UPL4_ARATH
ID UPL4_ARATH Reviewed; 1502 AA.
AC Q9LYZ7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=E3 ubiquitin-protein ligase UPL4;
DE Short=Ubiquitin-protein ligase 4;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase UPL4;
GN Name=UPL4; Synonyms=KLI5; OrderedLocusNames=At5g02880; ORFNames=F9G14_190;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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).
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. K-HECT subfamily. {ECO:0000305}.
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DR EMBL; AL162973; CAB86042.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90531.1; -; Genomic_DNA.
DR PIR; T48309; T48309.
DR RefSeq; NP_195908.1; NM_120366.4.
DR AlphaFoldDB; Q9LYZ7; -.
DR SMR; Q9LYZ7; -.
DR STRING; 3702.AT5G02880.1; -.
DR iPTMnet; Q9LYZ7; -.
DR PaxDb; Q9LYZ7; -.
DR PRIDE; Q9LYZ7; -.
DR ProteomicsDB; 233004; -.
DR EnsemblPlants; AT5G02880.1; AT5G02880.1; AT5G02880.
DR GeneID; 831758; -.
DR Gramene; AT5G02880.1; AT5G02880.1; AT5G02880.
DR KEGG; ath:AT5G02880; -.
DR Araport; AT5G02880; -.
DR TAIR; locus:2151306; AT5G02880.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR HOGENOM; CLU_000366_1_0_1; -.
DR InParanoid; Q9LYZ7; -.
DR OMA; FFTIHAQ; -.
DR OrthoDB; 34110at2759; -.
DR PhylomeDB; Q9LYZ7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LYZ7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYZ7; baseline and differential.
DR Genevisible; Q9LYZ7; AT.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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 CDD; cd00078; HECTc; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
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; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway.
FT CHAIN 1..1502
FT /note="E3 ubiquitin-protein ligase UPL4"
FT /id="PRO_0000312022"
FT REPEAT 143..183
FT /note="ARM 1"
FT REPEAT 186..226
FT /note="ARM 2"
FT REPEAT 228..265
FT /note="ARM 3"
FT REPEAT 267..306
FT /note="ARM 4"
FT DOMAIN 1128..1502
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1096
FT /note="K-box"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1469
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1502 AA; 167292 MW; E5ED26801EB972D4 CRC64;
MENRGQKRME VVEELPADKR ACNSQDFRPS TSGSSVQAQA NDTNPGHENV DADMDTSSSA
SPSSRSDEEE QEEQDKEDSD YGSCDSDEED PRQRVLQDYQ RQRSSGDHGK LKSLLLNLTG
ETDPSGQLSR LTELCEVLSF STEESLSSVM ANMLSPVLVK LAKHENNADI MLLAIRAITY
LCDVYPPSVE FLVRHDTIPA LCQRLLTIEY LDVAEQCLQA LEKISRDEPV ACLNAGAIMA
VLSFIDFFST SIQRVAISTV VNICKQLSSE SPSPFMDAVP ILCTLLQYED RQLVENVAIC
LTKIADQASE SPAMLDQLCR HGLINESTHL LNLNSRTTLS QPVYNGVIGM LRKLSSGSAL
AFRTLYELNI GYSLKEIMST YDISHSVSST HPINACSNQV HEVLKLVIEL LPASPVEDNQ
LASEKESFLV NQPDLLQQFG RDMLPVMIQV LNSGANVYVS YGCLSAIHKL TCLSKSGDIV
ELLKNTNMSS VLAGILSRKD HHVIVVALQV AEVLLEKYRD TFLNSFIKEG VFFAIEALLS
SDRGQQNQGS ADLSQKPVTK EIVKCLCQSF ERSLSSSSQT CKIEKDSVYV LATRIKEGFF
GPEVFNSEKG LTDVLQNLKN LSVALSELMT VPIDAHVLHD EKFFSIWNQI MERLNGRESV
STFEFIESGV VKSLASYLSN GLYQRKLSKG GPECDSLPFI GKRFEVFTRL LWSDGEATSS
LLIQKLQNSL SSLENFPIVL SQFLKQKNSF AAIPNGRCTS YPCLKVRFLK AEGETSLRDY
SQDFVTVDPL CYLDAVDQYL WPKVNIEPID SVEAKDQAIE CQSSQLQSTS ISCQAESSSP
MEIDSESSDA SQLQGSQVED QTQLPGQQNA SSSETSSEKE DAVPRLLFRL EGLELDRSLT
VYQAILLHKL KSESEATNDS KLSGPHNITY ERSAQLGDSR ENLFPPGSME DDEYRPFLSY
LFTHRLALRL KGSSHPPYDI LFLLKSLEGM NRFLFHLISL ERINAFGEGR LENLDDLRVQ
VRPVPHSEFV SSKLTEKLEQ QLRDSFAVST CGLPPWFNDL MDSCPCLFSF EAKSKYFRLA
AFGSQKIRHH PQHLSSSNVH GEARPVTGSL PRKKFLACRE NILESAAKMM ELYGNQKVVI
EVEYSEEVGT GLGPTLEFYT LVSRAFQNPD LGMWRNDCSF IVGKPVEHSG VLASSSGLFP
RPWSGTSTTS DVLQKFVLLG TVVAKALQDG RVLDLPLSKA FYKLILGQEL SSFDIHFVDP
ELCKTLVELQ ALVRRKKLFA EAHGDSGAAK CDLSFHGTKI EDLCLEFALP GYTDYDLAPY
SANDMVNLDN LEEYIKGIVN ATVCNGIQKQ VEAFRSGFNQ VFSIEHLRIF NEEELETMLC
GECDLFSMNE VLDHIKFDHG YTSSSPPVEY LLQILHEFDR EQQRAFLQFV TGSPRLPHGG
LASLSPKLTI VRKHGSDSSD TDLPSVMTCA NYLKLPPYSS KEKMKEKLIY AITEGQGSFH
LS
