UBC24_ARATH
ID UBC24_ARATH Reviewed; 907 AA.
AC Q8VY10; P93012; Q0WLN6; Q0WM96;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable ubiquitin-conjugating enzyme E2 24 {ECO:0000303|PubMed:16339806};
DE EC=2.3.2.23 {ECO:0000305};
DE AltName: Full=AtPHO2 {ECO:0000303|PubMed:16679424};
DE AltName: Full=E2 ubiquitin-conjugating enzyme 24 {ECO:0000303|PubMed:16339806};
DE AltName: Full=Ubiquitin carrier protein 24 {ECO:0000303|PubMed:16339806};
DE AltName: Full=Ubiquitin-protein ligase 24 {ECO:0000303|PubMed:16339806};
GN Name=UBC24 {ECO:0000303|PubMed:16339806};
GN Synonyms=PHO2 {ECO:0000303|PubMed:16679424};
GN OrderedLocusNames=At2g33770 {ECO:0000312|Araport:AT2G33770};
GN ORFNames=T1B8.8 {ECO:0000312|EMBL:AAC69130.1};
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 [MRNA] (ISOFORM 1), GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16339806; DOI=10.1104/pp.105.067983;
RA Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W.,
RA Callis J.;
RT "Genome analysis and functional characterization of the E2 and RING-type E3
RT ligase ubiquitination enzymes of Arabidopsis.";
RL Plant Physiol. 139:1597-1611(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, DEVELOPMENTAL
RP STAGE, TISSUE SPECIFICITY, AND REGULATION BY MIR399.
RX PubMed=16679424; DOI=10.1104/pp.106.079707;
RA Bari R., Datt Pant B., Stitt M., Scheible W.-R.;
RT "PHO2, microRNA399, and PHR1 define a phosphate-signaling pathway in
RT plants.";
RL Plant Physiol. 141:988-999(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, REGULATION BY
RP MIR399, AND TISSUE SPECIFICITY.
RX PubMed=16679417; DOI=10.1104/pp.106.078063;
RA Aung K., Lin S.-I., Wu C.-C., Huang Y.-T., Su C.-L., Chiou T.-J.;
RT "pho2, a phosphate overaccumulator, is caused by a nonsense mutation in a
RT microRNA399 target gene.";
RL Plant Physiol. 141:1000-1011(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP REGULATION BY MIR399.
RX PubMed=17643101; DOI=10.1038/ng2079;
RA Franco-Zorrilla J.M., Valli A., Todesco M., Mateos I., Puga M.I.,
RA Rubio-Somoza I., Leyva A., Weigel D., Garcia J.A., Paz-Ares J.;
RT "Target mimicry provides a new mechanism for regulation of microRNA
RT activity.";
RL Nat. Genet. 39:1033-1037(2007).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=18390805; DOI=10.1104/pp.108.116269;
RA Lin S.-I., Chiang S.-F., Lin W.-Y., Chen J.-W., Tseng C.-Y., Wu P.-C.,
RA Chiou T.-J.;
RT "Regulatory network of MicroRNA399 and PHO2 by systemic signaling.";
RL Plant Physiol. 147:732-746(2008).
RN [10]
RP FUNCTION, INTERACTION WITH PHO1, MUTAGENESIS OF CYS-748, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22634761; DOI=10.1105/tpc.112.096636;
RA Liu T.Y., Huang T.K., Tseng C.Y., Lai Y.S., Lin S.I., Lin W.Y., Chen J.W.,
RA Chiou T.J.;
RT "PHO2-dependent degradation of PHO1 modulates phosphate homeostasis in
RT Arabidopsis.";
RL Plant Cell 24:2168-2183(2012).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24122829; DOI=10.1105/tpc.113.115998;
RA Huang T.K., Han C.L., Lin S.I., Chen Y.J., Tsai Y.C., Chen Y.R., Chen J.W.,
RA Lin W.Y., Chen P.M., Liu T.Y., Chen Y.S., Sun C.M., Chiou T.J.;
RT "Identification of downstream components of ubiquitin-conjugating enzyme
RT PHOSPHATE2 by quantitative membrane proteomics in Arabidopsis roots.";
RL Plant Cell 25:4044-4060(2013).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins (By similarity). Mediates PHO1
CC degradation through multivesicular body-mediated vacuolar proteolysis
CC in response to inorganic phosphate (Pi) availability (PubMed:22634761).
CC Negatively regulates the protein abundance of PHF1 and PHT1s under Pi-
CC sufficient conditions by facilitating the degradation of PHT1 proteins
CC at the endomembrane (PubMed:24122829). {ECO:0000250|UniProtKB:P42743,
CC ECO:0000269|PubMed:22634761, ECO:0000269|PubMed:24122829}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with PHO1. {ECO:0000269|PubMed:22634761}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22634761, ECO:0000269|PubMed:24122829}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:22634761,
CC ECO:0000269|PubMed:24122829}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VY10-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VY10-2; Sequence=VSP_034751;
CC -!- TISSUE SPECIFICITY: Expressed in the vascular tissues of cotyledons,
CC leaves, roots, sepals, filaments, anthers and junctions between the
CC inflorescence stems and siliques. {ECO:0000269|PubMed:16679417,
CC ECO:0000269|PubMed:16679424}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in senescing leaves and maturating
CC seeds. {ECO:0000269|PubMed:16679424}.
CC -!- INDUCTION: Down-regulated by phosphate deprivation (PubMed:16679424).
