XB34_ARATH
ID XB34_ARATH Reviewed; 376 AA.
AC Q9FPH0; Q8LAN6;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Putative E3 ubiquitin-protein ligase XBAT34;
DE EC=2.3.2.27;
DE AltName: Full=Ankyrin repeat domain and RING finger-containing protein XBAT34;
DE AltName: Full=Protein XB3 homolog 4;
DE AltName: Full=RING-type E3 ubiquitin transferase XBAT34;
GN Name=XBAT34; OrderedLocusNames=At4g14365; ORFNames=dl3220c, FCAALL.222;
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=Seedling;
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=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].
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.
CC -!- FUNCTION: No E3 ubiquitin-protein ligase activity observed when
CC associated with the E2 enzyme UBC8 in vitro.
CC {ECO:0000269|PubMed:15644464}.
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 -!- SEQUENCE CAUTION:
CC Sequence=CAB10215.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g14360 has been split into 2 genes: At4g14365 and At4g14360.; Evidence={ECO:0000305};
CC Sequence=CAB78478.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g14360 has been split into 2 genes: At4g14365 and At4g14360.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ086842; AAZ14066.1; -; mRNA.
DR EMBL; Z97336; CAB10215.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161538; CAB78478.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83429.1; -; Genomic_DNA.
DR EMBL; AF325044; AAG40396.1; -; mRNA.
DR EMBL; AY062788; AAL32866.1; -; mRNA.
DR EMBL; AY081602; AAM10164.1; -; mRNA.
DR EMBL; AY087705; AAM65242.1; -; mRNA.
DR RefSeq; NP_567428.1; NM_117514.4.
DR AlphaFoldDB; Q9FPH0; -.
DR SMR; Q9FPH0; -.
DR STRING; 3702.AT4G14365.1; -.
DR PaxDb; Q9FPH0; -.
DR PRIDE; Q9FPH0; -.
DR ProteomicsDB; 242776; -.
DR EnsemblPlants; AT4G14365.1; AT4G14365.1; AT4G14365.
DR GeneID; 827080; -.
DR Gramene; AT4G14365.1; AT4G14365.1; AT4G14365.
DR KEGG; ath:AT4G14365; -.
DR Araport; AT4G14365; -.
DR TAIR; locus:505006458; AT4G14365.
DR eggNOG; ENOG502QQ81; Eukaryota.
DR HOGENOM; CLU_027253_2_0_1; -.
DR OMA; KCHYRAS; -.
DR OrthoDB; 896321at2759; -.
DR PhylomeDB; Q9FPH0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FPH0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9FPH0; baseline and differential.
DR Genevisible; Q9FPH0; AT.
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; 1.25.40.20; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12796; Ank_2; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Metal-binding; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..376
FT /note="Putative E3 ubiquitin-protein ligase XBAT34"
FT /id="PRO_0000395742"
FT REPEAT 41..71
FT /note="ANK 1"
FT REPEAT 77..106
FT /note="ANK 2"
FT ZN_FING 325..364
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CONFLICT 117
FT /note="V -> A (in Ref. 6; AAM65242)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="Y -> F (in Ref. 6; AAM65242)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="V -> I (in Ref. 6; AAM65242)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="A -> T (in Ref. 6; AAM65242)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="A -> D (in Ref. 6; AAM65242)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="A -> D (in Ref. 6; AAM65242)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="A -> E (in Ref. 6; AAM65242)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="S -> Y (in Ref. 6; AAM65242)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="E -> K (in Ref. 6; AAM65242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41383 MW; 4F4BF549E9ABBFB6 CRC64;
MGQQQSQSKD EMLFQEVSNN NVEGIKSLHH EGAGLEGVDK LGRTPLILAC TNDDLYDVAK
TLLELGSNVN AYRSGCNGGT PLHHAAKRGL VHTVKLLLSH GANPLVLDDD VKTALEVARD
EGYSNVVRAI ESHICLFSGC MREYSGSSLL NLFAPQLLSR KVWVVVVPTG SRNPTKPLKL
ELVLYDSIQD AQPRMVIPLW KANLEEPKSF RCDDSVMIID DSRSPKSMRQ RRESGFISQA
RRWAQVDRQI RLKLAAEIKG DMKQMNWFSE ACKGVPQPMN PPRFMKTSQA TTTTTNVPAL
SDDALTRVAM SLPSPKTANK EDGLCVICVD APSEAVCVPC GHVAGCISCL KEIENKKMGC
PVCRANIDQV IKLYHV
