RHF2A_ARATH
ID RHF2A_ARATH Reviewed; 375 AA.
AC Q9ZT42; B9DFN0; Q3E981; Q8GXA8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=E3 ubiquitin-protein ligase RHF2A {ECO:0000305};
DE EC=2.3.2.27;
DE AltName: Full=RING-H2 finger F2a {ECO:0000303|PubMed:9781696};
DE AltName: Full=RING-H2 zinc finger protein RHF2a {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase RHF2A {ECO:0000305};
GN Name=RHF2A {ECO:0000303|PubMed:9781696}; OrderedLocusNames=At5g22000;
GN ORFNames=T6G21.110;
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 [MRNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=18552199; DOI=10.1105/tpc.108.059741;
RA Liu J., Zhang Y., Qin G., Tsuge T., Sakaguchi N., Luo G., Sun K., Shi D.,
RA Aki S., Zheng N., Aoyama T., Oka A., Yang W., Umeda M., Xie Q., Gu H.,
RA Qu L.J.;
RT "Targeted degradation of the cyclin-dependent kinase inhibitor ICK4/KRP6 by
RT RING-type E3 ligases is essential for mitotic cell cycle progression during
RT Arabidopsis gametogenesis.";
RL Plant Cell 20:1538-1554(2008).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in the positive
CC regulation of the gametogenesis progression. Required for the
CC degradation of KRP6, a cyclin-dependent kinase inhibitor which
CC accumulates during meiosis and blocks the progression of subsequent
CC mitoses during gametophytes development. Functions in association with
CC RHF1A. {ECO:0000269|PubMed:18552199}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZT42-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZT42-2; Sequence=VSP_039550;
CC -!- DEVELOPMENTAL STAGE: Expressed throughout flower development.
CC {ECO:0000269|PubMed:18552199}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC42950.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF079182; AAC69856.1; -; mRNA.
DR EMBL; AL589883; CAC34493.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92965.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92966.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92967.1; -; Genomic_DNA.
DR EMBL; AK118336; BAC42950.1; ALT_FRAME; mRNA.
DR EMBL; AF324994; AAG40346.1; -; mRNA.
DR EMBL; BT002347; AAN86180.1; -; mRNA.
DR EMBL; AK316835; BAH19547.1; -; mRNA.
DR PIR; T51854; T51854.
DR RefSeq; NP_568410.1; NM_122125.3. [Q9ZT42-1]
DR RefSeq; NP_851050.1; NM_180719.4. [Q9ZT42-1]
DR RefSeq; NP_851051.1; NM_180720.1. [Q9ZT42-2]
DR AlphaFoldDB; Q9ZT42; -.
DR BioGRID; 17535; 1.
DR STRING; 3702.AT5G22000.1; -.
DR iPTMnet; Q9ZT42; -.
DR PaxDb; Q9ZT42; -.
DR PRIDE; Q9ZT42; -.
DR ProteomicsDB; 237002; -. [Q9ZT42-1]
DR EnsemblPlants; AT5G22000.1; AT5G22000.1; AT5G22000. [Q9ZT42-1]
DR EnsemblPlants; AT5G22000.2; AT5G22000.2; AT5G22000. [Q9ZT42-2]
DR EnsemblPlants; AT5G22000.3; AT5G22000.3; AT5G22000. [Q9ZT42-1]
DR GeneID; 832260; -.
DR Gramene; AT5G22000.1; AT5G22000.1; AT5G22000. [Q9ZT42-1]
DR Gramene; AT5G22000.2; AT5G22000.2; AT5G22000. [Q9ZT42-2]
DR Gramene; AT5G22000.3; AT5G22000.3; AT5G22000. [Q9ZT42-1]
DR KEGG; ath:AT5G22000; -.
DR Araport; AT5G22000; -.
DR TAIR; locus:505006626; AT5G22000.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_053463_0_0_1; -.
DR InParanoid; Q9ZT42; -.
DR OMA; SMRCKES; -.
DR OrthoDB; 1003237at2759; -.
DR PhylomeDB; Q9ZT42; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9ZT42; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ZT42; baseline and differential.
DR Genevisible; Q9ZT42; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0009561; P:megagametogenesis; IGI:TAIR.
DR GO; GO:0055046; P:microgametogenesis; IGI:TAIR.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IGI:TAIR.
DR GO; GO:0051726; P:regulation of cell cycle; IGI:TAIR.
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 Alternative splicing; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..375
FT /note="E3 ubiquitin-protein ligase RHF2A"
FT /id="PRO_0000395846"
FT ZN_FING 33..74
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 146..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 3..6
FT /note="GAGE -> VRVS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039550"
FT CONFLICT 66
FT /note="R -> K (in Ref. 4; BAC42950)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="E -> K (in Ref. 6; BAH19547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 41029 MW; C633AF0D4DA11DD6 CRC64;
MEGAGETTTS EGHLTSAAAF VEGGIQDACD DACSICLESF CESDPSTLTS CKHEYHLQCI
LEWCQRSSQC PMCWQSISLK DPTSQELLEA VEQERNFRFN PTRNATIFRH PTLGDFELQH
LPVGVDNAEI EERIIQHLAA AAAMGRARHG VRREGHRSRS SSQGHQQFMV FSSQPNASSP
PPHPPMPSSP SQRDESDTVS NLPHNALGEG SHQSNTQPPT SSHPRQVSPS ASDSNSRPLN
QSSPSEQDRA GPSELQSFSE SLKSRLNAVS TRYKESISKN TRNWKDRLFS RNTSMADLGS
EVKREVSAGI ATVSRMMERL ETRENSRPST ASVSDVSENH TPETNNEHNR AAAGDEHSVN
ERGVKETCAT GSGSS
