ATL11_ARATH
ID ATL11_ARATH Reviewed; 404 AA.
AC Q84W40; Q9C7T5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=RING-H2 finger protein ATL11;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL11 {ECO:0000305};
DE Flags: Precursor;
GN Name=ATL11; OrderedLocusNames=At1g72200; ORFNames=T9N14.11;
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=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 [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 Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) 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 IDENTIFICATION.
RX PubMed=15238540; DOI=10.1534/genetics.104.028043;
RA Serrano M., Guzman P.;
RT "Isolation and gene expression analysis of Arabidopsis thaliana mutants
RT with constitutive expression of ATL2, an early elicitor-response RING-H2
RT zinc-finger gene.";
RL Genetics 167:919-929(2004).
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 -!- 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; AC067754; AAG51795.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35288.1; -; Genomic_DNA.
DR EMBL; BT004268; AAO42269.1; -; mRNA.
DR EMBL; BT020487; AAW38988.1; -; mRNA.
DR PIR; E96745; E96745.
DR RefSeq; NP_177365.1; NM_105879.4.
DR AlphaFoldDB; Q84W40; -.
DR SMR; Q84W40; -.
DR BioGRID; 28772; 5.
DR IntAct; Q84W40; 4.
DR STRING; 3702.AT1G72200.1; -.
DR PaxDb; Q84W40; -.
DR PRIDE; Q84W40; -.
DR ProteomicsDB; 246745; -.
DR EnsemblPlants; AT1G72200.1; AT1G72200.1; AT1G72200.
DR GeneID; 843552; -.
DR Gramene; AT1G72200.1; AT1G72200.1; AT1G72200.
DR KEGG; ath:AT1G72200; -.
DR Araport; AT1G72200; -.
DR TAIR; locus:2207026; AT1G72200.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_035191_1_0_1; -.
DR InParanoid; Q84W40; -.
DR OMA; PDRWGFT; -.
DR OrthoDB; 1087626at2759; -.
DR PhylomeDB; Q84W40; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q84W40; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84W40; baseline and differential.
DR Genevisible; Q84W40; 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; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..404
FT /note="RING-H2 finger protein ATL11"
FT /id="PRO_0000030704"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 144..186
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 339..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 324
FT /note="D -> G (in Ref. 3; AAO42269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 44629 MW; C6F742464FE2BF58 CRC64;
MNPKGRTNLN RSIIGGHDHG SILQLLLFLL LLSSHGGFKF VAGQATHGGS DVSGDSSRFD
PTMAILMIVL VSVFFFLGFF SVYIRRCLER VMGMDYGNPN DAGNWLATNR QQARGLDASI
IETFPTFQYS TVKTLRIGKE ALECSVCLNE FEDDETLRLI PKCCHVFHPG CIDAWLRSHT
TCPLCRADLI PVPGESIVSI QIPGLVNDPP GSDPNGDRIR SLGSPDARLI ESVALTCNQS
MPRRSMSTGW NLAGMFTNSD RTGQHSENLD RFTLRLPQDI HNKLVNPNLS KVHVALPQVM
SSTRGYRTGS LGSERNYFYY ERFDQDGRLD RRPFSITPPY RTSSINHMSP GGSGGDKVRA
SSPKSLLLAM RSPFDRLFLG KNNNVGENSS DHLRSCDATP SNTV
