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G3P_DANRE
ID   G3P_DANRE               Reviewed;         333 AA.
AC   Q5XJ10; Q1RM54;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P00355};
DE            Short=GAPDH {ECO:0000250|UniProtKB:P00355};
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 {ECO:0000312|ZFIN:ZDB-GENE-030115-1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000312|EMBL:AAH83506.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH83506.2}, and
RC   Ovary {ECO:0000312|EMBL:AAI15132.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2006) 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 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. {ECO:0000250|UniProtKB:P00355}.
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:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI15132.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC083506; AAH83506.2; -; mRNA.
DR   EMBL; BC095386; AAH95386.2; -; mRNA.
DR   EMBL; BC115131; AAI15132.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001108586.1; NM_001115114.1.
DR   AlphaFoldDB; Q5XJ10; -.
DR   SMR; Q5XJ10; -.
DR   STRING; 7955.ENSDARP00000063799; -.
DR   PaxDb; Q5XJ10; -.
DR   PRIDE; Q5XJ10; -.
DR   Ensembl; ENSDART00000063800; ENSDARP00000063799; ENSDARG00000043457.
DR   Ensembl; ENSDART00000163606; ENSDARP00000134592; ENSDARG00000043457.
DR   GeneID; 317743; -.
DR   KEGG; dre:317743; -.
DR   CTD; 2597; -.
DR   ZFIN; ZDB-GENE-030115-1; gapdh.
DR   eggNOG; KOG0657; Eukaryota.
DR   GeneTree; ENSGT00940000153298; -.
DR   HOGENOM; CLU_030140_0_3_1; -.
DR   InParanoid; Q5XJ10; -.
DR   OrthoDB; 945145at2759; -.
DR   PhylomeDB; Q5XJ10; -.
DR   TreeFam; TF300533; -.
DR   Reactome; R-DRE-70171; Glycolysis.
DR   Reactome; R-DRE-70263; Gluconeogenesis.
DR   UniPathway; UPA00109; UER00184.
DR   PRO; PR:Q5XJ10; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 16.
DR   Bgee; ENSDARG00000043457; Expressed in muscle tissue and 36 other tissues.
DR   ExpressionAtlas; Q5XJ10; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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   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_0000382469"
FT   ACT_SITE        150
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P04406,
FT                   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        210
FT                   /note="G -> E (in Ref. 1; AAI15132)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        318
FT                   /note="Y -> H (in Ref. 1; AAI15132)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   333 AA;  35784 MW;  206FC71AA4774526 CRC64;
     MVKVGINGFG RIGRLVTRAA FLTKKVEIVA INDPFIDLDY MVYMFQYDST HGKYKGEVKA
     EGGKLVIDGH AITVYSERDP ANIKWGDAGA TYVVESTGVF TTIEKASAHI KGGAKRVIIS
     APSADAPMFV MGVNHEKYDN SLTVVSNASC TTNCLAPLAK VINDNFVIVE GLMSTVHAIT
     ATQKTVDGPS GKLWRDGRGA SQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV
     VDLTVRLEKP AKYDEIKKVV KAAADGPMKG ILGYTEHQVV STDFNGDCRS SIFDAGAGIA
     LNDHFVKLVT WYDNEFGYSN RVCDLMAHMA SKE
 
 
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