ATL76_ARATH
ID ATL76_ARATH Reviewed; 225 AA.
AC Q6NML0; Q4FE33; Q9M9C0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=E3 ubiquitin-protein ligase ATL76;
DE EC=2.3.2.27 {ECO:0000269|PubMed:15644464};
DE AltName: Full=RING-H2 finger protein ATL76;
DE AltName: Full=RING-type E3 ubiquitin transferase ATL76 {ECO:0000305};
GN Name=ATL76; OrderedLocusNames=At1g49210; ORFNames=F27J15.3;
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;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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=AAF69722.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g49200 has been split into 2 genes: At1g49200 and At1g49210.; Evidence={ECO:0000305};
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DR EMBL; DQ086858; AAZ14074.1; -; mRNA.
DR EMBL; AC016041; AAF69722.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32405.1; -; Genomic_DNA.
DR EMBL; BT010932; AAR24710.1; -; mRNA.
DR EMBL; BT011647; AAS47653.1; -; mRNA.
DR RefSeq; NP_175347.1; NM_103811.4.
DR AlphaFoldDB; Q6NML0; -.
DR SMR; Q6NML0; -.
DR STRING; 3702.AT1G49210.1; -.
DR PaxDb; Q6NML0; -.
DR PRIDE; Q6NML0; -.
DR EnsemblPlants; AT1G49210.1; AT1G49210.1; AT1G49210.
DR GeneID; 841344; -.
DR Gramene; AT1G49210.1; AT1G49210.1; AT1G49210.
DR KEGG; ath:AT1G49210; -.
DR Araport; AT1G49210; -.
DR TAIR; locus:2028406; AT1G49210.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_013137_9_0_1; -.
DR InParanoid; Q6NML0; -.
DR OMA; DPFDHNS; -.
DR OrthoDB; 1555832at2759; -.
DR PhylomeDB; Q6NML0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6NML0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NML0; baseline and differential.
DR Genevisible; Q6NML0; 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:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044602; ATL10/ATL75-79.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46905; PTHR46905; 1.
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..225
FT /note="E3 ubiquitin-protein ligase ATL76"
FT /id="PRO_0000055767"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 135..177
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 225 AA; 25184 MW; EA73773C3DEDB630 CRC64;
MSANELPASA QSLQEQFLGS FVTRKLLLHD PFDHNSLRVF AVAPSPLITH ENNLKGNVLM
LLSVLICGII CCLGLHYIIR CAFRRSSRFM ISEPISSLST PRSSSNKGIK KKALRMFPVV
SYSREMNLPG IGEECVICLS DFVSGEQLRL LPKCNHGFHV RCIDKWLQHH LTCPKCRHCL
VETCQKILGD FSQADSMAST PTESVIVRID PLEPEGRVNT FRESS
