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G6PC3_RAT
ID   G6PC3_RAT               Reviewed;         346 AA.
AC   Q6AZ83; Q811R7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Glucose-6-phosphatase 3;
DE            Short=G-6-Pase 3;
DE            Short=G6Pase 3;
DE            EC=3.1.3.9;
GN   Name=G6pc3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Middleditch C., Darakhshan F., Guionie O., Bonnefont J., Burchell A.,
RA   Clottes E.;
RT   "Cloning of a glucose-6-phosphatase catalytic subunit-related sequence
RT   expressed in rodent tissues.";
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=17158265; DOI=10.1152/ajpregu.00566.2006;
RA   Azzout-Marniche D., Gaudichon C., Blouet C., Bos C., Mathe V.,
RA   Huneau J.-F., Tome D.;
RT   "Liver glyconeogenesis: a pathway to cope with postprandial amino acid
RT   excess in high-protein fed rats?";
RL   Am. J. Physiol. 292:R1400-R1407(2007).
CC   -!- FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic
CC       reticulum. May form with the glucose-6-phosphate transporter
CC       (SLC37A4/G6PT) a ubiquitously expressed complex responsible for glucose
CC       production through glycogenolysis and gluconeogenesis. Probably
CC       required for normal neutrophil function (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose 6-phosphate + H2O = D-glucose + phosphate;
CC         Xref=Rhea:RHEA:16689, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:61548; EC=3.1.3.9;
CC   -!- ACTIVITY REGULATION: Inhibited by vanadate. {ECO:0000250}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver and kidney. It is the major
CC       glucose-6-phosphatase expressed in the small intestine.
CC       {ECO:0000269|PubMed:17158265}.
CC   -!- INDUCTION: Up-regulated upon fasting. {ECO:0000269|PubMed:17158265}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphatase family. {ECO:0000305}.
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DR   EMBL; AY186240; AAO39165.1; -; mRNA.
DR   EMBL; BC078689; AAH78689.1; -; mRNA.
DR   RefSeq; NP_788266.2; NM_176077.3.
DR   AlphaFoldDB; Q6AZ83; -.
DR   SMR; Q6AZ83; -.
DR   STRING; 10116.ENSRNOP00000028375; -.
DR   PaxDb; Q6AZ83; -.
DR   Ensembl; ENSRNOT00000108412; ENSRNOP00000080695; ENSRNOG00000020902.
DR   GeneID; 303565; -.
DR   KEGG; rno:303565; -.
DR   UCSC; RGD:727875; rat.
DR   CTD; 92579; -.
DR   RGD; 727875; G6pc3.
DR   eggNOG; ENOG502QS5D; Eukaryota.
DR   GeneTree; ENSGT00950000183150; -.
DR   HOGENOM; CLU_052517_0_0_1; -.
DR   InParanoid; Q6AZ83; -.
DR   OMA; KKWCSRA; -.
DR   OrthoDB; 743717at2759; -.
DR   PhylomeDB; Q6AZ83; -.
DR   TreeFam; TF324388; -.
DR   Reactome; R-RNO-70263; Gluconeogenesis.
DR   UniPathway; UPA00138; -.
DR   PRO; PR:Q6AZ83; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000020902; Expressed in testis and 20 other tissues.
DR   Genevisible; Q6AZ83; RN.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0004346; F:glucose-6-phosphatase activity; IDA:RGD.
DR   GO; GO:0006094; P:gluconeogenesis; IDA:RGD.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IDA:RGD.
DR   GO; GO:0015760; P:glucose-6-phosphate transport; ISO:RGD.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; IDA:RGD.
DR   InterPro; IPR016275; Glucose-6-phosphatase.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Pfam; PF01569; PAP2; 1.
DR   PIRSF; PIRSF000905; Glucose-6-phosphatase; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Gluconeogenesis; Hydrolase; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..346
FT                   /note="Glucose-6-phosphatase 3"
FT                   /id="PRO_0000334514"
FT   TOPO_DOM        1..25
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..56
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..115
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..140
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..167
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..197
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        219..254
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        274..283
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        305..307
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..346
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        114
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        167
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        106
FT                   /note="T -> I (in Ref. 1; AAO39165)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   346 AA;  38834 MW;  59531F3030990F2F CRC64;
     MESTLSAGIM MAEALQNQLP GLENMWLWVT FLADPKNLFQ FYFPAVYYAS RRLGISLFWI
     AFITEWLNLV FKWFLFGDRP FWWVHESGYS AQTPVQIHQF PSSCETGPGS PSGHCMITGA
     ALWPVMIAIS SQVASQTRSP WVRVIPGLAY CTFLLAVGLS RVFLLAHFPH QVLAGLLAGV
     ILGWLLSPRV PMERELSFYG LTALTLMLGA SLMYWTLFTL GLDLSWSINL ASKWCDRPEW
     VLVDSRPFAS LSRDSGSALG LGIALHTPCY AQIRRVHLGN GQKIACFVLA MGLLVFLEWL
     GHPPQISLFY IFNFLKFTLW PCLVVALVPW MVHTLSAQEA PPIRSS
 
 
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