ATL42_ARATH
ID ATL42_ARATH Reviewed; 432 AA.
AC Q5XF85; Q4TU11; Q9SV57;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=E3 ubiquitin-protein ligase ATL42;
DE EC=2.3.2.27 {ECO:0000269|PubMed:15644464};
DE AltName: Full=RING-H2 finger protein ATL42;
DE AltName: Full=RING-type E3 ubiquitin transferase ATL42 {ECO:0000305};
DE Flags: Precursor;
GN Name=ATL42; OrderedLocusNames=At4g28890; ORFNames=F25O24.10;
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 [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-432.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-432.
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 -!- FUNCTION: E3 ubiquitin-protein ligase able to catalyze
CC polyubiquitination with ubiquitin-conjugating enzyme E2 UBC8 in vitro.
CC {ECO:0000269|PubMed:15644464}.
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:0000269|PubMed:15644464};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU84668.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAV43780.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ059125; AAY57611.1; -; mRNA.
DR EMBL; AL078469; CAB43903.1; -; Genomic_DNA.
DR EMBL; AL161573; CAB81477.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85559.1; -; Genomic_DNA.
DR EMBL; BX828195; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT015731; AAU84668.1; ALT_INIT; mRNA.
DR EMBL; BT020178; AAV43780.1; ALT_INIT; mRNA.
DR PIR; T08944; T08944.
DR RefSeq; NP_194618.3; NM_119033.5.
DR AlphaFoldDB; Q5XF85; -.
DR SMR; Q5XF85; -.
DR STRING; 3702.AT4G28890.1; -.
DR iPTMnet; Q5XF85; -.
DR PaxDb; Q5XF85; -.
DR PRIDE; Q5XF85; -.
DR ProteomicsDB; 246567; -.
DR EnsemblPlants; AT4G28890.1; AT4G28890.1; AT4G28890.
DR GeneID; 829010; -.
DR Gramene; AT4G28890.1; AT4G28890.1; AT4G28890.
DR KEGG; ath:AT4G28890; -.
DR Araport; AT4G28890; -.
DR TAIR; locus:2123558; AT4G28890.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_046350_0_0_1; -.
DR InParanoid; Q5XF85; -.
DR OMA; FANRETC; -.
DR OrthoDB; 957971at2759; -.
DR PhylomeDB; Q5XF85; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5XF85; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5XF85; baseline and differential.
DR Genevisible; Q5XF85; 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:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Membrane; Metal-binding; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..432
FT /note="E3 ubiquitin-protein ligase ATL42"
FT /id="PRO_0000030711"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 123..165
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CONFLICT 133
FT /note="V -> F (in Ref. 4; BX828195)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="D -> N (in Ref. 4; BX828195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 49374 MW; 07BB8AD7653ECFDF CRC64;
MYQIFFFFLP LLHSYASAQT PPPFRNGDLV ANFEPSLAVV TGVLAIMFAL TFVLLVYAKC
CHIDLRSGSG DRRRHDRRLR QGIFFNRSTA SSDRFSGLDK TAIESLPLFR FSALKGSKQG
LDCSVCLSKF ESVEILRLLP KCRHAFHIGC IDQWLEQHAT CPLCRDRVSM EEDSSVLTNG
NSFRFLNQSE IREDSSLELY IEREEEEERI HREELSGSSR FSIGESFRKI LKLGNKEKTL
LDEHVNDKDE KKLMHKFNHR IVVSDVVFKN RWSNVSSSDL MFLNSEMVNS ISSERFSSLD
HVKRGDEEDQ IGILRIKEEM EAKRMLENKL TSMTTMFSSE NGDSGSKSRS VMIEPGRRSV
SDITAVPRLS ISIHGDCSGS AAETASALQN GGNETEERRR RLWLPIARKT AQWFANREKR
SQINTTHQHF DV
