ID ATL46_ARATH Reviewed; 376 AA.
AC Q9FL07;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=RING-H2 finger protein ATL46;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL46 {ECO:0000305};
GN Name=ATL46; OrderedLocusNames=At5g40250; ORFNames=MSN9.150, MSN9.16;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY ORGANIZATION.
RX PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
RA Kosarev P., Mayer K.F.X., Hardtke C.S.;
RT "Evaluation and classification of RING-finger domains encoded by the
RT Arabidopsis genome.";
RL Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
RN [5]
RP NOMENCLATURE, AND GENE FAMILY ORGANIZATION.
RX PubMed=16557337; DOI=10.1007/s00239-005-0038-y;
RA Serrano M., Parra S., Alcaraz L.D., Guzman P.;
RT "The ATL gene family from Arabidopsis thaliana and Oryza sativa comprises a
RT large number of putative ubiquitin ligases of the RING-H2 type.";
RL J. Mol. Evol. 62:434-445(2006).
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; Evidence={ECO:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily.
CC {ECO:0000305}.
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DR EMBL; AB010699; BAB10906.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94525.1; -; Genomic_DNA.
DR EMBL; AK176313; BAD44076.1; -; mRNA.
DR RefSeq; NP_198841.1; NM_123389.4.
DR AlphaFoldDB; Q9FL07; -.
DR SMR; Q9FL07; -.
DR STRING; 3702.Q9FL07; -.
DR iPTMnet; Q9FL07; -.
DR PaxDb; 3702-AT5G40250-1; -.
DR ProteomicsDB; 246762; -.
DR EnsemblPlants; AT5G40250.1; AT5G40250.1; AT5G40250.
DR GeneID; 834023; -.
DR Gramene; AT5G40250.1; AT5G40250.1; AT5G40250.
DR KEGG; ath:AT5G40250; -.
DR Araport; AT5G40250; -.
DR TAIR; AT5G40250; ATL46.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_034332_1_0_1; -.
DR InParanoid; Q9FL07; -.
DR OMA; HLKMAWV; -.
DR OrthoDB; 400239at2759; -.
DR PhylomeDB; Q9FL07; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FL07; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FL07; baseline and differential.
DR Genevisible; Q9FL07; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16461; RING-H2_EL5-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45768; E3 UBIQUITIN-PROTEIN LIGASE RNF13-LIKE; 1.
DR PANTHER; PTHR45768:SF18; RING-H2 FINGER PROTEIN ATL18-RELATED; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 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..376
FT /note="RING-H2 finger protein ATL46"
FT /id="PRO_0000055812"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 143..185
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 296..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 376 AA; 41792 MW; 3B97283D610FDDC8 CRC64;
MSWVRFTIEQ KDGNFAYPPP FYKDPILSPP SPPPPSSGNR ISPAVLFVIV ILAVLFFISG
LLHLLVRFLI KHPSATASSR SNRFPEISTS DALQRQLQQL FHLNDSGLDQ AFIDALPVFH
YKEIVGSAGG GGGNGAAQEP FDCAVCLCEF SEKDKLRLLP MCSHAFHLNC IDTWLQSNST
CPLCRGTLFS PGFSMENPMF DFDDIREDEE GVTENGSQKT MEIQEIVVEK GVLPVRLGKF
KRLDNVGNGQ GQDVVAGGET SSSNLDARRC FSMGSYQYIL GNSELKVPFA NDRLPRLKPQ
DKESEQTGNS SSEDNKKINT VAKGESFSVS KIWLWPKKDK FSSDAQRRLP SSSLNVDDLP
KLPWMEEHKK LENDGR
//
