ATL13_ARATH
ID ATL13_ARATH Reviewed; 472 AA.
AC Q940Q4; Q9M0C0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=RING-H2 finger protein ATL13;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL13 {ECO:0000305};
GN Name=ATL13; OrderedLocusNames=At4g30400; ORFNames=F17I23.260;
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=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 [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 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 [5]
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 [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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB79758.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF160182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161577; CAB79758.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE85760.1; -; Genomic_DNA.
DR EMBL; AY054187; AAL06848.1; -; mRNA.
DR EMBL; AY103309; AAM65361.1; -; mRNA.
DR PIR; E85355; E85355.
DR RefSeq; NP_567846.1; NM_119186.3.
DR AlphaFoldDB; Q940Q4; -.
DR SMR; Q940Q4; -.
DR BioGRID; 14450; 1.
DR STRING; 3702.AT4G30400.1; -.
DR iPTMnet; Q940Q4; -.
DR PaxDb; Q940Q4; -.
DR PRIDE; Q940Q4; -.
DR ProteomicsDB; 246552; -.
DR EnsemblPlants; AT4G30400.1; AT4G30400.1; AT4G30400.
DR GeneID; 829163; -.
DR Gramene; AT4G30400.1; AT4G30400.1; AT4G30400.
DR KEGG; ath:AT4G30400; -.
DR Araport; AT4G30400; -.
DR TAIR; locus:2118666; AT4G30400.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_034332_0_0_1; -.
DR InParanoid; Q940Q4; -.
DR OMA; VPNSHEL; -.
DR OrthoDB; 945746at2759; -.
DR PhylomeDB; Q940Q4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q940Q4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q940Q4; baseline and differential.
DR Genevisible; Q940Q4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA: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..472
FT /note="RING-H2 finger protein ATL13"
FT /id="PRO_0000055804"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 134..176
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 320..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 79
FT /note="S -> P (in Ref. 3; AAL06848/AAM65361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 52339 MW; 352223639E386E4D CRC64;
MKFSRENMKW VFPEIKTTQN FLSPSSLPQE PPLSLRSSAN FDLNSKISPS ILLIIIILSI
IFFISGLLHL LVRFLLTPSS RDREDYFDNV TALQGQLQQL FHLHDSGVDQ SFIDTLPVFH
YKSIIGLKNY PFDCAVCLCE FETEDKLRLL PKCSHAFHMD CIDTWLLSHS TCPLCRSSLL
SDLSSHQDPR SSFLLVLESA SDHSSREIGG DRDSAACVAA NDDIDVSSAH LGLVGNNDLG
STRIDSGHGD QYLDGELGGS VGKVVPFSVK LGKFRNIDIG EGTSSNNNIG NSSSLDERRC
FSMGSYEYIM DEETTLKVHV STKKQSSKNR GLPGHRTAMS ECGFDPTGRL KFSGSGSMRI
VEEAAEKNVV ERESFSVSKI WLRGKKEKHS KVQGKEDSSL VSSSSGRAFS FRLSNQRNHP
DAMIESGCEE DNQKCENSES LETKTPSFAR RTMLWLAGRQ NKVVHSSSST NV
