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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-)

 G3P_CHICK               Reviewed;         333 AA.
P00356; Q90848; Q90849; Q98926;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 159.
RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
Short=GAPDH;
EC=1.2.1.12;
AltName: Full=Peptidyl-cysteine S-nitrosylase GAPDH;
EC=2.6.99.-;
Name=GAPDH; Synonyms=GAPD;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6322764; DOI=10.1016/0006-291X(84)91461-X;
Panabieres F., Piechaczyk M., Rainer B., Dani C., Fort P., Riaad S.,
Marty L., Imbach J.L., Jeanteur P., Blanchard J.-M.;
"Complete nucleotide sequence of the messenger RNA coding for chicken
muscle glyceraldehyde-3-phosphate dehydrogenase.";
Biochem. Biophys. Res. Commun. 118:767-773(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6303388; DOI=10.1021/bi00276a013;
Dugaiczyk A., Haron J.A., Stone E.M., Dennison O.E., Rothblum K.N.,
Schwartz R.J.;
"Cloning and sequencing of a deoxyribonucleic acid copy of
glyceraldehyde-3-phosphate dehydrogenase messenger ribonucleic acid
isolated from chicken muscle.";
Biochemistry 22:1605-1613(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3856841; DOI=10.1073/pnas.82.6.1628;
Stone E.M., Rothblum K.N., Alevy M.C., Kuo T.M., Schwartz R.J.;
"Complete sequence of the chicken glyceraldehyde-3-phosphate
dehydrogenase gene.";
Proc. Natl. Acad. Sci. U.S.A. 82:1628-1632(1985).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Hubbard White Mountain; TISSUE=Testis;
PubMed=9736461;
DOI=10.1002/(SICI)1097-4644(19981001)71:1<127::AID-JCB13>3.0.CO;2-K;
Mezquita J., Pau M., Mezquita C.;
"Several novel transcripts of glyceraldehyde-3-phosphate dehydrogenase
expressed in adult chicken testis.";
J. Cell. Biochem. 71:127-139(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 197-333.
TISSUE=Heart;
PubMed=6179937;
Arnold H.H., Domdey H., Wiebauer K., Datta K., Siddiqui M.A.Q.;
"Cloning, partial sequencing, and expression of glyceraldehyde-3-
phosphate dehydrogenase gene in chick embryonic heart muscle cells.";
J. Biol. Chem. 257:9872-9877(1982).
[6]
ERRATUM, AND SEQUENCE REVISION TO 329.
Arnold H.H., Domdey H., Wiebauer K., Datta K., Siddiqui M.A.Q.;
J. Biol. Chem. 258:2063-2063(1983).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-225.
TISSUE=Brain;
PubMed=6687938; DOI=10.1093/nar/11.10.3301;
Milner R.J., Brow M.A.D., Cleveland D.W., Shinnick T.M.,
Sutcliff J.G.;
"Glyceraldehyde 3-phosphate dehydrogenase protein and mRNA are both
differentially expressed in adult chickens but not chick embryos.";
Nucleic Acids Res. 11:3301-3315(1983).
-!- FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and
nitrosylase activities, thereby playing a role in glycolysis and
nuclear functions, respectively. Glyceraldehyde-3-phosphate
dehydrogenase is a key enzyme in glycolysis that catalyzes the
first step of the pathway by converting D-glyceraldehyde 3-
phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates
the organization and assembly of the cytoskeleton. Also
participates in nuclear events including transcription, RNA
transport, DNA replication and apoptosis. Nuclear functions are
probably due to the nitrosylase activity that mediates cysteine S-
nitrosylation of nuclear target proteins (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
{ECO:0000255|PROSITE-ProRule:PRU10009}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 1/5.
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
{ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
-!- PTM: S-nitrosylation of Cys-150 leads to translocation to the
nucleus. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
dehydrogenase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; K01458; AAA48778.1; -; mRNA.
EMBL; V00407; CAA23698.1; -; mRNA.
EMBL; M11213; AAA48774.1; -; Genomic_DNA.
EMBL; AF047874; AAD02474.1; -; mRNA.
EMBL; V00406; CAA23697.1; -; mRNA.
EMBL; X01578; CAA25733.1; -; mRNA.
PIR; A00368; DECHG3.
RefSeq; NP_989636.1; NM_204305.1.
UniGene; Gga.6383; -.
ProteinModelPortal; P00356; -.
SMR; P00356; -.
BioGrid; 675216; 2.
IntAct; P00356; 1.
STRING; 9031.ENSGALP00000036329; -.
Allergome; 12127; Gal d GAPDH.
PaxDb; P00356; -.
