ATL65_ARATH
ID ATL65_ARATH Reviewed; 411 AA.
AC Q67YI6; Q9LJ73;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=RING-H2 finger protein ATL65;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL65 {ECO:0000305};
GN Name=ATL65; OrderedLocusNames=At3g18930; ORFNames=K13E13.2;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-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 -!- 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; AP000735; BAB01689.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76169.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76170.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65228.1; -; Genomic_DNA.
DR EMBL; AY090932; AAM13984.1; -; mRNA.
DR EMBL; AY122920; AAM67453.1; -; mRNA.
DR EMBL; AY136452; AAM97117.1; -; mRNA.
DR EMBL; BT008506; AAP37865.1; -; mRNA.
DR EMBL; AK175597; BAD43360.1; -; mRNA.
DR EMBL; AK176482; BAD44245.1; -; mRNA.
DR RefSeq; NP_001327213.1; NM_001338371.1.
DR RefSeq; NP_188523.1; NM_112779.5.
DR RefSeq; NP_974336.1; NM_202607.2.
DR AlphaFoldDB; Q67YI6; -.
DR SMR; Q67YI6; -.
DR BioGRID; 6758; 4.
DR IntAct; Q67YI6; 4.
DR iPTMnet; Q67YI6; -.
DR PaxDb; Q67YI6; -.
DR PRIDE; Q67YI6; -.
DR ProteomicsDB; 246571; -.
DR EnsemblPlants; AT3G18930.1; AT3G18930.1; AT3G18930.
DR EnsemblPlants; AT3G18930.2; AT3G18930.2; AT3G18930.
DR EnsemblPlants; AT3G18930.3; AT3G18930.3; AT3G18930.
DR GeneID; 821425; -.
DR Gramene; AT3G18930.1; AT3G18930.1; AT3G18930.
DR Gramene; AT3G18930.2; AT3G18930.2; AT3G18930.
DR Gramene; AT3G18930.3; AT3G18930.3; AT3G18930.
DR KEGG; ath:AT3G18930; -.
DR Araport; AT3G18930; -.
DR TAIR; locus:2085914; AT3G18930.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_753050_0_0_1; -.
DR InParanoid; Q67YI6; -.
DR OMA; RYRLNIG; -.
DR OrthoDB; 1411786at2759; -.
DR PhylomeDB; Q67YI6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q67YI6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q67YI6; baseline and differential.
DR Genevisible; Q67YI6; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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..411
FT /note="RING-H2 finger protein ATL65"
FT /id="PRO_0000055792"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 156..198
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 325
FT /note="K -> R (in Ref. 4; BAD44245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 46664 MW; 0A30FB7B460C736F CRC64;
MRFVAPPPRS GDNSPSPSPS SGISEEILSR SSDPPLEFSP PLIAMVVVLA AAFLFVTYSR
LISRRFLSPL FRRFRRWRCR RRRLLHLSSA SSASTSSSDL RSFSPFPFDS FHYSSYSPYG
LDDSVIKTLP LFLYSAAACT GKPAVGKTSA ANCRDCAVCL LEFEEGDYVR TLPLCFHAFH
LECIDEWLRS HPNCPLCRTA ILGSAGVLTP MSPFVPLMAP RIRPSLDDEE NNAIIIRGEI
TPSRSNWNTI AADTTNDQEI RASVEEQSSP AISRFRELKR SYSFECERES ESERVTMEPA
TVSPWRYRRS TWNKRQSPFG NLISKSRVFS FRYYRSTKSP FFRRRSSAGV FYPISERIPA
TGSSSRRTKS MTSPMFFRTA PHSSSRLRCG DPEALLSPER WRRRDTCRAE M
