Database: UniProt
Entry: P00355
LinkDB: P00355
Original site: P00355 
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   22-NOV-2017, entry version 144.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE            Short=GAPDH;
DE            EC=;
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]
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]
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]
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]
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]
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]
RA   Foss D.L., Murtaugh M.P.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RX   PubMed=9241041; DOI=10.1095/biolreprod57.2.286;
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]
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). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC       {ECO:0000255|PROSITE-ProRule:PRU10009}.
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       Interacts with phosphorylated RPL13A (By similarity). Component of
CC       the GAIT complex. Interacts with FKBP6; leading to inhibit GAPDH
CC       catalytic activity (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P04406}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC       Note=Translocates to the nucleus following S-nitrosylation and
CC       interaction with SIAH1, which contains a nuclear localization
CC       signal. {ECO:0000250}.
CC   -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC       cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC       transnitrosylase complex. {ECO:0000250|UniProtKB:P04406}.
CC   -!- PTM: ISGylated. {ECO:0000250}.
CC   -!- PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1,
CC       followed by translocation to the nucleus. S-nitrosylation of Cys-
CC       245 is induced by interferon-gamma and LDL(ox) implicating the
CC       iNOS-S100A8/9 transnitrosylase complex and seems to prevent
CC       interaction with phosphorylated RPL13A and to interfere with GAIT
CC       complex activity (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P04406}.
CC   -!- PTM: Sulfhydration at Cys-150 increases catalytic activity.
CC       {ECO:0000250}.
CC   -!- PTM: Oxidative stress can promote the formation of high molecular
CC       weight disulfide-linked GAPDH aggregates, through a process called
CC       nucleocytoplasmic coagulation. {ECO:0000250|UniProtKB:P04406}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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   PDB; 5DDI; X-ray; 2.40 A; P/R/S=2-333.
DR   PDB; 5TSO; X-ray; 1.90 A; P/R/S=1-333.
DR   PDBsum; 5DDI; -.
DR   PDBsum; 5TSO; -.
DR   ProteinModelPortal; P00355; -.
DR   SMR; P00355; -.
DR   IntAct; P00355; 1.
DR   STRING; 9823.ENSSSCP00000000740; -.
DR   PeptideAtlas; P00355; -.
DR   PRIDE; P00355; -.
DR   Ensembl; ENSSSCT00000000756; ENSSSCP00000000740; ENSSSCG00000000694.
DR   GeneID; 396823; -.
DR   KEGG; ssc:396823; -.
DR   CTD; 2597; -.
DR   GeneTree; ENSGT00760000119172; -.
DR   HOVERGEN; HBG000227; -.
DR   InParanoid; P00355; -.
DR   KO; K00134; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0097452; C:GAIT complex; 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:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; 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   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   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ADP-ribosylation; Apoptosis;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Glycolysis; Isopeptide bond; Methylation; NAD; Nucleus;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; S-nitrosylation;
KW   Transferase; Translation regulation; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:1201027,
FT                                ECO:0000269|PubMed:4299800}.
FT   CHAIN         2    333       Glyceraldehyde-3-phosphate dehydrogenase.
FT                                /FTId=PRO_0000145491.
FT   NP_BIND      11     12       NAD. {ECO:0000250}.
FT   REGION        2    146       Interaction with WARS. {ECO:0000250}.
FT   REGION      149    151       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000250}.
FT   REGION      209    210       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000250}.
FT   MOTIF       243    248       [IL]-x-C-x-x-[DE] motif.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   ACT_SITE    150    150       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10009}.
FT   BINDING      33     33       NAD. {ECO:0000250}.
FT   BINDING      78     78       NAD; via carbonyl oxygen. {ECO:0000250}.
FT   BINDING     120    120       NAD. {ECO:0000250}.
FT   BINDING     180    180       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000250}.
FT   BINDING     232    232       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000250}.
FT   BINDING     314    314       NAD. {ECO:0000250}.
FT   SITE        177    177       Activates thiol group during catalysis.
FT                                {ECO:0000250}.
FT   MOD_RES       3      3       N6,N6-dimethyllysine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES       7      7       Deamidated asparagine. {ECO:0000250}.
FT   MOD_RES      40     40       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES      59     59       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES      62     62       Deamidated asparagine. {ECO:0000250}.
FT   MOD_RES      64     64       N6,N6-dimethyllysine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES      68     68       Deamidated asparagine. {ECO:0000250}.
FT   MOD_RES      73     73       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     120    120       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     146    146       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     147    147       Deamidated asparagine. {ECO:0000250}.
FT   MOD_RES     149    149       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     150    150       ADP-ribosylcysteine; by autocatalysis; in
FT                                irreversibly inhibited form.
FT                                {ECO:0000250}.
FT   MOD_RES     150    150       Cysteine persulfide. {ECO:0000250}.
FT   MOD_RES     150    150       S-nitrosocysteine; in reversibly
FT                                inhibited form.
FT                                {ECO:0000250|UniProtKB:P04797}.
FT   MOD_RES     151    151       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     153    153       Deamidated asparagine. {ECO:0000250}.
FT   MOD_RES     175    175       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     180    180       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     182    182       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     192    192       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     192    192       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     192    192       N6-malonyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES     209    209       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     213    213       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     213    213       N6-malonyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES     217    217       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     223    223       Deamidated asparagine. {ECO:0000250}.
