G3P_CHICK
ID G3P_CHICK Reviewed; 333 AA.
AC P00356; Q90848; Q90849; Q98926;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P04406};
DE AltName: Full=Peptidyl-cysteine S-nitrosylase GAPDH {ECO:0000305};
DE EC=2.6.99.- {ECO:0000250|UniProtKB:P04797};
GN Name=GAPDH; Synonyms=GAPD;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6322764; DOI=10.1016/0006-291x(84)91461-x;
RA Panabieres F., Piechaczyk M., Rainer B., Dani C., Fort P., Riaad S.,
RA Marty L., Imbach J.L., Jeanteur P., Blanchard J.-M.;
RT "Complete nucleotide sequence of the messenger RNA coding for chicken
RT muscle glyceraldehyde-3-phosphate dehydrogenase.";
RL Biochem. Biophys. Res. Commun. 118:767-773(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6303388; DOI=10.1021/bi00276a013;
RA Dugaiczyk A., Haron J.A., Stone E.M., Dennison O.E., Rothblum K.N.,
RA Schwartz R.J.;
RT "Cloning and sequencing of a deoxyribonucleic acid copy of glyceraldehyde-
RT 3-phosphate dehydrogenase messenger ribonucleic acid isolated from chicken
RT muscle.";
RL Biochemistry 22:1605-1613(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3856841; DOI=10.1073/pnas.82.6.1628;
RA Stone E.M., Rothblum K.N., Alevy M.C., Kuo T.M., Schwartz R.J.;
RT "Complete sequence of the chicken glyceraldehyde-3-phosphate dehydrogenase
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1628-1632(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hubbard White Mountain; TISSUE=Testis;
RX PubMed=9736461;
RX DOI=10.1002/(sici)1097-4644(19981001)71:1<127::aid-jcb13>3.0.co;2-k;
RA Mezquita J., Pau M., Mezquita C.;
RT "Several novel transcripts of glyceraldehyde-3-phosphate dehydrogenase
RT expressed in adult chicken testis.";
RL J. Cell. Biochem. 71:127-139(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 197-333.
RC TISSUE=Heart;
RX PubMed=6179937; DOI=10.1016/s0021-9258(18)34153-x;
RA Arnold H.H., Domdey H., Wiebauer K., Datta K., Siddiqui M.A.Q.;
RT "Cloning, partial sequencing, and expression of glyceraldehyde-3-phosphate
RT dehydrogenase gene in chick embryonic heart muscle cells.";
RL J. Biol. Chem. 257:9872-9877(1982).
RN [6]
RP ERRATUM OF PUBMED:6179937, AND SEQUENCE REVISION TO 329.
RA Arnold H.H., Domdey H., Wiebauer K., Datta K., Siddiqui M.A.Q.;
RL J. Biol. Chem. 258:2063-2063(1983).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-225.
RC TISSUE=Brain;
RX PubMed=6687938; DOI=10.1093/nar/11.10.3301;
RA Milner R.J., Brow M.A.D., Cleveland D.W., Shinnick T.M., Sutcliff J.G.;
RT "Glyceraldehyde 3-phosphate dehydrogenase protein and mRNA are both
RT differentially expressed in adult chickens but not chick embryos.";
RL Nucleic Acids Res. 11:3301-3315(1983).
CC -!- FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and
CC nitrosylase activities, thereby playing a role in glycolysis and
CC nuclear functions, respectively. Glyceraldehyde-3-phosphate
CC dehydrogenase is a key enzyme in glycolysis that catalyzes the first
CC step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P)
CC into 3-phospho-D-glyceroyl phosphate (By similarity). Participates in
CC nuclear events including transcription, RNA transport, DNA replication
CC and apoptosis. Nuclear functions are probably due to the nitrosylase
CC activity that mediates cysteine S-nitrosylation of nuclear target
CC proteins such as SIRT1, HDAC2 and PRKDC (By similarity).
CC {ECO:0000250|UniProtKB:P04406, ECO:0000250|UniProtKB:P04797}.
