PUB5_ARATH
ID PUB5_ARATH Reviewed; 718 AA.
AC O23225; F4JQE6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=U-box domain-containing protein 5;
DE EC=2.3.2.27;
DE AltName: Full=Plant U-box protein 5;
DE AltName: Full=RING-type E3 ubiquitin transferase PUB5 {ECO:0000305};
GN Name=PUB5; OrderedLocusNames=At4g36550; ORFNames=AP22.63, C7A10.810;
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=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 [2]
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 [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 GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=11495788; DOI=10.1016/s1360-1385(01)01960-4;
RA Azevedo C., Santos-Rosa M.J., Shirasu K.;
RT "The U-box protein family in plants.";
RL Trends Plant Sci. 6:354-358(2001).
RN [5]
RP GENE FAMILY ORGANIZATION.
RX PubMed=14657406; DOI=10.1104/pp.103.029553;
RA Mudgil Y., Shiu S.-H., Stone S.L., Salt J.N., Goring D.R.;
RT "A large complement of the predicted Arabidopsis ARM repeat proteins are
RT members of the U-box E3 ubiquitin ligase family.";
RL Plant Physiol. 134:59-66(2004).
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase. {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 -!- SEQUENCE CAUTION:
CC Sequence=CAB16838.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80321.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z99708; CAB16838.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161589; CAB80321.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86671.1; -; Genomic_DNA.
DR PIR; E85431; E85431.
DR RefSeq; NP_195373.6; NM_119818.6.
DR AlphaFoldDB; O23225; -.
DR SMR; O23225; -.
DR STRING; 3702.AT4G36550.1; -.
DR iPTMnet; O23225; -.
DR PaxDb; O23225; -.
DR PRIDE; O23225; -.
DR ProteomicsDB; 226355; -.
DR EnsemblPlants; AT4G36550.1; AT4G36550.1; AT4G36550.
DR GeneID; 829807; -.
DR Gramene; AT4G36550.1; AT4G36550.1; AT4G36550.
DR KEGG; ath:AT4G36550; -.
DR Araport; AT4G36550; -.
DR TAIR; locus:2115365; AT4G36550.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_006348_4_1_1; -.
DR InParanoid; O23225; -.
DR OMA; GSHNRIA; -.
DR OrthoDB; 478706at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O23225; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23225; baseline and differential.
DR Genevisible; O23225; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 3: Inferred from homology;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway.
FT CHAIN 1..718
FT /note="U-box domain-containing protein 5"
FT /id="PRO_0000322150"
FT DOMAIN 218..292
FT /note="U-box"
FT REPEAT 493..532
FT /note="ARM 1"
FT REPEAT 534..571
FT /note="ARM 2"
FT REPEAT 573..613
FT /note="ARM 3"
FT REGION 662..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 79919 MW; 531C7070C1B4C78F CRC64;
MRIDYTERMP QSYKMHSSMC LELKRLVDRI MRIFPDIEDA RPGCSSGIQT LCLLHNALDK
TKQLLQYCSE SSKLYMAVTG DAILARGSRA KKSLEQCLND IRSIVPTILE IKISQIVQDL
RSTQLTLEFS EEEAGKAIRE LMQKSTSSSA SPDEIKDFHY AALKLQLSTP EAIVTERRSL
KIICEDHKQN SFTHHQSIDD SLHANAAEAE ASEEHNGTLP EKFKCTLSRT VMYDPVIISS
GNTFERMQIQ KWFDEGNDSC PISKRKLDDF TLKPNVELKS QISEWCAKNG LDVQDPARKH
VKASNSIDFS VSIASFGSSL YNIPDHSGIS ITDFNSSYSI DSSSYSKMSK GGYFTPMQRI
DSASGAGDTD SSHSEIEIDP LCGLTNLPWD AQIKVVEDVR SRFEHSTRAF RSMSPSKFLE
PLITYLKNAL ERNGTAGEII KGGLDLLLAF LSGNRRAIES LEEEVFKMFS VFLESEVVAE
EALNILEVLS NHPHGPSKIT SSGSLSSLLK IVESQAEHLQ EQAMITLKNL SSSMEICLEM
VSLDFIQKLT SFLQQKVFCK HSIIILKNLC STEKGRGCIT ETPDCLASIA ELLESNVPEE
QENAISILLQ LCVQKIEYCC LVVREATDIY SSLILISNNG TEEVKVSASE LLRALVEVDS
DKEEEEEVSS RPEGRTTASP TSQVVTPVTH PEPVKITPSP KKSGLFGFNF SSLKKKKK
