ID Q9M1D5_ARATH Unreviewed; 306 AA.
AC Q9M1D5; A0A178V9H3;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 183.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=BTL13 {ECO:0000313|TAIR:AT3G60080};
GN Synonyms=T2O9.60 {ECO:0000313|EMBL:CAB75923.1};
GN OrderedLocusNames=At3g60080 {ECO:0000313|Araport:AT3G60080,
GN ECO:0000313|EMBL:AEE80009.1};
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 {ECO:0000313|EMBL:CAB75923.1};
RN [1] {ECO:0000313|EMBL:AEE80009.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130713; DOI=10.1038/35048706;
RG European Union Chromosome 3 Arabidopsis Sequencing Consortium;
RG Institute for Genomic Research;
RG Kazusa DNA Research Institute;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Blocker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M.,
RA Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N.,
RA Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L.,
RA Weissenbach J., Saurin W., Quetier F., Schafer M., Muller-Auer S.,
RA Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N.,
RA Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P.,
RA Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S.,
RA Simionati B., Conrad A., Hornischer K., Kauer G., Lohnert T.H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schon O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwalder 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., Kaul S.,
RA 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 [2] {ECO:0000313|EMBL:CAB75923.1}
RP NUCLEOTIDE SEQUENCE.
RA EU Arabidopsis sequencing project;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAB75923.1}
RP NUCLEOTIDE SEQUENCE.
RA Nyakatura G., Fartmann B., Dauner D., Sterr W., Holland R.,
RA Weichselgartner M., Mewes H.W., Lemcke K., Mayer K.F.X., Quetier F.,
RA Salanoubat M.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AAW78589.1}
RP NUCLEOTIDE SEQUENCE.
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:BAF01193.1}
RP NUCLEOTIDE SEQUENCE.
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T.,
RA Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K.,
RA Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K.,
RA Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA Hayashizaki Y., Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:AEE80009.1}
RP NUCLEOTIDE SEQUENCE.
RG TAIR;
RA Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:AEE80009.1}
RP NUCLEOTIDE SEQUENCE.
RA Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
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:0000256|ARBA:ARBA00000900};
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DR EMBL; BT020239; AAV74233.1; -; mRNA.
DR EMBL; BT020570; AAW78589.1; -; mRNA.
DR EMBL; CP002686; AEE80009.1; -; Genomic_DNA.
DR EMBL; AK229330; BAF01193.1; -; mRNA.
DR EMBL; AL138658; CAB75923.1; -; Genomic_DNA.
DR PIR; T47832; T47832.
DR RefSeq; NP_191567.1; NM_115871.3.
DR AlphaFoldDB; Q9M1D5; -.
DR SMR; Q9M1D5; -.
DR IntAct; Q9M1D5; 1.
DR STRING; 3702.Q9M1D5; -.
DR PaxDb; 3702-AT3G60080-1; -.
DR EnsemblPlants; AT3G60080.1; AT3G60080.1; AT3G60080.
DR GeneID; 825178; -.
DR Gramene; AT3G60080.1; AT3G60080.1; AT3G60080.
DR KEGG; ath:AT3G60080; -.
DR Araport; AT3G60080; -.
DR TAIR; AT3G60080; BTL13.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_967559_0_0_1; -.
DR OMA; DPIVICA; -.
DR OrthoDB; 690674at2759; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1D5; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR PANTHER; PTHR15710:SF187; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; zinc_ribbon_9; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q9M1D5};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 169..210
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 119..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 306 AA; 33798 MW; 88C75B4290080449 CRC64;
MSSSTTTTTT VHGEPERRTY WCHECDMSLS LLSSSDSDSD SSPLLCPQCR VDFLERMDHD
SSSSNLFDVT IGDFEEQDGE NDDEDDEEDW CFVDPAVNSD DNFLLDSPYL HRLLRHLASD
NSGSSSSSSS SSSSSLLKSS DIDSIPTIQI SSSLLCSTDD SDPDSVLLCA VCKEDFIIGE
SARRLPCSHI YHSDCIVPWL SDHNSCPLCR FELPTTAKVG IGGSEAEMRI RLSDLATIAA
DGDDVEDDWL GIRNALRRLA RRHEQMRLGV GEMERNLART VSGLGIGMRR REEIEADRSN
VTTTPL
//
