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   27-MAR-2024, entry version 148.
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).
RN   [12]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=24122828; DOI=10.1105/tpc.113.116012;
RA   Lin W.Y., Huang T.K., Chiou T.J.;
RT   "Nitrogen limitation adaptation, a target of microRNA827, mediates
RT   degradation of plasma membrane-localized phosphate transporters to maintain
RT   phosphate homeostasis in Arabidopsis.";
RL   Plant Cell 25:4061-4074(2013).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH NLA.
RX   PubMed=24474629; DOI=10.1105/tpc.113.120311;
RA   Park B.S., Seo J.S., Chua N.H.;
RT   "NITROGEN LIMITATION ADAPTATION recruits PHOSPHATE2 to target the phosphate
RT   transporter PT2 for degradation during the regulation of Arabidopsis
RT   phosphate homeostasis.";
RL   Plant Cell 26:454-464(2014).
CC   -!- FUNCTION: E2 ubiquitin-protein ligase that mediates E1-dependent
CC       protein ubiquitination (PubMed:24474629). Mediates PHO1 degradation
CC       through multivesicular body-mediated vacuolar proteolysis in response
CC       to inorganic phosphate (Pi) availability (PubMed:22634761). Negatively
CC       regulates the protein abundance of PHF1 and PHT1s under Pi-sufficient
CC       conditions by facilitating the degradation of PHT1 proteins at the
CC       endomembrane (PubMed:24122829, PubMed:22634761). Functions
CC       cooperatively with NLA to regulate the abundance of the inorganic
CC       phosphate (Pi) transporters PHT1-1, PHT1-2 and PHT1-3 in different
CC       subcellular compartments (PubMed:24122828). Regulates Pi homeostasis by
CC       mediating, cooperatively with NLA, polyubiquitination of PHT1-4 and its
CC       targeting for degradation (PubMed:24474629).
CC       {ECO:0000269|PubMed:22634761, ECO:0000269|PubMed:24122828,
CC       ECO:0000269|PubMed:24122829, ECO:0000269|PubMed:24474629}.
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 (PubMed:22634761). Interacts with NLA
CC       (PubMed:24474629). {ECO:0000269|PubMed:22634761,
CC       ECO:0000269|PubMed:24474629}.
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.Q8VY10; -.
DR   PaxDb; 3702-AT2G33770-1; -.
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; AT2G33770; PHO2.
DR   eggNOG; KOG0895; Eukaryota.
DR   HOGENOM; CLU_002088_0_0_1; -.
DR   InParanoid; Q8VY10; -.
DR   OMA; GCKNSST; -.
DR   OrthoDB; 1211582at2759; -.
DR   PhylomeDB; Q8VY10; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q8VY10; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8VY10; baseline and differential.
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; IEA:UniProtKB-EC.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:2000185; P:regulation of phosphate transmembrane transport; IGI:TAIR.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR46116; (E3-INDEPENDENT) E2 UBIQUITIN-CONJUGATING ENZYME; 1.
DR   PANTHER; PTHR46116:SF15; UBIQUITIN-CONJUGATING ENZYME E2 24-RELATED; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; Q8VY10; AT.
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
//