SIS3_ARATH
ID SIS3_ARATH Reviewed; 358 AA.
AC Q8GYT9; Q9SU62;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=E3 ubiquitin-protein ligase SIS3;
DE EC=2.3.2.27;
DE AltName: Full=Protein SUGAR INSENSITIVE 3;
DE AltName: Full=RING-type E3 ubiquitin transferase SIS3 {ECO:0000305};
DE Flags: Precursor;
GN Name=SIS3; OrderedLocusNames=At3g47990; ORFNames=T17F15.140;
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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20147494; DOI=10.1104/pp.109.150573;
RA Huang Y., Li C.Y., Pattison D.L., Gray W.M., Park S., Gibson S.I.;
RT "SUGAR-INSENSITIVE3, a RING E3 ligase, is a new player in plant sugar
RT response.";
RL Plant Physiol. 152:1889-1900(2010).
CC -!- FUNCTION: E3 ubiquitin protein ligase that acts as positive regulator
CC of sugar signaling during early seedling development. Possesses E3
CC ligase activity in vitro. {ECO:0000269|PubMed:20147494}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:20147494}.
CC -!- DISRUPTION PHENOTYPE: Resistance to high concentrations of exogenous
CC glucose and sucrose on early seedling development.
CC {ECO:0000269|PubMed:20147494}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41140.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049658; CAB41140.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78354.1; -; Genomic_DNA.
DR EMBL; AK117391; BAC42060.1; -; mRNA.
DR PIR; T06684; T06684.
DR RefSeq; NP_190382.2; NM_114668.3.
DR AlphaFoldDB; Q8GYT9; -.
DR SMR; Q8GYT9; -.
DR STRING; 3702.AT3G47990.1; -.
DR PaxDb; Q8GYT9; -.
DR PRIDE; Q8GYT9; -.
DR ProteomicsDB; 234550; -.
DR EnsemblPlants; AT3G47990.1; AT3G47990.1; AT3G47990.
DR GeneID; 823954; -.
DR Gramene; AT3G47990.1; AT3G47990.1; AT3G47990.
DR KEGG; ath:AT3G47990; -.
DR Araport; AT3G47990; -.
DR TAIR; locus:2097830; AT3G47990.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_041738_0_0_1; -.
DR InParanoid; Q8GYT9; -.
DR OMA; LVCIACM; -.
DR OrthoDB; 747114at2759; -.
DR PhylomeDB; Q8GYT9; -.
DR BRENDA; 2.3.2.27; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8GYT9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GYT9; baseline and differential.
DR Genevisible; Q8GYT9; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0010182; P:sugar mediated signaling pathway; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044793; SIS3.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47179; PTHR47179; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Membrane; Metal-binding; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..358
FT /note="E3 ubiquitin-protein ligase SIS3"
FT /id="PRO_0000395964"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 235..276
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 336..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 334
FT /note="T -> A (in Ref. 3; BAC42060)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 40686 MW; 79C9D7B545163C4C CRC64;
MAMRGVDFKW YDGFFLSMLA TSVIIVAVNW NRYRACEYPL HIWIVVDYTT VFIFRVFMFV
DNGLASGLGL DFGSQQRNAM FCGRVVVLSV LSLLLYPFLW AWTVIGTQWF TKSKTCLPEE
GQKWGFLIWL MFSYCGLLCI AFICVGKWLT RRQVHLLRAQ QGIPISEFGI LVDMIRVPDW
AFEAAGQEMR GISQDAATYH PGLYLTPAQT EAVEALIQEL PKFRLKAVPD DCGECLICLE
EFHIGHEVRG LPCAHNFHVE CIDQWLRLNV KCPRCRCSVF PDLDLSALSN LQSSGTEQHS
QVNTETSEAR YIRSQPQSES YFLRVQSLIH PVHTDTALET AENGGVPPVL TDLSPSRR
