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NUDT6_RAT
ID   NUDT6_RAT               Reviewed;         313 AA.
AC   P70563; Q9QZD7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Nucleoside diphosphate-linked moiety X motif 6;
DE            Short=Nudix motif 6;
DE            EC=3.6.1.-;
DE   AltName: Full=Protein GFG;
GN   Name=Nudt6;
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] (ISOFORM 1).
RC   STRAIN=Sprague-Dawley;
RA   Knee R.S., Li A.W., Murphy P.R.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=10854699; DOI=10.1016/s0303-7207(00)00209-4;
RA   Li A.W., Murphy P.R.;
RT   "Expression of alternatively spliced FGF-2 antisense RNA transcripts in the
RT   central nervous system: regulation of FGF-2 mRNA translation.";
RL   Mol. Cell. Endocrinol. 162:69-78(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=8660369; DOI=10.1006/bbrc.1996.0839;
RA   Li A.W., Too C.K., Murphy P.R.;
RT   "The basic fibroblast growth factor (FGF-2) antisense RNA (GFG) is
RT   translated into a MutT-related protein in vivo.";
RL   Biochem. Biophys. Res. Commun. 223:19-23(1996).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=9406864; DOI=10.1016/s0303-7207(97)00148-2;
RA   Li A.W., Too C.K., Knee R., Wilkinson M., Murphy P.R.;
RT   "FGF-2 antisense RNA encodes a nuclear protein with MutT-like antimutator
RT   activity.";
RL   Mol. Cell. Endocrinol. 133:177-182(1997).
RN   [6]
RP   ABSENCE OF ANTI-MUTATOR FUNCTION IN DNA REPAIR.
RX   PubMed=17569023; DOI=10.1007/s00109-007-0219-9;
RA   Zhang S.C., Barclay C., Alexander L.A., Geldenhuys L., Porter G.A.,
RA   Casson A.G., Murphy P.R.;
RT   "Alternative splicing of the FGF antisense gene: differential subcellular
RT   localization in human tissues and esophageal adenocarcinoma.";
RL   J. Mol. Med. 85:1215-1228(2007).
RN   [7]
RP   ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=18215310; DOI=10.1186/1471-2199-9-10;
RA   Zhang S.C., MacDonald K.A., Baguma-Nibasheka M., Geldenhuys L.,
RA   Casson A.G., Murphy P.R.;
RT   "Alternative splicing and differential subcellular localization of the rat
RT   FGF antisense gene product.";
RL   BMC Mol. Biol. 9:10-10(2008).
CC   -!- FUNCTION: May contribute to the regulation of cell proliferation.
CC       {ECO:0000269|PubMed:10854699, ECO:0000269|PubMed:9406864}.
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Mitochondrion. Cytoplasm.
CC       Note=Subcellular location depends on the isoform.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1; Synonyms=Full length;
CC         IsoId=P70563-1; Sequence=Displayed;
CC       Name=2; Synonyms=1;
CC         IsoId=P70563-2; Sequence=VSP_038852;
CC   -!- TISSUE SPECIFICITY: Detected in liver and in brain (at protein level).
CC       Detected in liver, spleen, lung, brain, hypothalamus, cerebellum,
CC       pituitary, heart and skeletal muscle. {ECO:0000269|PubMed:10854699,
CC       ECO:0000269|PubMed:18215310, ECO:0000269|PubMed:8660369,
CC       ECO:0000269|PubMed:9406864}.
CC   -!- MISCELLANEOUS: This protein is coded from a FGF2 (BFGF) gene antisense
CC       transcript.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC   -!- CAUTION: The rat protein was reported to play a role in DNA repair
CC       (PubMed:9406864), based on its ability to complement E.coli deficient
CC       in the DNA repair enzyme mutT that hydrolyzes oxidized guanine
CC       nucleotides. PubMed:17569023 found no such activity, neither for the
CC       human nor the rat protein. {ECO:0000305|PubMed:9406864}.
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DR   EMBL; U58289; AAB58250.1; -; mRNA.
DR   EMBL; AF188995; AAF07934.1; -; mRNA.
DR   EMBL; CH473961; EDM01306.1; -; Genomic_DNA.
DR   RefSeq; NP_852028.1; NM_181363.2. [P70563-1]
DR   AlphaFoldDB; P70563; -.
DR   SMR; P70563; -.
DR   STRING; 10116.ENSRNOP00000023437; -.
DR   iPTMnet; P70563; -.
DR   PhosphoSitePlus; P70563; -.
DR   PaxDb; P70563; -.
DR   PRIDE; P70563; -.
DR   Ensembl; ENSRNOT00000023448; ENSRNOP00000023448; ENSRNOG00000017420. [P70563-2]
DR   GeneID; 207120; -.
DR   KEGG; rno:207120; -.
DR   UCSC; RGD:621356; rat. [P70563-1]
DR   CTD; 11162; -.
DR   RGD; 621356; Nudt6.
DR   VEuPathDB; HostDB:ENSRNOG00000017420; -.
DR   eggNOG; KOG0648; Eukaryota.
DR   GeneTree; ENSGT00390000008458; -.
DR   HOGENOM; CLU_054299_4_0_1; -.
DR   InParanoid; P70563; -.
DR   OMA; CTFVARL; -.
DR   OrthoDB; 835461at2759; -.
DR   PhylomeDB; P70563; -.
DR   TreeFam; TF106346; -.
DR   PRO; PR:P70563; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Proteomes; UP000234681; Chromosome 2.
DR   Bgee; ENSRNOG00000017420; Expressed in pancreas and 19 other tissues.
DR   ExpressionAtlas; P70563; baseline and differential.
DR   Genevisible; P70563; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0047631; F:ADP-ribose diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; IBA:GO_Central.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; IBA:GO_Central.
DR   GO; GO:0045786; P:negative regulation of cell cycle; ISO:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR003293; Nudix_hydrolase6-like.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR040618; Pre-Nudix.
DR   PANTHER; PTHR13994; PTHR13994; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   Pfam; PF18290; Nudix_hydro; 1.
DR   PRINTS; PR01356; GFGPROTEIN.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Hydrolase; Mitochondrion; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..313
FT                   /note="Nucleoside diphosphate-linked moiety X motif 6"
FT                   /id="PRO_0000057109"
FT   DOMAIN          138..270
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           173..194
FT                   /note="Nudix box"
FT   VAR_SEQ         77..144
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10854699, ECO:0000303|Ref.1"
FT                   /id="VSP_038852"
SQ   SEQUENCE   313 AA;  35292 MW;  5535FB573DCDC598 CRC64;
     MWWASRARWL FSALLDVGGV GLRARRRTAS SGLEITGSCG GELQGELDRF GGISVHLSRH
     RTLHRLDAAA FRRLLQAAIQ QWRAEGRIAA WLHIPILQSH FIAPAASLGF CFHHAEPHLS
     TLTLWLGEGP SRLPGYATHQ VGVAGAVFDV STRKVLVVQD RNKLKNMWKF PGGLSEPGED
     IGDTAVREVF EETGVKSEFR SLLSIRQQHR SPGAFGMSDM YLICRLQPRS FTINFCQQEC
     LKCEWMDLES LARTKHTTPI TSRVARLLLY GHREGFDKID LSMEELPAVY TGLFYKLYHR
     GLPERYKAEM GTD
 
 
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