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ARI15_ARATH
ID   ARI15_ARATH             Reviewed;         452 AA.
AC   Q84RQ8; Q9FFN8;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase ARI15;
DE            EC=2.3.2.31 {ECO:0000250|UniProtKB:Q9Y4X5};
DE   AltName: Full=ARIADNE-like protein ARI15;
DE   AltName: Full=Protein ariadne homolog 15;
DE   AltName: Full=RING-type E3 ubiquitin transferase ARI15 {ECO:0000305};
GN   Name=ARI15; OrderedLocusNames=At5g63760; ORFNames=MBK5.24;
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], TISSUE SPECIFICITY, NOMENCLATURE, AND
RP   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=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
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;
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12529512}.
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}.
CC   -!- CAUTION: Lacks two Cys residues in the RING-type zinc finger domain 2
CC       that are conserved features of the family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB10469.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ510218; CAD52897.1; -; Genomic_DNA.
DR   EMBL; AB005234; BAB10469.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED97793.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97794.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70851.1; -; Genomic_DNA.
DR   EMBL; BT022004; AAY25416.1; -; mRNA.
DR   EMBL; BT029215; ABJ17150.1; -; mRNA.
DR   RefSeq; NP_001332429.1; NM_001345608.1.
DR   RefSeq; NP_201181.2; NM_125771.3.
DR   RefSeq; NP_974987.1; NM_203258.2.
DR   AlphaFoldDB; Q84RQ8; -.
DR   SMR; Q84RQ8; -.
DR   STRING; 3702.AT5G63760.2; -.
DR   PaxDb; Q84RQ8; -.
DR   PRIDE; Q84RQ8; -.
DR   ProteomicsDB; 245189; -.
DR   EnsemblPlants; AT5G63760.1; AT5G63760.1; AT5G63760.
DR   EnsemblPlants; AT5G63760.2; AT5G63760.2; AT5G63760.
DR   EnsemblPlants; AT5G63760.3; AT5G63760.3; AT5G63760.
DR   GeneID; 836496; -.
DR   Gramene; AT5G63760.1; AT5G63760.1; AT5G63760.
DR   Gramene; AT5G63760.2; AT5G63760.2; AT5G63760.
DR   Gramene; AT5G63760.3; AT5G63760.3; AT5G63760.
DR   KEGG; ath:AT5G63760; -.
DR   Araport; AT5G63760; -.
DR   TAIR; locus:2160584; AT5G63760.
DR   eggNOG; KOG1815; Eukaryota.
DR   HOGENOM; CLU_009823_3_2_1; -.
DR   InParanoid; Q84RQ8; -.
DR   OMA; QTVESHN; -.
DR   OrthoDB; 469819at2759; -.
DR   PhylomeDB; Q84RQ8; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q84RQ8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q84RQ8; baseline and differential.
DR   Genevisible; Q84RQ8; 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; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; PTHR11685; 1.
DR   Pfam; PF01485; IBR; 1.
DR   SMART; SM00647; IBR; 2.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 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..452
FT                   /note="Probable E3 ubiquitin-protein ligase ARI15"
FT                   /id="PRO_0000356208"
FT   ZN_FING         26..88
FT                   /note="RING-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ZN_FING         106..174
FT                   /note="IBR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ZN_FING         208..239
FT                   /note="RING-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ZN_FING         414..445
FT                   /note="RanBP2-type"
FT   REGION          22..256
FT                   /note="TRIAD supradomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         229
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
SQ   SEQUENCE   452 AA;  51767 MW;  D2F3A23CC5DDEA20 CRC64;
     MEKLMTESGL KPVVIDSNQD LSRVYCGICS NIGDDDYDGD AVVVDGDLIS TPFCSHKFCK
     ACWSKYLKKN FFSVEKNHTA ISCPDRDCRA AVGPETVEKL TVRDQAMYEL YILKSYREKY
     LGWKLKLCPA RGCNYVIEFH LASEDEEHSL NIVCLCGHIF CWRCMLESHR PVTCNNASDW
     LSRDLEKLIE EVDKPSTVSW IDANTKPCPH CFIPVEIDGE RPWAQFLTCV CSGRFCWKCF
     RSPETHGTSG SCLAPARSSN VGFNHWNRAK PGISCLDLWN ASQVNLVNAK YELEAFEESI
     IKKPSDLKEQ DVKVLREGLM LIVQCRQFLK WSCAYDYIHT EYDMAKREYL RFLQQNASGI
     VHSFSQSIKE ETEAKELTCG KLLSETTNIG NFFYHFIKTL REGLPEVQAE SYDNYGGPYW
     LCDRCTYGNS WFQRACKMCC DPTASKMDEL SD
 
 
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