ID   ATL63_ARATH             Reviewed;         308 AA.
AC   Q9LUZ9; Q4PSB0;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=RING-H2 finger protein ATL63;
DE            EC=2.3.2.27 {ECO:0000305};
DE   AltName: Full=Protein ARABIDOPSIS TOXICOS EN LEVADURA 63;
DE            Short=Protein ATL63;
DE   AltName: Full=RING-type E3 ubiquitin transferase ATL63 {ECO:0000305};
GN   Name=ATL63; OrderedLocusNames=At5g58580; ORFNames=MZN1.3;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
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   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   [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; AB020755; BAA97327.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97072.1; -; Genomic_DNA.
DR   EMBL; DQ056726; AAY78870.1; -; mRNA.
DR   RefSeq; NP_200666.1; NM_125245.2.
DR   AlphaFoldDB; Q9LUZ9; -.
DR   SMR; Q9LUZ9; -.
DR   BioGRID; 21216; 5.
DR   STRING; 3702.AT5G58580.1; -.
DR   PaxDb; Q9LUZ9; -.
DR   PRIDE; Q9LUZ9; -.
DR   ProteomicsDB; 246765; -.
DR   EnsemblPlants; AT5G58580.1; AT5G58580.1; AT5G58580.
DR   GeneID; 835972; -.
DR   Gramene; AT5G58580.1; AT5G58580.1; AT5G58580.
DR   KEGG; ath:AT5G58580; -.
DR   Araport; AT5G58580; -.
DR   TAIR; locus:2178788; AT5G58580.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_066543_2_0_1; -.
DR   InParanoid; Q9LUZ9; -.
DR   OMA; KLRNCGH; -.
DR   OrthoDB; 1220350at2759; -.
DR   PhylomeDB; Q9LUZ9; -.
DR   BRENDA; 2.3.2.27; 399.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9LUZ9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LUZ9; baseline and differential.
DR   Genevisible; Q9LUZ9; AT.
DR   GO; GO:0005769; C:early endosome; IDA:TAIR.
DR   GO; GO:0005768; C:endosome; IDA:TAIR.
DR   GO; GO:0005798; C:Golgi-associated vesicle; IDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:TAIR.
DR   GO; GO:0071470; P:cellular response to osmotic stress; IMP:TAIR.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0030100; P:regulation of endocytosis; IMP:TAIR.
DR   GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; IMP:TAIR.
DR   GO; GO:1901000; P:regulation of response to salt stress; IMP:TAIR.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 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..308
FT                   /note="RING-H2 finger protein ATL63"
FT                   /id="PRO_0000055817"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         138..180
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          252..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   308 AA;  34295 MW;  4EFAA482C4282609 CRC64;
     MSEEDGGSMS VKSSLSSFLK ILSSYNSNVL LAALVFLLLV VLFVLLLHFY ARFFWSPSHQ
     DFSAAARHRR RRRRNRRRTV TTTRIIPSLP LGGFDDGVSS PAATATRDDK GLDSSVISSI
     PLFVYEENEE EEDEEEECVI CLGLWEAGDF GRKLRNCGHG FHVECIDMWL SSHSTCPLCR
     SPVLAAVSDE ENLKLAVNAV EEEAEVRLQM SPAGENESNV SGDRRVSLSL SVMEDDLKTG
     DDDGEEEVRI EVFDDDEEIN DGGTRSDRRR SMSMTSSASS SLMRMLSSSS SRSERNKVFP
     TARQDSSK