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G3P_MUSPF
ID   G3P_MUSPF               Reviewed;         333 AA.
AC   A3FKF7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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;
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC   Mustela.
OX   NCBI_TaxID=9669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=17289104; DOI=10.1016/j.virol.2007.01.002;
RA   Svitek N., von Messling V.;
RT   "Early cytokine mRNA expression profiles predict Morbillivirus disease
RT   outcome in ferrets.";
RL   Virology 362:404-410(2007).
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). Modulates the
CC       organization and assembly of the cytoskeleton. Facilitates the CHP1-
CC       dependent microtubule and membrane associations through its ability to
CC       stimulate the binding of CHP1 to microtubules (By similarity).
CC       Component of the GAIT (gamma interferon-activated inhibitor of
CC       translation) complex which mediates interferon-gamma-induced
CC       transcript-selective translation inhibition in inflammation processes.
CC       Upon interferon-gamma treatment assembles into the GAIT complex which
CC       binds to stem loop-containing GAIT elements in the 3'-UTR of diverse
CC       inflammatory mRNAs (such as ceruplasmin) and suppresses their
CC       translation. Also plays a role in innate immunity by promoting TNF-
CC       induced NF-kappa-B activation and type I interferon production, via
CC       interaction with TRAF2 and TRAF3, respectively (By similarity).
CC       Participates in nuclear events including transcription, RNA transport,
CC       DNA replication and apoptosis. Nuclear functions are probably due to
CC       the nitrosylase activity that mediates cysteine S-nitrosylation of
CC       nuclear target 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   -!- ACTIVITY REGULATION: Glyceraldehyde-3-phosphate dehydrogenase activity
CC       is inhibited by fumarate, via the formation of S-(2-succinyl)cysteine
CC       residues. {ECO:0000250|UniProtKB:P04797}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC   -!- SUBUNIT: Homotetramer (By similarity). Interacts with TPPP; the
CC       interaction is direct (By similarity). Interacts (when S-nitrosylated)
CC       with SIAH1; leading to nuclear translocation. Interacts with
CC       RILPL1/GOSPEL, leading to prevent the interaction between GAPDH and
CC       SIAH1 and prevent nuclear translocation. Interacts with CHP1; the
CC       interaction increases the binding of CHP1 with microtubules. Associates
CC       with microtubules (By similarity). Interacts with EIF1AD, USP25, PRKCI
CC       and WARS1. Interacts with phosphorylated RPL13A; inhibited by
CC       oxidatively-modified low-densitity lipoprotein (LDL(ox)). Component of
CC       the GAIT complex. Interacts with FKBP6; leading to inhibit GAPDH
CC       catalytic activity. Interacts with TRAF2, promoting TRAF2
CC       ubiquitination. Interacts with TRAF3, promoting TRAF3 ubiquitination
CC       (By similarity). {ECO:0000250|UniProtKB:P04406,
CC       ECO:0000250|UniProtKB:P04797, ECO:0000250|UniProtKB:P10096}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}.
CC       Note=Translocates to the nucleus following S-nitrosylation and
CC       interaction with SIAH1, which contains a nuclear localization signal.
CC       Colocalizes with CHP1 to small punctate structures along the
CC       microtubules tracks. {ECO:0000250|UniProtKB:P04797}.
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|UniProtKB:P04406}.
CC   -!- PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1,
CC       followed by translocation to the nucleus S-nitrosylation of Cys-245 is
CC       induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9
CC       transnitrosylase complex and seems to prevent interaction with
CC       phosphorylated RPL13A and to interfere with GAIT complex activity (By
CC       similarity). {ECO:0000250|UniProtKB:P04406,
CC       ECO:0000250|UniProtKB:P04797}.
CC   -!- PTM: Sulfhydration at Cys-150 increases catalytic activity.
CC       {ECO:0000250|UniProtKB:P16858}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; EF392835; ABN54800.1; -; mRNA.
DR   RefSeq; NP_001297102.1; NM_001310173.1.
DR   AlphaFoldDB; A3FKF7; -.
DR   SMR; A3FKF7; -.
DR   STRING; 9668.ENSMPUP00000016786; -.
DR   GeneID; 101694263; -.
DR   eggNOG; KOG0657; Eukaryota.
DR   InParanoid; A3FKF7; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000000715; Unassembled WGS sequence.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
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: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   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   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   Acetylation; ADP-ribosylation; Apoptosis; Cytoplasm; Cytoskeleton;
KW   Glycolysis; Immunity; Innate immunity; Isopeptide bond; Methylation; NAD;
KW   Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   S-nitrosylation; Transferase; Translation regulation; Ubl conjugation.
FT   CHAIN           1..333
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT                   /id="PRO_0000310944"
FT   REGION          1..146
FT                   /note="Interaction with WARS1"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOTIF           243..248
FT                   /note="[IL]-x-C-x-x-[DE] motif"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
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         3
FT                   /note="N6,N6-dimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         7
FT                   /note="Deamidated asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         40
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         59
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         62
FT                   /note="Deamidated asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         64
FT                   /note="N6,N6-dimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         68
FT                   /note="Deamidated asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         147
FT                   /note="Deamidated asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         150
FT                   /note="ADP-ribosylcysteine; by autocatalysis; in
FT                   irreversibly inhibited form"
FT                   /evidence="ECO:0000250|UniProtKB:P04797"
FT   MOD_RES         150
FT                   /note="Cysteine persulfide"
FT                   /evidence="ECO:0000250|UniProtKB:P16858"
FT   MOD_RES         150
FT                   /note="S-(2-succinyl)cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P04797"
FT   MOD_RES         150
FT                   /note="S-nitrosocysteine; in reversibly inhibited form"
FT                   /evidence="ECO:0000250|UniProtKB:P04797"
FT   MOD_RES         151
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         153
FT                   /note="Deamidated asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         175
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         180
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         182
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         192
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         192
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         192
FT                   /note="N6-malonyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         209
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         213
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         213
FT                   /note="N6-malonyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         217
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         223
FT                   /note="Deamidated asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         225
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         225
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         227
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         235
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         239
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         245
FT                   /note="S-(2-succinyl)cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P04797"
FT   MOD_RES         245
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         252
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         258
FT                   /note="N6,N6-dimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         261
FT                   /note="N6,N6-dimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         310
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         314
FT                   /note="Deamidated asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         331
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         332
FT                   /note="N6,N6-dimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   CROSSLNK        184
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
SQ   SEQUENCE   333 AA;  35820 MW;  28932F1234CA814C CRC64;
     MVKVGVNGFG RIGRLVTRAA FNSGKVDIVA INDPFIDLNY MVYMFQYDST HGKFHGTVKA
     ENGKLVINGK SISIFQERDP ANIKWGDAGA EYVVESTGVF TTMEKAGAHL KGGAKRVIIS
     APSADAPMFV MGVNHEKYDN SLKIVSNASC TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT
     ATQKTVDGPS GKLWRDGRGA AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV
     VDLTCRLEKA AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSDTHS STFDAGAGIA
     LNDHFVKLIS WYDNEFGYSN RVVDLMVYMA SKE
 
 
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