ID G3P_PIG Reviewed; 333 AA.
AC P00355; O18816; P79299; P79317; Q29546;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-APR-2013, entry version 116.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12;
DE AltName: Full=Peptidyl-cysteine S-nitrosylase GAPDH;
DE EC=2.6.99.-;
GN Name=GAPDH; Synonyms=GAPD;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Behdjani R., Silversides D.W.;
RT "Sus scrofa glyceraldehyde-3-phosphate dehydrogenase, genomic and cDNA
RT sequences.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-126.
RC TISSUE=Small intestine;
RA Winteroe A.K., Fredholm M.;
RT "Evaluation and characterization of a porcine small intestine cDNA
RT library.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-333.
RX PubMed=4299800; DOI=10.1038/2191025a0;
RA Harris J.I., Perham R.N.;
RT "Glyceraldehyde 3-phosphate dehydrogenase from pig muscle.";
RL Nature 219:1025-1028(1968).
RN [4]
RP SEQUENCE REVISION TO 46.
RA Harris J.I., Davidson B.E., Sajgo M., Noller H.F., Perham R.N.;
RL (In) Shugar D. (eds.);
RL Enzymes and isoenzymes: structure, properties and function, pp.1-15,
RL Academic Press, London and New York (1970).
RN [5]
RP PROTEIN SEQUENCE OF 2-23.
RC TISSUE=Liver;
RX PubMed=1201027; DOI=10.1016/0006-291X(75)90279-X;
RA Kulbe K.D., Jackson K.W., Tang J.;
RT "Structural evidence for a liver-specific glyceraldehyde-3-phosphate
RT dehydrogenase.";
RL Biochem. Biophys. Res. Commun. 67:35-42(1975).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-301.
RA Foss D.L., Murtaugh M.P.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 174-323.
RX PubMed=9241041;
RA Yelich J.V., Pomp D., Geisert R.D.;
RT "Detection of transcripts for retinoic acid receptors, retinol-binding
RT protein, and transforming growth factors during rapid trophoblastic
RT elongation in the porcine conceptus.";
RL Biol. Reprod. 57:286-294(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 299-333.
RC TISSUE=Skeletal muscle;
RA Davoli R., Zambonelli P., Fontanesi L., Bigi D., Costosi E., Russo V.;
RT "Isolation and characterization of cDNA clones coding for porcine
RT muscle proteins.";
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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
CC first step of the pathway by converting D-glyceraldehyde 3-
CC phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates
CC the organization and assembly of the cytoskeleton. Facilitates the
CC CHP1-dependent microtubule and membrane associations through its
CC ability to stimulate the binding of CHP1 to microtubules. Also
CC participates in nuclear events including transcription, RNA
CC transport, DNA replication and apoptosis. Nuclear functions are
CC probably due to the nitrosylase activity that mediates cysteine S-
CC nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and
CC PRKDC. Component of the GAIT (gamma interferon-activated inhibitor
CC of translation) complex which mediates interferon-gamma-induced
CC transcript-selective translation inhibition in inflammation
CC processes. Upon interferon-gamma treatment assembles into the GAIT
CC complex which binds to stem loop-containing GAIT elements in the
CC 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and
CC suppresses their translation (By similarity).
CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. Interacts with EIF1AD, USP25, PRKCI and
CC WARS. Interacts with TPPP; the interaction is direct. Interacts
CC (when S-nitrosylated) with SIAH1; leading to nuclear
CC translocation. Interacts with RILPL1/GOSPEL, leading to prevent
CC the interaction between GAPDH and SIAH1 and prevent nuclear
CC translocation. Interacts with CHP1; the interaction increases the
CC binding of CHP1 with microtubules. Associates with microtubules.
CC Component of the GAIT complex (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). Nucleus
CC (By similarity). Cytoplasm, cytoskeleton (By similarity).