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:0000250|UniProtKB:P04406, ECO:0000255|PROSITE-
CC ProRule:PRU10009};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + S-nitroso-L-cysteinyl-[GAPDH] = L-
CC cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:66684, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:17089,
CC Rhea:RHEA-COMP:17090, Rhea:RHEA-COMP:17091, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:149494; Evidence={ECO:0000250|UniProtKB:P04797};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685;
CC Evidence={ECO:0000250|UniProtKB:P04797};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P04406}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}.
CC -!- PTM: S-nitrosylation of Cys-150 leads to translocation to the nucleus.
CC {ECO:0000250|UniProtKB:P04797}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {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; K01458; AAA48778.1; -; mRNA.
DR EMBL; V00407; CAA23698.1; -; mRNA.
DR EMBL; M11213; AAA48774.1; -; Genomic_DNA.
DR EMBL; AF047874; AAD02474.1; -; mRNA.
DR EMBL; V00406; CAA23697.1; -; mRNA.
DR EMBL; X01578; CAA25733.1; -; mRNA.
DR PIR; A00368; DECHG3.
DR RefSeq; NP_989636.1; NM_204305.1.
DR AlphaFoldDB; P00356; -.
DR SMR; P00356; -.
DR BioGRID; 675216; 2.
DR IntAct; P00356; 1.
DR STRING; 9031.ENSGALP00000023278; -.
DR Allergome; 12127; Gal d GAPDH.
DR PaxDb; P00356; -.
DR Ensembl; ENSGALT00000023323; ENSGALP00000023278; ENSGALG00000014442.
DR Ensembl; ENSGALT00000086032; ENSGALP00000063325; ENSGALG00000014442.
DR GeneID; 374193; -.
DR KEGG; gga:374193; -.
DR CTD; 2597; -.
DR VEuPathDB; HostDB:geneid_374193; -.
DR eggNOG; KOG0657; Eukaryota.
DR GeneTree; ENSGT00940000153298; -.
DR HOGENOM; CLU_030140_0_1_1; -.
DR InParanoid; P00356; -.
DR OMA; NCVAPMA; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; P00356; -.
DR BRENDA; 1.2.1.12; 1306.
DR Reactome; R-GGA-352875; Gluconeogenesis.
DR Reactome; R-GGA-352882; Glycolysis.
DR UniPathway; UPA00109; UER00184.
DR PRO; PR:P00356; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000014442; Expressed in muscle tissue and 13 other tissues.
DR ExpressionAtlas; P00356; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097452; C:GAIT complex; IEA:Ensembl.
DR GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IEA:Ensembl.
DR GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0035605; F:peptidyl-cysteine S-nitrosylase activity; ISS:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0050832; P:defense response to fungus; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; NAS:AgBase.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0051873; P:killing by host of symbiont cells; IEA:Ensembl.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:AgBase.
DR GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0000740; P:nuclear membrane fusion; IMP:AgBase.
DR GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS: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 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Cytoskeleton; Glycolysis; NAD; Nucleus;
KW Oxidoreductase; Reference proteome; S-nitrosylation; Transferase.
FT CHAIN 1..333
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145496"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 149..151
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 180
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 150
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P04797"
FT CONFLICT 2
FT /note="V -> RSE (in Ref. 7; CAA25733)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="V -> L (in Ref. 7; CAA25733)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="G -> D (in Ref. 1; AAA48778, 2; CAA23698 and 3;
FT AAA48774)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="D -> E (in Ref. 5; CAA23697)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="D -> H (in Ref. 3; AAA48774)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="M -> T (in Ref. 5; CAA23697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 35704 MW; 9DB2517A1C94342B CRC64;
MVKVGVNGFG RIGRLVTRAA VLSGKVQVVA INDPFIDLNY MVYMFKYDST HGHFKGTVKA
ENGKLVINGH AITIFQERDP SNIKWADAGA EYVVESTGVF TTMEKAGAHL KGGAKRVIIS
APSADAPMFV MGVNHEKYDK SLKIVSNASC TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT
ATQKTVDGPS GKLWRDGRGA AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV
VDLTCRLEKP AKYDDIKRVV KAAADGPLKG ILGYTEDQVV SCDFNGDSHS STFDAGAGIA
LNDHFVKLVS WYDNEFGYSN RVVDLMVHMA SKE
