RHG1A_ARATH
ID RHG1A_ARATH Reviewed; 691 AA.
AC Q9FMM4; Q9ZT41;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Probable E3 ubiquitin-protein ligase RHG1A {ECO:0000305};
DE EC=2.3.2.27;
DE AltName: Full=RING-H2 finger G1a {ECO:0000303|PubMed:9781696};
DE AltName: Full=RING-H2 zinc finger protein RHG1a {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase RHG1A {ECO:0000305};
GN Name=RHG1A {ECO:0000303|PubMed:9781696};
GN OrderedLocusNames=At5g42940 {ECO:0000312|Araport:AT5G42940};
GN ORFNames=MBD2.14 {ECO:0000312|EMBL:BAB09196.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 502-691, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9781696; DOI=10.1016/s0014-5793(98)01143-0;
RA Jensen R.B., Jensen K.L., Jespersen H.M., Skriver K.;
RT "Widespread occurrence of a highly conserved RING-H2 zinc finger motif in
RT the model plant Arabidopsis thaliana.";
RL FEBS Lett. 436:283-287(1998).
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase that may possess E3
CC ubiquitin ligase activity in vitro. {ECO:0000250|UniProtKB:Q9ZT50}.
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. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, flowers, green siliques,
CC cauline leaves, seeds and roots. {ECO:0000269|PubMed:9781696}.
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DR EMBL; AB008264; BAB09196.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94890.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68691.1; -; Genomic_DNA.
DR EMBL; AF462851; AAL58938.1; -; mRNA.
DR EMBL; BT004548; AAO42794.1; -; mRNA.
DR EMBL; AK319077; BAH57192.1; -; mRNA.
DR EMBL; AF079183; AAC69857.1; -; mRNA.
DR PIR; T51859; T51859.
DR RefSeq; NP_001330419.1; NM_001344467.1.
DR RefSeq; NP_199108.1; NM_123659.4.
DR AlphaFoldDB; Q9FMM4; -.
DR SMR; Q9FMM4; -.
DR IntAct; Q9FMM4; 5.
DR STRING; 3702.AT5G42940.1; -.
DR iPTMnet; Q9FMM4; -.
DR PaxDb; Q9FMM4; -.
DR PRIDE; Q9FMM4; -.
DR ProteomicsDB; 236914; -.
DR EnsemblPlants; AT5G42940.1; AT5G42940.1; AT5G42940.
DR EnsemblPlants; AT5G42940.2; AT5G42940.2; AT5G42940.
DR GeneID; 834306; -.
DR Gramene; AT5G42940.1; AT5G42940.1; AT5G42940.
DR Gramene; AT5G42940.2; AT5G42940.2; AT5G42940.
DR KEGG; ath:AT5G42940; -.
DR Araport; AT5G42940; -.
DR TAIR; locus:2160031; AT5G42940.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_024479_0_0_1; -.
DR InParanoid; Q9FMM4; -.
DR OMA; RNTCVRS; -.
DR OrthoDB; 301445at2759; -.
DR PhylomeDB; Q9FMM4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FMM4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMM4; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045191; MBR1/2-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22937; PTHR22937; 1.
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 Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..691
FT /note="Probable E3 ubiquitin-protein ligase RHG1A"
FT /id="PRO_0000436417"
FT ZN_FING 637..678
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 71..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 665
FT /note="K -> E (in Ref. 5; AAC69857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 691 AA; 75284 MW; 6FDC83FE448558CB CRC64;
MQGERASLGY LSEALNFEHG SSSSNGVIDH WENIHSLGDN DLQDYMIANS ESNTSLANSV
YHEQQGLRRF SLGEASSSGT KDEASSHNEQ RMETRCFDGR GNEIIDLDPV FAQPSGTNQP
VQNVNLNAEY IEIHEDINPY RGRSGFIEAN GPGTRVSQPG RSFEENGVGT GSSVEGRRAS
CKRKALEGSI SQSSSGGYHD FQRGESSSWT PGSTVFRPGN GLNISGSLDN GPRGMVSGTV
PNFPVSAPNF PVSAIAESSS RNICVRSNPS DHQETVNPST FAAGTVVRRP VPPSQLNLSR
HLPADQHSLD LRPGQSFVVS RNPNSTPVSI PPGSRTMLPP FRWTGSSLVG GTSNSTAPVE
RNLHLDETRS RSIPGNTLEI PMFAAPEVGN FARSQSSRNV TNGNLNSASS VSRTGSTTSV
PPPPPPSSNL AWTSYQNSPH YQRRRTERSE LARRSLLSSL AADATNQRSG DHPTLRSLAP
PASSDGLVLQ PGGDNSQMHN RAYSRAGPLF DRQGDSVVGI PHPLRALAAA SRGRSRLMVS
QMQNVLDVMR RDANNNNLRL EDVMLLNHSV LFDGATGHDR YRDMRLDVDN MSYEELLALE
ERIGDVCTGV NEETISNRLK QRKYKSNTKS PQDAEPCCVC QEEYTEGEDM GTLECGHEFH
SQCIKEWLKQ KNLCPICKTT GLNTAKKRRI A
