(data stored in ACNUC4932 zone)

HOVERGEN: F264_MOUSE

ID   F264_MOUSE              Reviewed;         469 AA.
AC   Q6DTY7; Q5UD55; Q5UD56; Q5UD57; Q5Y296; Q6PFE8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-NOV-2009, entry version 45.
DE   RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4;
DE   AltName: Full=6PF-2-K/Fru-2,6-P2ASE testis-type isozyme;
DE   Includes:
DE     RecName: Full=6-phosphofructo-2-kinase;
DE              EC=2.7.1.105;
DE   Includes:
DE     RecName: Full=Fructose-2,6-bisphosphatase;
DE              EC=3.1.3.46;
GN   Name=Pfkfb4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Testis;
RX   PubMed=14623077; DOI=10.1016/S0014-5793(03)01179-7;
RA   Minchenko O.H., Opentanova I.L., Caro J.;
RT   "Hypoxic regulation of the 6-phosphofructo-2-kinase/fructose-2,6-
RT   bisphosphatase gene family (PFKFB-1-4) expression in vivo.";
RL   FEBS Lett. 554:264-270(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RC   STRAIN=C57BL/6; TISSUE=Testis;
RX   PubMed=16311927; DOI=10.1007/s11010-005-8009-6;
RA   Minchenko O.H., Ogura T., Opentanova I.L., Minchenko D.O., Esumi H.;
RT   "Splice isoform of 6-phosphofructo-2-kinase/fructose-2,6-
RT   bisphosphatase-4: expression and hypoxic regulation.";
RL   Mol. Cell. Biochem. 280:227-234(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
RC   STRAIN=C57BL/6; TISSUE=Testis;
RA   Minchenko D.O., Opentanova I.L., Minchenko O.H.;
RT   "Alternative splice isoforms of mouse 6-phosphofructo-2-
RT   kinase/fructose-2,6-biphosphatase 4.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   STRAIN=C57BL/6; TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Beta-D-fructose 2,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + beta-D-
CC       fructose 2,6-bisphosphate.
CC   -!- ENZYME REGULATION: The most important regulatory mechanism of
CC       these opposing activities is by phosphorylation and
CC       dephosphorylation of the enzyme (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q6DTY7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6DTY7-2; Sequence=VSP_021959;
CC       Name=3;
CC         IsoId=Q6DTY7-3; Sequence=VSP_021964;
CC       Name=4;
CC         IsoId=Q6DTY7-4; Sequence=VSP_021962, VSP_021963;
CC       Name=5;
CC         IsoId=Q6DTY7-5; Sequence=VSP_021961;
CC       Name=6;
CC         IsoId=Q6DTY7-6; Sequence=VSP_021960;
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       phosphoglycerate mutase family.
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CC   -!- GENE_FAMILY: HBG005628 [ FAMILY / ALN / TREE ]
DR   EMBL; AY646092; AAT72897.2; -; mRNA.
DR   EMBL; AY707862; AAU88258.1; -; mRNA.
DR   EMBL; DQ350638; ABC71307.1; -; mRNA.
DR   EMBL; AY756065; AAV32501.1; -; mRNA.
DR   EMBL; AY756066; AAV32502.1; -; mRNA.
DR   EMBL; AY756067; AAV32503.1; -; mRNA.
DR   EMBL; AK155172; BAE33093.1; -; mRNA.
DR   EMBL; BC057594; AAH57594.1; -; mRNA.
DR   IPI; IPI00465760; -.
DR   IPI; IPI00720247; -.
DR   IPI; IPI00816846; -.
DR   IPI; IPI00816868; -.
DR   IPI; IPI00816913; -.
DR   IPI; IPI00817003; -.
DR   RefSeq; NP_766607.3; -.
DR   UniGene; Mm.132391; -.
DR   SMR; Q6DTY7; 38-469.
DR   STRING; Q6DTY7; -.
DR   PhosphoSite; Q6DTY7; -.
DR   PRIDE; Q6DTY7; -.
