid; Q9SCQ2; -.
DR OMA; LCKRLPP; -.
DR OrthoDB; 1163565at2759; -.
DR PhylomeDB; Q9SCQ2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SCQ2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCQ2; baseline and differential.
DR Genevisible; Q9SCQ2; AT.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd00078; HECTc; 1.
DR InterPro; IPR044611; E3B/C.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR PANTHER; PTHR45700; PTHR45700; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50096; IQ; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..1142
FT /note="E3 ubiquitin-protein ligase UPL7"
FT /id="PRO_0000312025"
FT DOMAIN 41..70
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 794..1142
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 567..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1110
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT CONFLICT 756
FT /note="D -> N (in Ref. 3; BAE99175)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1142 AA; 128486 MW; A4A642A48709D1E1 CRC64;
MDLNRKHKVS LRGASSGEIS RDALLAKVSQ ERELRSYARR ANAASLFIQR VWRSYIVRKK
AAIEIQEEWE NLLSCHSVTL TKSWVSSRVL RPFLFFVRSL SVQHQKIQAR EIHCMQTCFK
ILLESINSND QGYNFCSLAV GTSEDSKTWA CQTRRMVSLC SFLLTECNYS QERIKDVIGV
NALLLRILIV LTDPKSWKII TNENFEDAET AKKIIIQFIG SCKSGYYSAV RRYIKTLTKH
TDERLVITTS AVTLALRPFH VKQPAFVDDN QPDTNLAVEE YVSLILTIPR LVCYLPSALI
RALKHKSILM PSFHTILLLK DKILNIISEM ENSEKQSCTM EIPSVGWVIG NIISLATVSE
TDFMDPQESN PEMFYVLYVH VIVTLAENLL SQVESVGIQD IHLDIEATSN ETEKGNSVKI
SFVEMLRPVC QQWHLAKLLA ASGKEIRVIA DKDASTSSKK GSETLGLLDI ARLYSCMLRI
FCVMNPVLGP LPVLNMLSFC PGYIVSLWNS LESVLLPENG CTADDASHGS AKTSWNTRSP
SEKKLKHLKN DSVNKWVNVL NKFSGKSPGP REHVECTSDQ PGSGQVNEST NDVWDVETLR
GGPVGISKEV SCLLHLFCAT YAHLLVVLDD IQFYEKQVPF MLEKQQRIAS MLNTLVYYGL
LRGTGPESRQ LMDSAIRCLH LLYERDCRHP FCASALWLSP GRTSRPPIAF AARTHEVLPT
SDVLTTPSMG SVITITPHVF PFEERVHVFR EFISKDKASR KMAGEVDAPG ARSIEIVVRR
GHVVEDGFQQ LNSIGSRLKS SIHVSFVNES GLPEAGLDYG GLSKEFLTDI TKAAFATEYG
LFSQTPTSDR LLVPSPSARH LENGIQMIEF LGRIVGKALY EGILLDYSFS HVFIQKLLGR
YSFIDELSGL DPELYRNLMY VKHYDGDLKE LCLDFTVTEE FCGKMSIIEL KPGGKDTSVT
NENKMQYIHA MADYKLNRQI VPFSNAFYRG LTDLISPAWL KLFNAHEFNQ LLSGGNHDID
VDDLRRNTKY TGGYSDSSRT IKIFWEVMKG FEPSERCLLL KFVTSCSRAP LLGFKYLQPT
FIIHKVSCDT SLWAAIGGQD VERLPSASTC YNTLKLPTYK RASTMREKLL YAITSNAGFE
LS