CC Systemically regulated by microRNA399 (miR399) (PubMed:16679424,
CC PubMed:18390805). {ECO:0000269|PubMed:16679424,
CC ECO:0000269|PubMed:18390805}.
CC -!- DISRUPTION PHENOTYPE: Plants are unable to regulate the amount of
CC phosphate accumulated into shoots. {ECO:0000269|PubMed:16679417}.
CC -!- MISCELLANEOUS: MicroRNA399 (miR399) can be sequestered by IPS1, a non-
CC protein coding RNA containing a motif with sequence complementarity to
CC miR399, but with a mismatched loop at the expected miRNA cleavage site.
CC Thus IPS1 mimics the target of miR399 to block the cleavage of
CC UBC24/PHO2 under Pi-deficient conditions.
CC {ECO:0000269|PubMed:17643101}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC69130.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ027037; AAY44863.1; -; mRNA.
DR EMBL; U78721; AAC69130.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08882.1; -; Genomic_DNA.
DR EMBL; AY074292; AAL66989.1; -; mRNA.
DR EMBL; AY091326; AAM14265.1; -; mRNA.
DR EMBL; AK229934; BAF01760.1; -; mRNA.
DR EMBL; AK230162; BAF01971.1; -; mRNA.
DR PIR; D84749; D84749.
DR RefSeq; NP_850218.1; NM_179887.3. [Q8VY10-1]
DR AlphaFoldDB; Q8VY10; -.
DR SMR; Q8VY10; -.
DR BioGRID; 3290; 1.
DR STRING; 3702.AT2G33770.1; -.
DR PaxDb; Q8VY10; -.
DR PRIDE; Q8VY10; -.
DR ProteomicsDB; 228691; -. [Q8VY10-1]
DR EnsemblPlants; AT2G33770.1; AT2G33770.1; AT2G33770. [Q8VY10-1]
DR GeneID; 817943; -.
DR Gramene; AT2G33770.1; AT2G33770.1; AT2G33770. [Q8VY10-1]
DR KEGG; ath:AT2G33770; -.
DR Araport; AT2G33770; -.
DR TAIR; locus:2057589; AT2G33770.
DR eggNOG; KOG0895; Eukaryota.
DR HOGENOM; CLU_002088_0_0_1; -.
DR InParanoid; Q8VY10; -.
DR OMA; GCKNSST; -.
DR OrthoDB; 808738at2759; -.
DR PhylomeDB; Q8VY10; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8VY10; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VY10; baseline and differential.
DR Genevisible; Q8VY10; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
DR GO; GO:0055062; P:phosphate ion homeostasis; IMP:TAIR.
DR GO; GO:0006817; P:phosphate ion transport; IMP:TAIR.
DR GO; GO:2000185; P:regulation of phosphate transmembrane transport; IGI:TAIR.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Endoplasmic reticulum; Golgi apparatus;
KW Ligase; Membrane; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..907
FT /note="Probable ubiquitin-conjugating enzyme E2 24"
FT /id="PRO_0000344361"
FT DOMAIN 662..822
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 748
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT VAR_SEQ 1..476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_034751"
FT MUTAGEN 748
FT /note="C->A: Loss of ubiquitin conjugase activity and loss
FT of down-regulation of PHO1."
FT /evidence="ECO:0000269|PubMed:22634761"
SQ SEQUENCE 907 AA; 100484 MW; 6C9CB1D8A3A95359 CRC64;
MEMSLTDSDW DSSSDSGSSE HEEVEFSYGG RAQNIFSNLE ETIGKIDEFL SFERGFMYGD
IVRSATEPSG QSGRVINIDM FVNLESTHGK IMKEVDTKRL QKLRSISLSD YVINGPWVGR
VDKIVERVSV TLDDGTNYEV LVDGQDKLVA IPPNLLEDSQ YSYYPGQRVQ VKLAHAPRST
TWLCGTWRGT QVMGTVCTVE AGLVYVDWVA SIVMEGDRNL TAPQALQNPE SLTLLPCVSH
ASWQLGDWCI LPGSSHCDIA ERQTPNVAAY NLNECHKTFQ KGFNRNMQNS GLDELFVITK
TKMKVAVMWQ DGSCSLGVDS QQLLPVGAVN AHDFWPEQFV VEKETCNSKK WGVVKAVNAK
EQTVKVQWTI QVEKEATGCV DEVMEEIVSA YELLEHPDFG FCFSDVVVKL LPEGKFDPNA
DTIVATEAKH LLTESDYSGA YFLSSIGVVT GFKNGSVKVK WANGSTSKVA PCEIWKMERS
EYSNSSTVSS EGSVQDLSQK ISQSDEASSN HQETGLVKLY SVGESCNENI PECSSFFLPK
AAIGFITNLA SSLFGYQGST SVISSHSRCN DSEDQSDSEV LVQETAESYD NSETNSGEVD
MTTTMVNIPI EGKGINKTLD STLLENSRNQ VRFRQFDMVN DCSDHHFLSS DKGLAQSQVT
KSWVKKVQQE WSNLEANLPN TIYVRVCEER MDLLRAALVG APGTPYHDGL FFFDIMLPPQ
YPHEPPMVHY HSGGMRLNPN LYESGRVCLS LLNTWSGSGT EVWNAGSSSI LQLLLSFQAL
VLNEKPYFNE AGYDKQLGRA EGEKNSVSYN ENAFLITCKS MISMLRKPPK HFEMLVKDHF
THRAQHVLAA CKAYMEGVPV GSSANLQGNS TTNSTGFKIM LSKLYPKLLE AFSEIGVDCV
QEIGPES