FT   MOD_RES     225    225       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     225    225       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     227    227       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     235    235       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     239    239       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     245    245       S-nitrosocysteine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     252    252       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     258    258       N6,N6-dimethyllysine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     261    261       N6,N6-dimethyllysine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     310    310       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     314    314       Deamidated asparagine. {ECO:0000250}.
FT   MOD_RES     331    331       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   MOD_RES     332    332       N6,N6-dimethyllysine.
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   CROSSLNK    184    184       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P04406}.
FT   CONFLICT      7      7       N -> D (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     62     62       N -> D (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     68     68       N -> D (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     70     71       KA -> NP (in Ref. 1; AAB94053).
FT                                {ECO:0000305}.
FT   CONFLICT     82     82       N -> K (in Ref. 1; AAB94053).
FT                                {ECO:0000305}.
FT   CONFLICT     90     91       AT -> TA (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     91     91       T -> E (in Ref. 1; AAB94053).
FT                                {ECO:0000305}.
FT   CONFLICT    133    133       V -> M (in Ref. 1; AAB94053).
FT                                {ECO:0000305}.
FT   CONFLICT    145    145       V -> I (in Ref. 1; AAB94053).
FT                                {ECO:0000305}.
FT   CONFLICT    165    165       H -> N (in Ref. 1; AAB94053).
FT                                {ECO:0000305}.
FT   CONFLICT    201    201       A -> L (in Ref. 1; AAB94053).
FT                                {ECO:0000305}.
FT   CONFLICT    223    223       N -> D (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    236    236       P -> A (in Ref. 1; AAB94053).
FT                                {ECO:0000305}.
FT   CONFLICT    277    277       D -> H (in Ref. 1; AAB94053).
FT                                {ECO:0000305}.
FT   CONFLICT    282    282       C -> S (in Ref. 1; AAB94053).
FT                                {ECO:0000305}.
FT   CONFLICT    286    287       SD -> DS (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    311    311       W -> S (in Ref. 1; AAB94053).
FT                                {ECO:0000305}.
FT   CONFLICT    321    321       R -> W (in Ref. 7; AAB40155).
FT                                {ECO:0000305}.
FT   STRAND        3      7       {ECO:0000244|PDB:5TSO}.
FT   HELIX        11     23       {ECO:0000244|PDB:5TSO}.
FT   STRAND       25     32       {ECO:0000244|PDB:5TSO}.
FT   HELIX        38     46       {ECO:0000244|PDB:5TSO}.
FT   TURN         49     51       {ECO:0000244|PDB:5TSO}.
FT   STRAND       58     61       {ECO:0000244|PDB:5TSO}.
FT   STRAND       64     67       {ECO:0000244|PDB:5TSO}.
FT   STRAND       70     75       {ECO:0000244|PDB:5TSO}.
FT   HELIX        80     82       {ECO:0000244|PDB:5TSO}.
FT   HELIX        85     88       {ECO:0000244|PDB:5TSO}.
FT   STRAND       92     95       {ECO:0000244|PDB:5TSO}.
FT   STRAND       97     99       {ECO:0000244|PDB:5TSO}.
FT   HELIX       103    106       {ECO:0000244|PDB:5TSO}.
FT   HELIX       108    111       {ECO:0000244|PDB:5TSO}.
FT   STRAND      115    121       {ECO:0000244|PDB:5TSO}.
FT   STRAND      124    126       {ECO:0000244|PDB:5TSO}.
FT   TURN        131    133       {ECO:0000244|PDB:5TSO}.
FT   HELIX       135    137       {ECO:0000244|PDB:5TSO}.
FT   STRAND      143    146       {ECO:0000244|PDB:5TSO}.
FT   HELIX       150    166       {ECO:0000244|PDB:5TSO}.
FT   STRAND      168    177       {ECO:0000244|PDB:5TSO}.
FT   STRAND      183    187       {ECO:0000244|PDB:5TSO}.
FT   HELIX       194    197       {ECO:0000244|PDB:5TSO}.
FT   TURN        200    202       {ECO:0000244|PDB:5TSO}.
FT   STRAND      205    207       {ECO:0000244|PDB:5TSO}.
FT   HELIX       211    218       {ECO:0000244|PDB:5TSO}.
FT   HELIX       220    222       {ECO:0000244|PDB:5TSO}.
FT   TURN        223    225       {ECO:0000244|PDB:5TSO}.
FT   STRAND      226    232       {ECO:0000244|PDB:5TSO}.
FT   STRAND      239    249       {ECO:0000244|PDB:5TSO}.
FT   HELIX       253    265       {ECO:0000244|PDB:5TSO}.
FT   TURN        266    271       {ECO:0000244|PDB:5TSO}.
FT   STRAND      272    275       {ECO:0000244|PDB:5TSO}.
FT   HELIX       281    284       {ECO:0000244|PDB:5TSO}.
FT   STRAND      290    294       {ECO:0000244|PDB:5TSO}.
FT   TURN        295    297       {ECO:0000244|PDB:5TSO}.
FT   STRAND      299    302       {ECO:0000244|PDB:5TSO}.
FT   STRAND      305    312       {ECO:0000244|PDB:5TSO}.
FT   HELIX       316    332       {ECO:0000244|PDB:5TSO}.
SQ   SEQUENCE   333 AA;  35836 MW;  5F29175285D897BB CRC64;
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