RHF1A_ARATH
ID RHF1A_ARATH Reviewed; 371 AA.
AC Q4TU14; O23280; Q8GXY4; Q9ZT43;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=E3 ubiquitin-protein ligase RHF1A {ECO:0000305};
DE EC=2.3.2.27;
DE AltName: Full=RING-H2 finger F1a {ECO:0000303|PubMed:9781696};
DE AltName: Full=RING-H2 zinc finger protein RHF1a {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase RHF1A {ECO:0000305};
GN Name=RHF1A {ECO:0000303|PubMed:9781696}; OrderedLocusNames=At4g14220;
GN ORFNames=dl3150w, FCAALL.146;
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], AND FUNCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 43-371, 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).
RN [7]
RP FUNCTION, INTERACTION WITH KRP6, 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. Mediates the proteasomal
CC degradation of KRP6, a cyclin-dependent kinase inhibitor which
CC accumulates during meiosis and blocks the progression of subsequent
CC mitoses during gametophyte development. Functions in association with
CC RHF2A (PubMed:18552199). Possesses E3 ubiquitin-protein ligase activity
CC when associated with the E2 enzyme UBC8 in vitro (PubMed:15644464).
CC {ECO:0000269|PubMed:15644464, 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 -!- SUBUNIT: Interacts with KRP6. {ECO:0000269|PubMed:18552199}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, flowers, green siliques,
CC cauline leaves, seeds and roots. {ECO:0000269|PubMed:9781696}.
CC -!- DEVELOPMENTAL STAGE: Expressed in emerging floral primordia and then in
CC stamens and carpels. Expressed first in stamen primordia, then in
CC pollen mother cells and tapetal cells and later in microspores until
CC flower stage 11. Expressed in carpels throughout flower development
CC from primordia to the mature embryo sac stage. Expressed in developing
CC embryo. {ECO:0000269|PubMed:18552199}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB46003.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78464.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ059122; AAY57608.1; -; mRNA.
DR EMBL; Z97335; CAB46003.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161538; CAB78464.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83395.1; -; Genomic_DNA.
DR EMBL; AK117968; BAC42605.1; -; mRNA.
DR EMBL; AF079181; AAC69855.1; -; mRNA.
DR PIR; C85155; C85155.
DR PIR; T51853; T51853.
DR RefSeq; NP_193158.2; NM_117499.5.
DR AlphaFoldDB; Q4TU14; -.
DR BioGRID; 12359; 1.
DR STRING; 3702.AT4G14220.1; -.
DR iPTMnet; Q4TU14; -.
DR PaxDb; Q4TU14; -.
DR PRIDE; Q4TU14; -.
DR ProteomicsDB; 236860; -.
DR EnsemblPlants; AT4G14220.1; AT4G14220.1; AT4G14220.
DR GeneID; 827062; -.
DR Gramene; AT4G14220.1; AT4G14220.1; AT4G14220.
DR KEGG; ath:AT4G14220; -.
DR Araport; AT4G14220; -.
DR TAIR; locus:2129525; AT4G14220.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_053463_0_0_1; -.
DR InParanoid; Q4TU14; -.
DR OMA; PICWQLF; -.
DR OrthoDB; 872903at2759; -.
DR PhylomeDB; Q4TU14; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q4TU14; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q4TU14; baseline and differential.
DR Genevisible; Q4TU14; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0009561; P:megagametogenesis; IGI:TAIR.
DR GO; GO:0055046; P:microgametogenesis; IGI:TAIR.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..371
FT /note="E3 ubiquitin-protein ligase RHF1A"
FT /id="PRO_0000395845"
FT ZN_FING 46..87
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 199..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 81
FT /note="K -> R (in Ref. 5; BAC42605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 40284 MW; E8DBE16ECEC28821 CRC64;
MSNFTYTSAF NLSDNSPFNP AIGSSSSSSS ALVVASDDDN NTDDACSICL EPFTLQDPST
VTSCKHEYHL QCIIEWSQRS KECPICWQLF VLRDPASQEL LAAVEKERLL KTRNISSSSP
ISIHHSHDDF HSEEEESQFS SFDEQFLRHL TEAAHRRCLL RRRDGQISSS LVSSSDPTTI
HPTDLVNLYR LSAISHVEHQ NSNPCPSPGS MTPSPVSGHS SIPADSNNGS RISPGPSPSR
SSQSPKSPEA SSLPEAIKSK LAAASAKYKE SISKSKQGLK EKLLARNNSV KELSKGVQRE
MNAGIAGVAR MIERMDFSSK RFGGSAHVST STATASGFNF SFKGKRVEAN SKSNNNGDKT
EPQKLQGGET C
