ID   ATL30_ARATH             Reviewed;         289 AA.
AC   Q9FIR0;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=RING-H2 finger protein ATL30;
DE            EC=2.3.2.27 {ECO:0000305};
DE   AltName: Full=RING-type E3 ubiquitin transferase ATL30 {ECO:0000305};
GN   Name=ATL30; OrderedLocusNames=At5g46650; ORFNames=MZA15.5;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(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   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   [4]
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; AB016882; BAB08909.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95410.1; -; Genomic_DNA.
DR   RefSeq; NP_199477.1; NM_124035.2.
DR   AlphaFoldDB; Q9FIR0; -.
DR   SMR; Q9FIR0; -.
DR   PaxDb; Q9FIR0; -.
DR   PRIDE; Q9FIR0; -.
DR   ProteomicsDB; 246752; -.
DR   EnsemblPlants; AT5G46650.1; AT5G46650.1; AT5G46650.
DR   GeneID; 834708; -.
DR   Gramene; AT5G46650.1; AT5G46650.1; AT5G46650.
DR   KEGG; ath:AT5G46650; -.
DR   Araport; AT5G46650; -.
DR   TAIR; locus:2178515; AT5G46650.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_035191_3_0_1; -.
DR   InParanoid; Q9FIR0; -.
DR   OMA; QENAHEN; -.
DR   OrthoDB; 986229at2759; -.
DR   PhylomeDB; Q9FIR0; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9FIR0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FIR0; baseline and differential.
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; IEA:UniProtKB-UniPathway.
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..289
FT                   /note="RING-H2 finger protein ATL30"
FT                   /id="PRO_0000055815"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         114..157
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          181..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   289 AA;  33432 MW;  B8528031CC637A10 CRC64;
     MPIAKPINQN TTVPYPPQHY SKPPLVIILT VILLVVFFIG FFAIYFCKCF YHTLTEAWNH
     HYHNGLPENQ IQAQQEPVQP PVNPGLEPHI IQSYPLFPFS SVKDLREDKY GLECAICLLE
     FEEEHILLRL LTTCYHVFHQ ECIDQWLESN KTCPVCRRNL DPNAPENIKE LIIEVIQENA
     HENRDQEQTS TSNEVMLSRQ SSGNNERKIE TLPDKFSRSK TTGHSIVRNK PEEEDRYTLR
     LPDHVKIKVT RRHNNNQTES CISFGELVRN REGRFGEVSG QSLVPESGS