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 29-MAY-2013, entry version 71.
DE RecName: Full=Probable E3 ubiquitin-protein ligase ARI15;
DE EC=6.3.2.-;
DE AltName: Full=ARIADNE-like protein ARI15;
DE AltName: Full=Protein ariadne homolog 15;
GN Name=ARI15; OrderedLocusNames=At5g63760; ORFNames=MBK5.24;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, NOMENCLATURE,
RP 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=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
RT P1 clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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;
RA Marin I., Ferrus A.;
RT "Comparative genomics of the RBR family, including the Parkinson's
RT disease-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
CC of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-
CC conjugating enzymes and then transfers it to substrates (By
CC similarity).
CC -!- COFACTOR: Binds 4 zinc ions per subunit (Potential).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme (By similarity).
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC -!- SIMILARITY: Contains 1 IBR-type zinc finger.
CC -!- SIMILARITY: Contains 1 RanBP2-type zinc finger.
CC -!- SIMILARITY: Contains 2 RING-type zinc fingers.
CC -!- CAUTION: Lacks two Cys residues in the RING-type zinc finger
CC domain 2 that are conserved features of the family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10469.1; Type=Erroneous gene model prediction;
CC -!- WEB RESOURCE: Name=PlantsUBQ; Note=A functional genomics database
CC for the ubiquitin/26S proteasome proteolytic pathway in plants;
CC URL="http://plantsubq.genomics.purdue.edu/";
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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; BT022004; AAY25416.1; -; mRNA.
DR EMBL; BT029215; ABJ17150.1; -; mRNA.
DR IPI; IPI00538933; -.
DR RefSeq; NP_201181.2; NM_125771.3.
DR RefSeq; NP_974987.1; NM_203258.1.
DR UniGene; At.28980; -.
DR ProteinModelPortal; Q84RQ8; -.
DR SMR; Q84RQ8; 22-97.
DR STRING; 3702.AT5G63760.2-P; -.
DR EnsemblPlants; AT5G63760.1; AT5G63760.1; AT5G63760.
DR EnsemblPlants; AT5G63760.2; AT5G63760.2; AT5G63760.
DR GeneID; 836496; -.
DR KEGG; ath:AT5G63760; -.
DR TAIR; At5g63760; -.
DR eggNOG; NOG306332; -.
DR HOGENOM; HOG000034049; -.
DR InParanoid; Q84RQ8; -.
DR KO; K11968; -.
DR OMA; SETTNIG; -.
DR PhylomeDB; Q84RQ8; -.
DR ProtClustDB; CLSN2687579; -.
DR UniPathway; UPA00143; -.
DR Genevestigator; Q84RQ8; -.
DR GO; GO:0005622; C:intracellular; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR002867; Znf_C6HC.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01485; IBR; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; FALSE_NEG.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Ligase; Metal-binding; Reference proteome; Repeat;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 452 Probable E3 ubiquitin-protein ligase
FT ARI15.
FT /FTId=PRO_0000356208.
FT ZN_FING 26 88 RING-type 1; atypical.
FT ZN_FING 106 174 IBR-type.
FT ZN_FING 208 239 RING-type 2; degenerate.
FT ZN_FING 414 445 RanBP2-type.
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
//
