G3PC2_ARATH
ID G3PC2_ARATH Reviewed; 338 AA.
AC Q9FX54; B9DGZ4;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic {ECO:0000303|PubMed:18298409, ECO:0000303|PubMed:22589465};
DE EC=1.2.1.12 {ECO:0000255|PROSITE-ProRule:PRU10009, ECO:0000269|PubMed:18298409};
DE AltName: Full=NAD-dependent glyceraldehydephosphate dehydrogenase C subunit 2 {ECO:0000303|PubMed:18298409, ECO:0000303|PubMed:22589465};
GN Name=GAPC2 {ECO:0000303|PubMed:18298409, ECO:0000303|PubMed:22589465};
GN Synonyms=GAPDH {ECO:0000303|PubMed:18298409};
GN OrderedLocusNames=At1g13440 {ECO:0000312|Araport:AT1G13440};
GN ORFNames=T6J4.17 {ECO:0000312|EMBL:AAG09543.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP GLUTATHIONYLATION AT CYS-156, S-NITROSYLATION AT CYS-156 AND CYS-160, AND
RP PATHWAY.
RX PubMed=18298409; DOI=10.1111/j.1399-3054.2008.01066.x;
RA Holtgrefe S., Gohlke J., Starmann J., Druce S., Klocke S., Altmann B.,
RA Wojtera J., Lindermayr C., Scheibe R.;
RT "Regulation of plant cytosolic glyceraldehyde 3-phosphate dehydrogenase
RT isoforms by thiol modifications.";
RL Physiol. Plantarum 133:211-228(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH PLDDELTA.
RX PubMed=22589465; DOI=10.1105/tpc.111.094946;
RA Guo L., Devaiah S.P., Narasimhan R., Pan X., Zhang Y., Zhang W., Wang X.;
RT "Cytosolic glyceraldehyde-3-phosphate dehydrogenases interact with
RT phospholipase Ddelta to transduce hydrogen peroxide signals in the
RT Arabidopsis response to stress.";
RL Plant Cell 24:2200-2212(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-121; LYS-219; LYS-223;
RP LYS-231 AND LYS-255, INTERACTION WITH DPB3-1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=32651385; DOI=10.1038/s41467-020-17311-4;
RA Kim S.-C., Guo L., Wang X.;
RT "Nuclear moonlighting of cytosolic glyceraldehyde-3-phosphate dehydrogenase
RT regulates Arabidopsis response to heat stress.";
RL Nat. Commun. 11:3439-3439(2020).
CC -!- FUNCTION: Key enzyme in glycolysis that catalyzes the first step of the
CC pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-
CC phospho-D-glyceroyl phosphate. Essential for the maintenance of
CC cellular ATP levels and carbohydrate metabolism (By similarity). Binds
CC DNA in vitro (PubMed:22589465). Together with DNA polymerase II subunit
CC B3-1 (DPB3-1) and GAPC1, enhances heat tolerance and promotes the
CC expression of heat-inducible genes (PubMed:32651385).
CC {ECO:0000250|UniProtKB:P25858, ECO:0000269|PubMed:22589465,
CC ECO:0000269|PubMed:32651385}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10009,
CC ECO:0000269|PubMed:18298409};
CC -!- ACTIVITY REGULATION: Inhibition by oxidized glutathione (GSSG), S-
CC nitrosoglutathione (GSNO) and hydrogen peroxide.
CC {ECO:0000269|PubMed:18298409, ECO:0000269|PubMed:22589465}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000269|PubMed:18298409}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with PLDDELTA (By
CC similarity). Binds to DPB3-1/NF-YC10 in response to heat-stress; this
CC interaction promotes DPB3-1/NF-YC10 DNA-binding ability to its target
CC promoter (PubMed:32651385). {ECO:0000250|UniProtKB:P25858,
CC ECO:0000250|UniProtKB:P54226, ECO:0000269|PubMed:22589465,
CC ECO:0000269|PubMed:32651385}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18298409,
CC ECO:0000269|PubMed:32651385}. Nucleus {ECO:0000269|PubMed:18298409,
CC ECO:0000269|PubMed:32651385}. Note=Accumulates in the nucleus under
CC heat stress. {ECO:0000269|PubMed:32651385}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FX54-1; Sequence=Displayed;
CC -!- PTM: S-glutathionylation at Cys-156 in the presence of oxidized
CC glutathione (GSSG). S-nitrosylation at Cys-156 and Cys-160 in the
CC presence of S-nitrosoglutathione (GSNO) or sodium nitroprusside (SNP).
CC These reactions may be both a protective mechanism against irreversible
CC oxidation and a mean to store inhibited enzyme in a recoverable form.
CC {ECO:0000269|PubMed:18298409}.
CC -!- DISRUPTION PHENOTYPE: The double mutant gapc1 gapc2 has an impaired
CC ability to enhance heat tolerance of seedlings and to promote the
CC expression of heat-inducible genes. {ECO:0000269|PubMed:32651385}.
CC -!- MISCELLANEOUS: Plants contain three types of GAPDH: NAD-dependent
CC cytosolic forms which participate in glycolysis, NAD-dependent
CC chloroplastic forms which participate in plastidic glycolysis and NADP-
CC dependent chloroplastic forms which participate in the photosynthetic
CC reductive pentose phosphate pathway (Calvin-Benson cycle). All the
CC forms are encoded by distinct genes.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AC011810; AAG09543.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29016.1; -; Genomic_DNA.
DR EMBL; AF410271; AAK95257.1; -; mRNA.
