UBE4_ARATH
ID UBE4_ARATH Reviewed; 1038 AA.
AC Q9LF41;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Probable ubiquitin conjugation factor E4;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:P54860, ECO:0000250|UniProtKB:Q9ES00};
DE AltName: Full=Plant U-box protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase E4;
DE AltName: Full=U-box domain-containing protein 1;
DE AltName: Full=Ubiquitin-fusion degradation protein 2-like;
DE Short=UB fusion protein 2-like;
GN Name=PUB1; Synonyms=UFD2; OrderedLocusNames=At5g15400; ORFNames=T20K14_10;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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).
CC -!- FUNCTION: Ubiquitin-protein ligase that may function as an E3 ligase in
CC conjunction with specific E1 and E2 ligases. May also function as an E4
CC ligase mediating the assembly of polyubiquitin chain assembly on
CC substrates monoubiquitinated by another E3 ubiquitin ligase.
CC {ECO:0000250|UniProtKB:P54860, ECO:0000250|UniProtKB:Q9ES00}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:P54860, ECO:0000250|UniProtKB:Q9ES00}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54860}. Nucleus
CC {ECO:0000250|UniProtKB:P54860}.
CC -!- DOMAIN: The U-box domain is required for the ubiquitin protein ligase
CC activity. {ECO:0000250|UniProtKB:P54860, ECO:0000250|UniProtKB:Q9ES00}.
CC -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX832575; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AL391143; CAC01739.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92156.1; -; Genomic_DNA.
DR EMBL; BX832575; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T51518; T51518.
DR RefSeq; NP_568313.2; NM_121544.4.
DR AlphaFoldDB; Q9LF41; -.
DR SMR; Q9LF41; -.
DR BioGRID; 16668; 10.
DR IntAct; Q9LF41; 1.
DR STRING; 3702.AT5G15400.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR PaxDb; Q9LF41; -.
DR PRIDE; Q9LF41; -.
DR ProteomicsDB; 228601; -.
DR EnsemblPlants; AT5G15400.1; AT5G15400.1; AT5G15400.
DR GeneID; 831392; -.
DR Gramene; AT5G15400.1; AT5G15400.1; AT5G15400.
DR KEGG; ath:AT5G15400; -.
DR Araport; AT5G15400; -.
DR TAIR; locus:2180862; AT5G15400.
DR eggNOG; KOG2042; Eukaryota.
DR HOGENOM; CLU_003224_2_1_1; -.
DR InParanoid; Q9LF41; -.
DR OMA; LRWELHS; -.
DR OrthoDB; 194967at2759; -.
DR PhylomeDB; Q9LF41; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LF41; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LF41; baseline and differential.
DR Genevisible; Q9LF41; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IGI:TAIR.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IGI:TAIR.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IGI:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR InterPro; IPR045132; UBE4.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13931; PTHR13931; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF10408; Ufd2P_core; 1.
DR SMART; SM00504; Ubox; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..1038
FT /note="Probable ubiquitin conjugation factor E4"
FT /id="PRO_0000322135"
FT DOMAIN 940..1014
FT /note="U-box"
FT REGION 430..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 117528 MW; 8F6FA8FF1D9CC4DA CRC64;
MATSKPQRSP AEIEDIILRK IFYVTLTEST DSDPRIVYLE MTAAEILSEG KELLLSRDLM
ERVLIDRLSG DFSDAEPPFP YLIGCHRRAY DESKKIQSMK DKNLRSEMEI VTKQAKKLAV
SYCRIHLGNP DMFGNSDKPS GGLDNRLKKR NVSPVLPLIF AEVGSGSLDM FGASSSGVQA
PPGFLDEFFK DSDFDSLDSI LKELYEDLRS TVINVSVLGD FQPPLRALKY LVSLPVGAKS
LVSHEWWVPR GAYMNGRAME LTSILGPFFH ISALPDNTLF KSQPDVGQQC FSEASERRPA
DLLSSFSTIK NFMNILYSGL HDVLMILLKS TDTRERVLQF LAEVINANAS RAHIQVDPVS
CASSGMFVNL SAVMLRLCEP FLDPHLTKRD KIDPKYAFCG HRLKLSDLTA LHASSEEVTE
WIGKDAMANA NDAGRENGNE SRLLQSKEAT SSSSNASGQN AKSATKYTFI CECFFMTARV
LNLGLLKALS DFKHLAQDIS RGEDNLATLK AMRDQAPSPQ LELDISRMEK ELELSSQEKL
CHEAQILRDG DFIQRALSFY RLMVVWLVGL VGGFKMPLPS TCPMEFSCMP EHFVEDAMEL
LIFASRIPKA LDGVPLDDFM NFIIMFMASP EYVRNPYLRA KMVEVLNCWM PRSSSSSSAT
STLFEGHQLS LEYLVRNLLK LYVDIEFTGS HTQFYDKFNI RHNIAELLEY LWQVPSHRNA
WRRIAKDEEK GVYLNFLNFL VNDSIYLLDE SLNKILEIKQ IEADMSNTAE WEQRPTQERQ
ERTRLFHSQE NIVRIDMKLA NEDVTMLAFT SEEITAPFLL PEMVERVANM LNYFLLQLVG
PQRKSLSLKD PEKYEFRPKQ LLKQIVRIYV NLARGDTVNI FPGAISSDGR SYNEQLFNAG
ADVLRRIGEE GRIIQEFMEL GTKAKAAASE ALDAEAALGE IPDEFLDPIQ YTLMRDPVIL
PSSRITVDRP IIQRHLLSDN HDPFNRAHLT SDMLIPDIEL KAKIDEFVKS HQSKKRTSGE
DSSNKERIQT TNSDMLID
