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ATL12_ARATH
ID   ATL12_ARATH             Reviewed;         390 AA.
AC   Q9SL78;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Putative RING-H2 finger protein ATL12;
DE            EC=2.3.2.27 {ECO:0000305};
DE   AltName: Full=RING-type E3 ubiquitin transferase ATL12 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ATL12; OrderedLocusNames=At2g20030; ORFNames=T2G17.17;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   IDENTIFICATION.
RX   PubMed=15238540; DOI=10.1534/genetics.104.028043;
RA   Serrano M., Guzman P.;
RT   "Isolation and gene expression analysis of Arabidopsis thaliana mutants
RT   with constitutive expression of ATL2, an early elicitor-response RING-H2
RT   zinc-finger gene.";
RL   Genetics 167:919-929(2004).
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; AC006081; AAD24393.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06957.1; -; Genomic_DNA.
DR   PIR; B84584; B84584.
DR   RefSeq; NP_179593.1; NM_127561.2.
DR   AlphaFoldDB; Q9SL78; -.
DR   SMR; Q9SL78; -.
DR   BioGRID; 1877; 1.
DR   STRING; 3702.AT2G20030.1; -.
DR   PaxDb; Q9SL78; -.
DR   PRIDE; Q9SL78; -.
DR   ProteomicsDB; 246551; -.
DR   EnsemblPlants; AT2G20030.1; AT2G20030.1; AT2G20030.
DR   GeneID; 816522; -.
DR   Gramene; AT2G20030.1; AT2G20030.1; AT2G20030.
DR   KEGG; ath:AT2G20030; -.
DR   Araport; AT2G20030; -.
DR   TAIR; locus:2061698; AT2G20030.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_046350_0_0_1; -.
DR   InParanoid; Q9SL78; -.
DR   OMA; MEMKRML; -.
DR   OrthoDB; 957971at2759; -.
DR   PhylomeDB; Q9SL78; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9SL78; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SL78; baseline and differential.
DR   Genevisible; Q9SL78; 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; 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   3: Inferred from homology;
KW   Membrane; Metal-binding; Reference proteome; Signal; Transferase;
KW   Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..390
FT                   /note="Putative RING-H2 finger protein ATL12"
FT                   /id="PRO_0000030705"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         124..166
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   390 AA;  45014 MW;  90A67B8D7BCD121F CRC64;
     MNSPQEISIL FFFIIFLDYV SAQSPPPPNL YATSDLFKPS LAIITGVFSI VFTLTFVLLV
     YAKCFHNDLR SETDSDGERI RHDRLWQGLF NRSSRFSGLD KKAIESLPFF RFSALKGLKQ
     GLECSVCLSK FEDVEILRLL PKCRHAFHIG CIDQWLEQHA TCPLCRNRVN IEDDLSVLGN
     SSTSLRILNQ SETREEDSRL EIYIEREEGT NDGSSRFSSF RKILKKSLLL EREGNENIDE
     KKLMHKFNHR IVVSDAVFKN RWSNITSSDL TFLTSEMLNS VSSDRFSSVD RVHRGNLRDK
     EDMEMKRMLI KHKDSSRRTV SEITTVSREK AVGGSYRGST ASTSQNYAVT ATTEERRRRL
     WLPIARRTAQ WFVNREKSND LNTTRQNLNV
 
 
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