ATL38_ARATH
ID ATL38_ARATH Reviewed; 302 AA.
AC O64762; Q4PSR9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=RING-H2 finger protein ATL38;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL38 {ECO:0000305};
GN Name=ATL38; OrderedLocusNames=At2g34990; ORFNames=F19I3.22;
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 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; AC004238; AAC12838.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09046.1; -; Genomic_DNA.
DR EMBL; DQ056567; AAY78717.1; -; mRNA.
DR PIR; T00480; T00480.
DR RefSeq; NP_181044.1; NM_129051.2.
DR AlphaFoldDB; O64762; -.
DR SMR; O64762; -.
DR STRING; 3702.AT2G34990.1; -.
DR PaxDb; O64762; -.
DR PRIDE; O64762; -.
DR EnsemblPlants; AT2G34990.1; AT2G34990.1; AT2G34990.
DR GeneID; 818063; -.
DR Gramene; AT2G34990.1; AT2G34990.1; AT2G34990.
DR KEGG; ath:AT2G34990; -.
DR Araport; AT2G34990; -.
DR TAIR; locus:2044742; AT2G34990.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_035191_1_0_1; -.
DR InParanoid; O64762; -.
DR PhylomeDB; O64762; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O64762; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64762; baseline and differential.
DR Genevisible; O64762; 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 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..302
FT /note="RING-H2 finger protein ATL38"
FT /id="PRO_0000055779"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 96..138
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 279..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 34171 MW; AE4F64FF0C252A2C CRC64;
MVQPGTEIKA SDLTLLVITI ILFAIFIVGL ASVCFRWTSR QFYSQESINP FTDSDVESRT
SITAVRGLDE AIINSFPTFL YSEVKERRIG IGGVECAVCI CEFEDHETLR LMPECCHVFH
ADCVSVWLSD HSTCPLCRVD LCLQPGERSY LNPEPDLVES TNSHLFDGVT WTNRNRPSRS
WSTRLSQCRV SQILISRSHS TGHSVVQPLD NLDRFTLRLP EEVRRQLTKK TVDNVAFSQA
RSSRRGYRSR SAGSERSVFS YQRRMHSFSD CAWSTSCGGE AVAPSKDSRR ISVEQSQLDD
RV