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ARI10_ARATH
ID   ARI10_ARATH             Reviewed;         514 AA.
AC   Q9SKC4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase ARI10;
DE            EC=2.3.2.31 {ECO:0000250|UniProtKB:Q9Y4X5};
DE   AltName: Full=ARIADNE-like protein ARI10;
DE   AltName: Full=Protein ariadne homolog 10;
DE   AltName: Full=RING-type E3 ubiquitin transferase ARI10 {ECO:0000305};
GN   Name=ARI10; OrderedLocusNames=At2g31760; ORFNames=F20M17.20;
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 [GENOMIC DNA], NOMENCLATURE, AND GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=12529512; DOI=10.1104/pp.012781;
RA   Mladek C., Guger K., Hauser M.-T.;
RT   "Identification and characterization of the ARIADNE gene family in
RT   Arabidopsis. A group of putative E3 ligases.";
RL   Plant Physiol. 131:27-40(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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [5]
RP   FUNCTION.
RX   PubMed=12446796; DOI=10.1093/oxfordjournals.molbev.a004029;
RA   Marin I., Ferrus A.;
RT   "Comparative genomics of the RBR family, including the Parkinson's disease-
RT   related gene parkin and the genes of the ariadne subfamily.";
RL   Mol. Biol. Evol. 19:2039-2050(2002).
CC   -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC       complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC       enzymes and then transfers it to substrates. {ECO:0000250,
CC       ECO:0000269|PubMed:12446796}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:Q9Y4X5};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 4 Zn(2+) ions per subunit. {ECO:0000305};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC       interact with the E2 conjugating enzyme UBE2L3 and function like HECT-
CC       type E3 enzymes: they bind E2s via the first RING-type zinc finger, but
CC       require an obligate trans-thiolation step during the ubiquitin
CC       transfer, requiring a conserved active site Cys residue in the second
CC       RING-type zinc finger. The active site probably forms a thioester
CC       intermediate with ubiquitin taken from the active-site cysteine of the
CC       E2 before ultimately transferring it to a Lys residue on the substrate.
CC       {ECO:0000250|UniProtKB:Q9Y4X5}.
CC   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ510213; CAD52892.1; -; Genomic_DNA.
DR   EMBL; AC006533; AAD32296.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08581.1; -; Genomic_DNA.
DR   EMBL; DQ056560; AAY78710.1; -; mRNA.
DR   PIR; G84724; G84724.
DR   RefSeq; NP_180735.1; NM_128734.1.
DR   AlphaFoldDB; Q9SKC4; -.
DR   SMR; Q9SKC4; -.
DR   STRING; 3702.AT2G31760.1; -.
DR   PaxDb; Q9SKC4; -.
DR   PRIDE; Q9SKC4; -.
DR   EnsemblPlants; AT2G31760.1; AT2G31760.1; AT2G31760.
DR   GeneID; 817733; -.
DR   Gramene; AT2G31760.1; AT2G31760.1; AT2G31760.
DR   KEGG; ath:AT2G31760; -.
DR   Araport; AT2G31760; -.
DR   TAIR; locus:2045223; AT2G31760.
DR   eggNOG; KOG1815; Eukaryota.
DR   HOGENOM; CLU_009823_3_1_1; -.
DR   InParanoid; Q9SKC4; -.
DR   OMA; WICLRAY; -.
DR   OrthoDB; 469819at2759; -.
DR   PhylomeDB; Q9SKC4; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9SKC4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SKC4; baseline and differential.
DR   Genevisible; Q9SKC4; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; 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   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR045840; Ariadne.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; PTHR11685; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00647; IBR; 2.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Reference proteome; Repeat; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..514
FT                   /note="Probable E3 ubiquitin-protein ligase ARI10"
FT                   /id="PRO_0000356203"
FT   ZN_FING         121..171
FT                   /note="RING-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ZN_FING         190..251
FT                   /note="IBR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ZN_FING         278..308
FT                   /note="RING-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..322
FT                   /note="TRIAD supradomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ACT_SITE        291
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         124
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         233
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         251
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         278
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         281
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
SQ   SEQUENCE   514 AA;  59448 MW;  E49DA5F3D0E1F8CC CRC64;
     MDYSDDDMID NESGEENNSD GGGNESYNYN AAVDTIILSE KSYVIIKEEE ILKLQRDDIE
     RVSTILFLSQ VEAIVLLLHY HWCVSKLEDE WFTDEERIRK TVGILKEPVV DVNGTEVDIQ
     CGICFESYTR KEIASVSCGH PYCKTCWTGY ITTKIEDGPG CLRVKCPEPS CYAVVGQDMI
     DEVTEKKDKD KYYRYFLRSY VEDGKKMKWC PSPGCECAVE FGESSGYDVA CLCSYRFCWN
     CSEDAHSPVD CETVSKWIFK NQDESENKNW ILANSKPCPK CKRPIEKSHG CNHMTCSASC
     GHRFCWICGK SYSDHYACNN YVEDADHDKR TLLQSEIKRY THYYVRWVEN QSSRLKAMSD
     LEKFQSVQLK QLSDNQCKPK IDLQFIVDAW LQIIECRRVL KWTYAYGYYL DNLAKRPLFE
     YLQGEAETGL ERLHHCAENE LKQFFIKSED PSDTFNAFRM KLTGLTKVTK TYFDNLVKAL
     ENGLADVTKS SEESADFLET QKLYDAYISE GCFF
 
 
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