CC Note=Translocates to the nucleus following S-nitrosylation and
CC interaction with SIAH1, which contains a nuclear localization
CC signal (By similarity).
CC -!- PTM: ISGylated (By similarity).
CC -!- PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1,
CC followed by translocation to the nucleus (By similarity).
CC -!- PTM: Sulfhydration at Cys-150 increases catalytic activity (By
CC similarity).
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC dehydrogenase family.
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DR EMBL; AF017079; AAB94053.1; -; mRNA.
DR EMBL; Z84063; CAB06323.1; -; mRNA.
DR EMBL; U48832; AAA91804.1; -; mRNA.
DR EMBL; U82261; AAB40155.1; -; mRNA.
DR EMBL; X94251; CAA63935.1; -; mRNA.
DR PIR; B12055; B12055.
DR RefSeq; NP_001193288.1; NM_001206359.1.
DR UniGene; Ssc.16135; -.
DR UniGene; Ssc.79971; -.
DR ProteinModelPortal; P00355; -.
DR SMR; P00355; 2-333.
DR PaxDb; P00355; -.
DR PRIDE; P00355; -.
DR GeneID; 396823; -.
DR KEGG; ssc:396823; -.
DR CTD; 2597; -.
DR eggNOG; COG0057; -.
DR HOVERGEN; HBG000227; -.
DR KO; K00134; -.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB.
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:0006096; P:glycolysis; IEA:UniProtKB-UniPathway.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; -; 1.
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; IPR016040; NAD(P)-bd_dom.
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 TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; Apoptosis; Complete proteome;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycolysis;
KW Methylation; NAD; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; S-nitrosylation; Transferase;
KW Translation regulation; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 333 Glyceraldehyde-3-phosphate dehydrogenase.
FT /FTId=PRO_0000145491.
FT NP_BIND 11 12 NAD (By similarity).
FT REGION 2 146 Interaction with WARS (By similarity).
FT REGION 149 151 Glyceraldehyde 3-phosphate binding (By
FT similarity).
FT REGION 209 210 Glyceraldehyde 3-phosphate binding (By
FT similarity).
FT ACT_SITE 150 150 Nucleophile (By similarity).
FT BINDING 33 33 NAD (By similarity).
FT BINDING 78 78 NAD; via carbonyl oxygen (By similarity).
FT BINDING 120 120 NAD (By similarity).
FT BINDING 180 180 Glyceraldehyde 3-phosphate (By
FT similarity).
FT BINDING 232 232 Glyceraldehyde 3-phosphate (By
FT similarity).
FT BINDING 314 314 NAD (By similarity).
FT SITE 177 177 Activates thiol group during catalysis
FT (By similarity).
FT MOD_RES 3 3 N6,N6-dimethyllysine (By similarity).
FT MOD_RES 7 7 Deamidated asparagine (By similarity).
FT MOD_RES 40 40 Phosphotyrosine (By similarity).
FT MOD_RES 59 59 N6-acetyllysine (By similarity).
FT MOD_RES 62 62 Deamidated asparagine (By similarity).
FT MOD_RES 64 64 N6,N6-dimethyllysine (By similarity).
FT MOD_RES 68 68 Deamidated asparagine (By similarity).
FT MOD_RES 73 73 Phosphothreonine (By similarity).
FT MOD_RES 120 120 Phosphoserine (By similarity).
FT MOD_RES 146 146 Phosphoserine (By similarity).
FT MOD_RES 147 147 Deamidated asparagine (By similarity).
FT MOD_RES 149 149 Phosphoserine (By similarity).
FT MOD_RES 150 150 ADP-ribosylcysteine; by autocatalysis; in
FT irreversibly inhibited form (By
FT similarity).
FT MOD_RES 150 150 Cysteine persulfide (By similarity).
FT MOD_RES 150 150 S-nitrosocysteine; in reversibly
FT inhibited form (By similarity).
FT MOD_RES 153 153 Deamidated asparagine (By similarity).
