ATL4_ARATH
ID ATL4_ARATH Reviewed; 334 AA.
AC Q9LY41; Q4TU21; Q9SPV6; Q9ZT40;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=E3 ubiquitin-protein ligase ATL4 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:15644464};
DE AltName: Full=Protein ARABIDOPSIS TOXICOS EN LEVADURA 4 {ECO:0000303|PubMed:10480382};
DE Short=Protein ATL4 {ECO:0000303|PubMed:10480382};
DE AltName: Full=RING-H2 finger X1a {ECO:0000303|PubMed:9781696};
DE AltName: Full=RING-H2 zinc finger protein ATL4 {ECO:0000305};
DE AltName: Full=RING-H2 zinc finger protein RHX1a {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL4 {ECO:0000305};
GN Name=ATL4 {ECO:0000303|PubMed:16557337};
GN Synonyms=RHX1A {ECO:0000303|PubMed:9781696}; OrderedLocusNames=At3g60220;
GN ORFNames=F27H5_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].
RX PubMed=10480382; DOI=10.1023/a:1006267201855;
RA Salinas-Mondragon R.E., Garciduenas-Pina C., Guzman P.;
RT "Early elicitor induction in members of a novel multigene family coding for
RT highly related RING-H2 proteins in Arabidopsis thaliana.";
RL Plant Mol. Biol. 40:579-590(1999).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-334.
RC STRAIN=cv. Columbia;
RX PubMed=9781696; DOI=10.1016/s0014-5793(98)01143-0;
RA Jensen R.B., Jensen K.L., Jespersen H.M., Skriver K.;
RT "Widespread occurrence of a highly conserved RING-H2 zinc finger motif in
RT the model plant Arabidopsis thaliana.";
RL FEBS Lett. 436:283-287(1998).
RN [7]
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 [8]
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=AAD33582.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF132014; AAD33582.1; ALT_FRAME; mRNA.
DR EMBL; DQ059115; AAY57601.1; -; mRNA.
DR EMBL; AL163852; CAB87859.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80025.1; -; Genomic_DNA.
DR EMBL; BT028933; ABI49480.1; -; mRNA.
DR EMBL; AF079184; AAC69858.1; -; mRNA.
DR PIR; T49217; T49217.
DR PIR; T51855; T51855.
DR PIR; T52407; T52407.
DR RefSeq; NP_191581.1; NM_115885.3.
DR AlphaFoldDB; Q9LY41; -.
DR SMR; Q9LY41; -.
DR BioGRID; 10506; 5.
DR IntAct; Q9LY41; 5.
DR STRING; 3702.AT3G60220.1; -.
DR iPTMnet; Q9LY41; -.
DR PaxDb; Q9LY41; -.
DR PRIDE; Q9LY41; -.
DR ProteomicsDB; 246570; -.
DR EnsemblPlants; AT3G60220.1; AT3G60220.1; AT3G60220.
DR GeneID; 825192; -.
DR Gramene; AT3G60220.1; AT3G60220.1; AT3G60220.
DR KEGG; ath:AT3G60220; -.
DR Araport; AT3G60220; -.
DR TAIR; locus:2081907; AT3G60220.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_060203_0_0_1; -.
DR InParanoid; Q9LY41; -.
DR OMA; AWLVTNQ; -.
DR OrthoDB; 1492050at2759; -.
DR PhylomeDB; Q9LY41; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LY41; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LY41; baseline and differential.
DR Genevisible; Q9LY41; 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:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
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; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..334
FT /note="E3 ubiquitin-protein ligase ATL4"
FT /id="PRO_0000055795"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 117..159
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 126
FT /note="P -> S (in Ref. 1; AAD33582)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 36562 MW; 4242795D598537AF CRC64;
MESLINPSHG GGNYDSHSSS LDSLKPSVLV IILILLMTLL ISVSICFLLR CLNRCSHRSV
LPLSSSSSVA TVTSDSRRFS GHRVSPETER SSVLDSLPIF KFSSVTRRSS SMNSGDCAVC
LSKFEPEDQL RLLPLCCHAF HADCIDIWLV SNQTCPLCRS PLFASESDLM KSLAVVGSNN
GGGENSFRLE IGSISRRRQT PIPESVEQHR TYSIGSFDYI VDDVDSEISE SNFNRGKQED
ATTTTATATA VTTNPTSFEA SLAADIGNDG SRSWLKDYVD RLSRGISSRA MSFRSSGRFF
TGSSRRSEEL TVMDLEANHA GEEISELFRW LSGV
