RING2_ARATH
ID RING2_ARATH Reviewed; 381 AA.
AC Q8LDB8; Q93Z65; Q9CAM6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=E3 ubiquitin-protein ligase At1g63170;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein At1g63170;
DE AltName: Full=RING-type E3 ubiquitin transferase At1g63170 {ECO:0000305};
GN OrderedLocusNames=At1g63170; ORFNames=F16M19.7;
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
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).
CC -!- FUNCTION: Mediates E2-dependent protein ubiquitination. {ECO:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-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}.
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DR EMBL; AC010795; AAG51597.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34064.1; -; Genomic_DNA.
DR EMBL; AY058092; AAL24200.1; -; mRNA.
DR EMBL; AY086095; AAM63303.1; -; mRNA.
DR PIR; C96657; C96657.
DR RefSeq; NP_564810.1; NM_104995.4.
DR AlphaFoldDB; Q8LDB8; -.
DR SMR; Q8LDB8; -.
DR STRING; 3702.AT1G63170.1; -.
DR PaxDb; Q8LDB8; -.
DR PRIDE; Q8LDB8; -.
DR ProteomicsDB; 236190; -.
DR EnsemblPlants; AT1G63170.1; AT1G63170.1; AT1G63170.
DR GeneID; 842621; -.
DR Gramene; AT1G63170.1; AT1G63170.1; AT1G63170.
DR KEGG; ath:AT1G63170; -.
DR Araport; AT1G63170; -.
DR TAIR; locus:2015248; AT1G63170.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_038211_0_1_1; -.
DR InParanoid; Q8LDB8; -.
DR OMA; ANTMISF; -.
DR OrthoDB; 923130at2759; -.
DR PhylomeDB; Q8LDB8; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8LDB8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LDB8; baseline and differential.
DR Genevisible; Q8LDB8; 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 Coiled coil; Membrane; Metal-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..381
FT /note="E3 ubiquitin-protein ligase At1g63170"
FT /id="PRO_0000271542"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 325..366
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..194
FT /evidence="ECO:0000255"
FT COMPBIAS 141..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 298
FT /note="Q -> E (in Ref. 4; AAM63303)"
FT /evidence="ECO:0000305"
FT CONFLICT 374..381
FT /note="NYEEGEEV -> GGGGGEKI (in Ref. 3; AAL24200)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 42677 MW; D17F999BFA6AD18B CRC64;
MSRETTTEAT PLILTDGGGG RRSVRRQGLR EAARLLRHAS SGRMMMREPS MLVREAAAEQ
LEERQSDWAY SKPVVVLDFV WNLAFVVVAT AVLVLSSDEN PNMPLRVWII GYGLQCMMHM
VCVCVEYRRR NSRRRRDLSP RSSSSSSSSS SSMDEEEGLG LSRNSDERYL ELGQLENENN
SFAKHLESAN TMISFIWWVI GFYWVSSGGQ ELAQGSPQLY WLCIVFLGFD VFFVVFCVAL
ACVIGIAVCC CLPCIIAVLY AVAEQEGASK EDIDQLTKFK FRKVGDTMKH TVDEEQGQGD
SGGVMTECGT DSPVEHALPH EDAECCICLS AYEDETELRE LPCGHHFHCG CVDKWLYINA
TCPLCKYNIL KSSNYEEGEE V