FT MOD_RES 182 182 Phosphothreonine (By similarity).
FT MOD_RES 192 192 N6,N6-dimethyllysine; alternate (By
FT similarity).
FT MOD_RES 192 192 N6-acetyllysine (By similarity).
FT MOD_RES 192 192 N6-malonyllysine; alternate (By
FT similarity).
FT MOD_RES 209 209 Phosphothreonine (By similarity).
FT MOD_RES 213 213 N6,N6-dimethyllysine; alternate (By
FT similarity).
FT MOD_RES 213 213 N6-malonyllysine; alternate (By
FT similarity).
FT MOD_RES 217 217 N6-acetyllysine (By similarity).
FT MOD_RES 223 223 Deamidated asparagine (By similarity).
FT MOD_RES 225 225 N6,N6-dimethyllysine; alternate (By
FT similarity).
FT MOD_RES 225 225 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 227 227 Phosphothreonine (By similarity).
FT MOD_RES 235 235 Phosphothreonine (By similarity).
FT MOD_RES 252 252 N6-acetyllysine (By similarity).
FT MOD_RES 258 258 N6,N6-dimethyllysine (By similarity).
FT MOD_RES 261 261 N6,N6-dimethyllysine (By similarity).
FT MOD_RES 310 310 Phosphoserine (By similarity).
FT MOD_RES 312 312 Phosphotyrosine (By similarity).
FT MOD_RES 314 314 Deamidated asparagine (By similarity).
FT MOD_RES 318 318 Phosphotyrosine (By similarity).
FT MOD_RES 332 332 N6,N6-dimethyllysine (By similarity).
FT CONFLICT 7 7 N -> D (in Ref. 3; AA sequence).
FT CONFLICT 62 62 N -> D (in Ref. 3; AA sequence).
FT CONFLICT 68 68 N -> D (in Ref. 3; AA sequence).
FT CONFLICT 70 71 KA -> NP (in Ref. 1; AAB94053).
FT CONFLICT 82 82 N -> K (in Ref. 1; AAB94053).
FT CONFLICT 90 91 AT -> TA (in Ref. 3; AA sequence).
FT CONFLICT 91 91 T -> E (in Ref. 1; AAB94053).
FT CONFLICT 133 133 V -> M (in Ref. 1; AAB94053).
FT CONFLICT 145 145 V -> I (in Ref. 1; AAB94053).
FT CONFLICT 165 165 H -> N (in Ref. 1; AAB94053).
FT CONFLICT 201 201 A -> L (in Ref. 1; AAB94053).
FT CONFLICT 223 223 N -> D (in Ref. 3; AA sequence).
FT CONFLICT 236 236 P -> A (in Ref. 1; AAB94053).
FT CONFLICT 277 277 D -> H (in Ref. 1; AAB94053).
FT CONFLICT 282 282 C -> S (in Ref. 1; AAB94053).
FT CONFLICT 286 287 SD -> DS (in Ref. 3; AA sequence).
FT CONFLICT 311 311 W -> S (in Ref. 1; AAB94053).
FT CONFLICT 321 321 R -> W (in Ref. 7; AAB40155).
SQ SEQUENCE 333 AA; 35836 MW; 5F29175285D897BB CRC64;
MVKVGVNGFG RIGRLVTRAA FNSGKVDIVA INDPFIDLHY MVYMFQYDST HGKFHGTVKA
ENGKLVINGK AITIFQERDP ANIKWGDAGA TYVVESTGVF TTMEKAGAHL KGGAKRVIIS
APSADAPMFV MGVNHEKYDN SLKIVSNASC TTNCLAPLAK VIHDHFGIVE GLMTTVHAIT
ATQKTVDGPS GKLWRDGRGA AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV
VDLTCRLEKP AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSDTHS STFDAGAGIA
LNDHFVKLIS WYDNEFGYSN RVVDLMVHMA SKE
//