PRIDE; P00356; -.
Ensembl; ENSGALT00000023323; ENSGALP00000023278; ENSGALG00000014442.
Ensembl; ENSGALT00000054080; ENSGALP00000053969; ENSGALG00000014442.
Ensembl; ENSGALT00000086032; ENSGALP00000063325; ENSGALG00000014442.
GeneID; 374193; -.
KEGG; gga:374193; -.
CTD; 2597; -.
eggNOG; KOG0657; Eukaryota.
eggNOG; COG0057; LUCA.
GeneTree; ENSGT00760000119172; -.
HOGENOM; HOG000071678; -.
HOVERGEN; HBG000227; -.
InParanoid; P00356; -.
KO; K00134; -.
OrthoDB; EOG091G0B1Y; -.
PhylomeDB; P00356; -.
Reactome; R-GGA-352875; Gluconeogenesis.
Reactome; R-GGA-352882; Glycolysis.
Reactome; R-GGA-70171; Glycolysis.
Reactome; R-GGA-70263; Gluconeogenesis.
UniPathway; UPA00109; UER00184.
PRO; PR:P00356; -.
Proteomes; UP000000539; Chromosome 1.
Bgee; ENSGALG00000014442; -.
ExpressionAtlas; P00356; baseline and differential.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0097452; C:GAIT complex; IEA:Ensembl.
GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:AgBase.
GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0035605; F:peptidyl-cysteine S-nitrosylase activity; ISS:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IEA:Ensembl.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0050832; P:defense response to fungus; IEA:Ensembl.
GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
GO; GO:0006096; P:glycolytic process; TAS:Reactome.
GO; GO:0051873; P:killing by host of symbiont cells; IEA:Ensembl.
GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:AgBase.
GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
GO; GO:0000740; P:nuclear membrane fusion; IMP:AgBase.
GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISS:UniProtKB.
GO; GO:0052501; P:positive regulation by organism of apoptotic process in other organism involved in symbiotic interaction; IEA:Ensembl.
GO; GO:0050715; P:positive regulation of cytokine secretion; IEA:Ensembl.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
InterPro; IPR020830; GlycerAld_3-P_DH_AS.
InterPro; IPR020829; GlycerAld_3-P_DH_cat.
InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR10836; PTHR10836; 1.
Pfam; PF02800; Gp_dh_C; 1.
Pfam; PF00044; Gp_dh_N; 1.
PIRSF; PIRSF000149; GAP_DH; 1.
PRINTS; PR00078; G3PDHDRGNASE.
SMART; SM00846; Gp_dh_N; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01534; GAPDH-I; 1.
PROSITE; PS00071; GAPDH; 1.
2: Evidence at transcript level;
Apoptosis; Complete proteome; Cytoplasm; Cytoskeleton; Glycolysis;
NAD; Nucleus; Oxidoreductase; Reference proteome; S-nitrosylation;
Transferase.
INIT_MET 1 1 Removed.
CHAIN 2 333 Glyceraldehyde-3-phosphate dehydrogenase.
/FTId=PRO_0000145496.
NP_BIND 11 12 NAD. {ECO:0000250}.
REGION 149 151 Glyceraldehyde 3-phosphate binding.
{ECO:0000250}.
REGION 209 210 Glyceraldehyde 3-phosphate binding.
{ECO:0000250}.
ACT_SITE 150 150 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10009}.
BINDING 33 33 NAD. {ECO:0000250}.
BINDING 78 78 NAD; via carbonyl oxygen. {ECO:0000250}.
BINDING 180 180 Glyceraldehyde 3-phosphate.
{ECO:0000250}.
BINDING 232 232 Glyceraldehyde 3-phosphate.
{ECO:0000250}.
BINDING 314 314 NAD. {ECO:0000250}.
SITE 177 177 Activates thiol group during catalysis.
{ECO:0000250}.
MOD_RES 150 150 S-nitrosocysteine. {ECO:0000250}.
CONFLICT 2 2 V -> RSE (in Ref. 7; CAA25733).
{ECO:0000305}.
CONFLICT 145 145 V -> L (in Ref. 7; CAA25733).
{ECO:0000305}.
CONFLICT 197 197 G -> D (in Ref. 1; AAA48778, 2; CAA23698
and 3; AAA48774). {ECO:0000305}.
CONFLICT 277 277 D -> E (in Ref. 5; CAA23697).
{ECO:0000305}.
CONFLICT 294 294 D -> H (in Ref. 3; AAA48774).
{ECO:0000305}.
CONFLICT 329 329 M -> T (in Ref. 5; CAA23697).
{ECO:0000305}.
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


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