ID   ATL66_ARATH             Reviewed;         158 AA.
AC   Q9SRM0; B2GVN5;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=RING-H2 finger protein ATL66;
DE            EC=2.3.2.27 {ECO:0000305};
DE   AltName: Full=RING-type E3 ubiquitin transferase ATL66 {ECO:0000305};
GN   Name=ATL66; OrderedLocusNames=At3g11110; ORFNames=F11B9.7, F9F8.8;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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   De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (APR-2008) 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; AC009991; AAF01530.1; -; Genomic_DNA.
DR   EMBL; AC073395; AAG50960.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75003.1; -; Genomic_DNA.
DR   EMBL; BT031381; ACB88837.1; -; mRNA.
DR   RefSeq; NP_187722.1; NM_111948.2.
DR   AlphaFoldDB; Q9SRM0; -.
DR   SMR; Q9SRM0; -.
DR   BioGRID; 5616; 1.
DR   IntAct; Q9SRM0; 1.
DR   iPTMnet; Q9SRM0; -.
DR   PaxDb; Q9SRM0; -.
DR   PRIDE; Q9SRM0; -.
DR   EnsemblPlants; AT3G11110.1; AT3G11110.1; AT3G11110.
DR   GeneID; 820282; -.
DR   Gramene; AT3G11110.1; AT3G11110.1; AT3G11110.
DR   KEGG; ath:AT3G11110; -.
DR   Araport; AT3G11110; -.
DR   TAIR; locus:2074678; AT3G11110.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_013137_15_7_1; -.
DR   InParanoid; Q9SRM0; -.
DR   OMA; VCFVAVC; -.
DR   OrthoDB; 1509547at2759; -.
DR   PhylomeDB; Q9SRM0; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9SRM0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SRM0; baseline and differential.
DR   Genevisible; Q9SRM0; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR044675; RING1-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45676; PTHR45676; 1.
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..158
FT                   /note="RING-H2 finger protein ATL66"
FT                   /id="PRO_0000055789"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         107..149
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   158 AA;  18090 MW;  93F440CCBB10F4F7 CRC64;
     MTSSSPSPQA SMLLYWHENQ YDDRNFQIHG RTLFFALALF SVVLFFALLT LYIHRNCLPR
     DSINLHASSP DRLTRCRSGG LDPAEIRSLP VVLCRRERAE EEEEKECCIC LGGFEEGEKM
     KVLPPCSHCY HCECVDRWLK TESSCPLCRV SIRVDSSS