ARI14_ARATH
ID ARI14_ARATH Reviewed; 506 AA.
AC Q9FFP1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable E3 ubiquitin-protein ligase ARI14 {ECO:0000303|PubMed:12529512};
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:Q9Y4X5};
DE AltName: Full=ARIADNE-like protein ARI14 {ECO:0000303|PubMed:12529512};
DE AltName: Full=Protein ariadne homolog 14 {ECO:0000303|PubMed:12529512};
DE AltName: Full=RING-type E3 ubiquitin transferase ARI14 {ECO:0000305};
GN Name=ARI14 {ECO:0000303|PubMed:12529512};
GN OrderedLocusNames=At5g63730 {ECO:0000312|Araport:AT5G63730};
GN ORFNames=MBK5.21 {ECO:0000312|EMBL:BAB10466.1};
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=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 Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) 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).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20478994; DOI=10.1101/gad.1882810;
RA Ron M., Alandete Saez M., Eshed Williams L., Fletcher J.C., McCormick S.;
RT "Proper regulation of a sperm-specific cis-nat-siRNA is essential for
RT double fertilization in Arabidopsis.";
RL Genes Dev. 24:1010-1021(2010).
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 (PubMed:12446796).
CC Regulates negatively male gametophyte formation and double
CC fertilization (PubMed:20478994). {ECO:0000269|PubMed:12446796,
CC ECO:0000269|PubMed:20478994}.
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: Mostly expressed in closed flowers and, to a lower
CC extent, in pollen. {ECO:0000269|PubMed:20478994}.
CC -!- DEVELOPMENTAL STAGE: During male gametophyte development, strongly
CC expressed in microspores and bicellular pollen, but decrease gradually
CC during pollen maturation in tricellular pollen to finally disappear in
CC mature pollen. {ECO:0000269|PubMed:20478994}.
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 -!- MISCELLANEOUS: Transcripts of KPL and ARI14, encoded by adjacent genes
CC organized in a reverse orientation, have the potential to generate
CC natural cis-antisense siRNAs (cis-nat-siRNAs) pair targeting ARI14 in
CC sperm, thus leading to opposite expression levels during male
CC gametophyte development. {ECO:0000269|PubMed:20478994}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks four Cys residues in the RING-type zinc finger domain 1
CC and two Cys residues in the RING-type zinc finger domain 2 that are
CC conserved features of the family. {ECO:0000305}.
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DR EMBL; AJ510217; CAD52896.1; -; Genomic_DNA.
DR EMBL; AB005234; BAB10466.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97790.1; -; Genomic_DNA.
DR EMBL; DQ056737; AAY78881.1; -; mRNA.
DR RefSeq; NP_201178.1; NM_125768.1.
DR AlphaFoldDB; Q9FFP1; -.
DR SMR; Q9FFP1; -.
DR STRING; 3702.AT5G63730.1; -.
DR PaxDb; Q9FFP1; -.
DR PRIDE; Q9FFP1; -.
DR EnsemblPlants; AT5G63730.1; AT5G63730.1; AT5G63730.
DR GeneID; 836493; -.
DR Gramene; AT5G63730.1; AT5G63730.1; AT5G63730.
DR KEGG; ath:AT5G63730; -.
DR Araport; AT5G63730; -.
DR TAIR; locus:2160664; AT5G63730.
DR eggNOG; KOG1815; Eukaryota.
DR HOGENOM; CLU_009823_3_2_1; -.
DR InParanoid; Q9FFP1; -.
DR OMA; WEDNECE; -.
DR OrthoDB; 469819at2759; -.
DR PhylomeDB; Q9FFP1; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FFP1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFP1; baseline and differential.
DR Genevisible; Q9FFP1; 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:0080155; P:regulation of double fertilization forming a zygote and endosperm; IMP:TAIR.
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; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; PTHR11685; 1.
DR Pfam; PF01485; IBR; 1.
DR SMART; SM00647; IBR; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Fertilization; Metal-binding; Reference proteome;
KW Repeat; Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..506
FT /note="Probable E3 ubiquitin-protein ligase ARI14"
FT /id="PRO_0000356207"
FT ZN_FING 83..140
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 158..227
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 258..287
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 462..492
FT /note="RanBP2-type"
FT REGION 79..308
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
SQ SEQUENCE 506 AA; 59010 MW; 7EB589A807E88496 CRC64;
MEYDGRRPYS VLTRNEITVK MKKQINEISD IFFISNSDAT VLLMYLRWDS LRVSERLGEN
KEKLLMDSGL KSVMIDPSPD SSSEISLETD VYEFDGDNDL ISMPFCSHKF DSKYWREYLE
KNFYYVEKIQ TTISCPDQDC RSAVGPDTIE KLTVRDQEMY ERYIWRSYIE GNKVLMIKQC
PARNCDYVIE FHQENDDDDE YSLNVVCICG HIFCWRCRLE SHRPVSCNKA SDWLCSATMK
ISDESFSLYP TKTKTVTCPH CLCSLESDTK MPQFLTCVCR LRFCSRCLRS EEAHKIEAVD
SGFCIKTEVG ILCEDRWNVC QKLLEQAKSD LEAFEETNIK KPSDLLREQD IMIIREGLML
IVQCRRVLKW CCVYDYFHTE YENSKEYLRY LQGNAIATLQ SYSNTLQEQK DIVLAAATYE
ECTFFRHTIP TATSNIGNYF YDFMKTLQDG LVDVKVKSYN GGTGPFWYCD RCTYANTWED
NECEMCYDDS ASLVGEISDL FLNKVS