DR EMBL; AY049259; AAK83601.1; -; mRNA.
DR EMBL; AY090275; AAL90936.1; -; mRNA.
DR EMBL; AK317337; BAH20011.1; -; mRNA.
DR RefSeq; NP_172801.1; NM_101214.4. [Q9FX54-1]
DR AlphaFoldDB; Q9FX54; -.
DR SMR; Q9FX54; -.
DR BioGRID; 23144; 18.
DR IntAct; Q9FX54; 2.
DR MINT; Q9FX54; -.
DR STRING; 3702.AT1G13440.1; -.
DR iPTMnet; Q9FX54; -.
DR MetOSite; Q9FX54; -.
DR World-2DPAGE; 0003:Q9FX54; -.
DR PaxDb; Q9FX54; -.
DR PRIDE; Q9FX54; -.
DR ProteomicsDB; 248598; -. [Q9FX54-1]
DR EnsemblPlants; AT1G13440.1; AT1G13440.1; AT1G13440. [Q9FX54-1]
DR GeneID; 837904; -.
DR Gramene; AT1G13440.1; AT1G13440.1; AT1G13440. [Q9FX54-1]
DR KEGG; ath:AT1G13440; -.
DR Araport; AT1G13440; -.
DR TAIR; locus:2010007; AT1G13440.
DR eggNOG; KOG0657; Eukaryota.
DR HOGENOM; CLU_030140_0_3_1; -.
DR InParanoid; Q9FX54; -.
DR OMA; NRMLDNC; -.
DR PhylomeDB; Q9FX54; -.
DR BRENDA; 1.2.1.12; 399.
DR UniPathway; UPA00109; UER00184.
DR PRO; PR:Q9FX54; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FX54; baseline and differential.
DR Genevisible; Q9FX54; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0006094; P:gluconeogenesis; TAS:TAIR.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10836; PTHR10836; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Glutathionylation;
KW Glycolysis; NAD; Nucleus; Oxidoreductase; Reference proteome;
KW S-nitrosylation.
FT CHAIN 1..338
FT /note="Glyceraldehyde-3-phosphate dehydrogenase GAPC2,
FT cytosolic"
FT /id="PRO_0000420730"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P25858"
FT BINDING 15..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 155..157
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 186
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 215..216
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 238
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT SITE 183
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT MOD_RES 156
FT /note="S-glutathionyl cysteine; transient; alternate"
FT /evidence="ECO:0000269|PubMed:18298409"
FT MOD_RES 156
FT /note="S-nitrosocysteine; transient; alternate"
FT /evidence="ECO:0000269|PubMed:18298409"
FT MOD_RES 160
FT /note="S-nitrosocysteine; transient"
FT /evidence="ECO:0000269|PubMed:18298409"
FT MUTAGEN 121
FT /note="K->A: In GAPCmut; compromised heat-induced nuclear
FT accumulation leading to impaired ability to enhance heat
FT tolerance; when associated with A-231. In GAPCmut';
FT impaired DPB3-1/NF-YC10 binding, but normal heat-induced
FT nuclear translocation and impaired ability to enhance heat
FT tolerance; when associated with A-219, A-223 and A-255."
FT /evidence="ECO:0000269|PubMed:32651385"
FT MUTAGEN 219
FT /note="K->A: In GAPCmut'; impaired DPB3-1/NF-YC10 binding,
FT but normal heat-induced nuclear translocation and impaired
FT ability to enhance heat tolerance; when associated with A-
FT 121, A-223 and A-255."
FT /evidence="ECO:0000269|PubMed:32651385"
FT MUTAGEN 223
FT /note="K->A: In GAPCmut'; impaired DPB3-1/NF-YC10 binding,
FT but normal heat-induced nuclear translocation and impaired
FT ability to enhance heat tolerance; when associated with A-
FT 121, A-219 and A-255."
FT /evidence="ECO:0000269|PubMed:32651385"
FT MUTAGEN 231
FT /note="K->A: In GAPCmut; compromised heat-induced nuclear
FT accumulation leading to impaired ability to enhance heat
FT tolerance; when associated with A-121."
FT /evidence="ECO:0000269|PubMed:32651385"
FT MUTAGEN 255
FT /note="K->A: In GAPCmut'; impaired DPB3-1/NF-YC10 binding,
FT but normal heat-induced nuclear translocation and impaired
FT ability to enhance heat tolerance; when associated with A-
FT 121, A-219 and A-223."
FT /evidence="ECO:0000269|PubMed:32651385"
FT CONFLICT 22
FT /note="R -> K (in Ref. 4; BAH20011)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="I -> V (in Ref. 4; BAH20011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 36913 MW; 6EED7A21EBD51D64 CRC64;
MADKKIRIGI NGFGRIGRLV ARVVLQRDDV ELVAVNDPFI TTEYMTYMFK YDSVHGQWKH
HELKVKDDKT LLFGEKPVTV FGIRNPEDIP WGEAGADFVV ESTGVFTDKD KAAAHLKGGA
KKVVISAPSK DAPMFVVGVN EHEYKSDLDI VSNASCTTNC LAPLAKVIND RFGIVEGLMT
TVHSITATQK TVDGPSMKDW RGGRAASFNI IPSSTGAAKA VGKVLPSLNG KLTGMSFRVP
TVDVSVVDLT VRLEKAATYD EIKKAIKEES EGKMKGILGY TEDDVVSTDF VGDNRSSIFD
AKAGIALSDK FVKLVSWYDN EWGYSSRVVD LIVHMSKA
