RIE1_ARATH
ID RIE1_ARATH Reviewed; 359 AA.
AC Q8GUU2;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=E3 ubiquitin protein ligase RIE1;
DE EC=2.3.2.27;
DE AltName: Full=Protein RING-FINGER FOR EMBRYOGENESIS 1;
DE AltName: Full=RING-type E3 ubiquitin transferase RIE1 {ECO:0000305};
GN Name=RIE1; OrderedLocusNames=At2g01735; ORFNames=T8O11;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=14756305; DOI=10.1023/b:plan.0000009256.01620.a6;
RA Xu R., Li Q.Q.;
RT "A RING-H2 zinc-finger protein gene RIE1 is essential for seed development
RT in Arabidopsis.";
RL Plant Mol. Biol. 53:37-50(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 required for embryo
CC development. {ECO:0000269|PubMed:14756305}.
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: Widely expressed. {ECO:0000269|PubMed:14756305}.
CC -!- DISRUPTION PHENOTYPE: Embryo-lethal phenotype. Embryo development
CC arrested between globular and torpedo stages.
CC {ECO:0000269|PubMed:14756305}.
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DR EMBL; AY168924; AAN87884.1; -; mRNA.
DR EMBL; AC006069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC05490.1; -; Genomic_DNA.
DR RefSeq; NP_849924.1; NM_179593.4.
DR AlphaFoldDB; Q8GUU2; -.
DR SMR; Q8GUU2; -.
DR STRING; 3702.AT2G01735.1; -.
DR PaxDb; Q8GUU2; -.
DR PRIDE; Q8GUU2; -.
DR EnsemblPlants; AT2G01735.1; AT2G01735.1; AT2G01735.
DR GeneID; 814703; -.
DR Gramene; AT2G01735.1; AT2G01735.1; AT2G01735.
DR KEGG; ath:AT2G01735; -.
DR Araport; AT2G01735; -.
DR TAIR; locus:1005452975; AT2G01735.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_038211_0_1_1; -.
DR InParanoid; Q8GUU2; -.
DR OMA; PTVARDQ; -.
DR OrthoDB; 789313at2759; -.
DR PhylomeDB; Q8GUU2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8GUU2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GUU2; baseline and differential.
DR Genevisible; Q8GUU2; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..359
FT /note="E3 ubiquitin protein ligase RIE1"
FT /id="PRO_0000397041"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 307..348
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 359 AA; 40098 MW; E8BE79378E11DC8F CRC64;
MSSYSSDSTA ARDQHAPLLR PRHDGSFSSS SSSARPTALA VLLGRITGHR APSMLVRETA
ARALEERRID WGYSKPVVAA DILWNAALVL ASAVMLVGTV EERPNEPIRV WICVYGLQCL
FHVVLVWSEY WRRNSTRRAR DLESYDHEDY NIEYDYEQDS DDNSTTYSFV KRCESINTVI
SFIWWIIGFY WVVEGGDKLL GEAPNLYWLS VIFLAIDVFF AVFCVVLACL VGIALCCCLP
CIIALLYAVA GTEGVSEAEL GVLPLYKFKA FHSNEKNITG PGKMVPIPIN GLCLATERTL
LAEDADCCIC LSSYEDGAEL HALPCNHHFH STCIVKWLKM RATCPLCKYN ILKGTTDQS