DR   Ensembl; ENSMUST00000051873; ENSMUSP00000057197; ENSMUSG00000025648; Mus musculus.
DR   Ensembl; ENSMUST00000098369; ENSMUSP00000095971; ENSMUSG00000025648; Mus musculus.
DR   GeneID; 270198; -.
DR   KEGG; mmu:270198; -.
DR   UCSC; uc009rri.1; mouse.
DR   UCSC; uc009rrk.1; mouse.
DR   UCSC; uc009rrl.1; mouse.
DR   CTD; 270198; -.
DR   MGI; MGI:2687284; Pfkfb4.
DR   HOVERGEN; Q6DTY7; -.
DR   OMA; SYETLDE; -.
DR   BRENDA; 2.7.1.105; 244.
DR   BRENDA; 3.1.3.46; 244.
DR   NextBio; 393301; -.
DR   ArrayExpress; Q6DTY7; -.
DR   Bgee; Q6DTY7; -.
DR   Genevestigator; Q6DTY7; -.
DR   GermOnline; ENSMUSG00000025648; Mus musculus.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase act...; IEA:EC.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR016260; Bifunct_6PFK/fruc_bisP_Ptase.
DR   InterPro; IPR001345; PG/BPGM_mutase_AC.
DR   InterPro; IPR013078; PG_mutase.
DR   PANTHER; PTHR10606; 6Pfruct_kin; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; PGAM; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR   PRINTS; PR00991; 6PFRUCTKNASE.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q6DTY7.
DR   SWISS-2DPAGE; Q6DTY7.
KW   Alternative splicing; ATP-binding; Hydrolase; Kinase;
KW   Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW   Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    469       6-phosphofructo-2-kinase/fructose-2,6-
FT                                biphosphatase 4.
FT                                /FTId=PRO_0000268187.
FT   NP_BIND      46     53       ATP (Potential).
FT   REGION        2    249       6-phosphofructo-2-kinase.
FT   REGION      250    469       Fructose-2,6-bisphosphatase.
FT   ACT_SITE    129    129       Potential.
FT   ACT_SITE    159    159       Potential.
FT   ACT_SITE    257    257       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    326    326       Potential.
FT   ACT_SITE    391    391       Proton donor (By similarity).
FT   BINDING     103    103       Fructose-6-phosphate (By similarity).
FT   BINDING     194    194       Fructose-6-phosphate (By similarity).
FT   MOD_RES      29     29       Phosphoserine; by PKC (Potential).
FT   MOD_RES     444    444       Phosphothreonine; by PKC (Potential).
FT   VAR_SEQ       1    218       Missing (in isoform 2).
FT                                /FTId=VSP_021959.
FT   VAR_SEQ       1     34       Missing (in isoform 6).
FT                                /FTId=VSP_021960.
FT   VAR_SEQ      33     48       Missing (in isoform 5).
FT                                /FTId=VSP_021961.
FT   VAR_SEQ     212    221       DLSYIKIMDV -> SSGQSRRLFS (in isoform 4).
FT                                /FTId=VSP_021962.
FT   VAR_SEQ     222    469       Missing (in isoform 4).
FT                                /FTId=VSP_021963.
FT   VAR_SEQ     358    469       YRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCL
FT                                LAYFLDKAAEELPYLKCPLHTVLKLTPVAYGCKVESIFLNV
FT                                AAVNTHRDRPQNVDISRPSEEALVTVPAHQ -> PMKTWCS
FT                                GWSPSSWNWRGRRMCWSFATRLSCAASWPTSLTRQLKSCPT
FT                                SNAPCTQS (in isoform 3).
FT                                /FTId=VSP_021964.
SQ   SEQUENCE   469 AA;  54067 MW;  53777000F163DDE7 CRC64;
     MASPRELTQN PLKKIWMPYS NGRPALHASQ RGVCMTNCPT LIVMVGLPAR GKTYISKKLT
     RYLNWIGVPT REFNVGQYRR DIVKTYKSFE FFLPDNEEGL KIRKQCALAA LSDVRKFLSE
     EGGHVAVFDA TNTTRERRAM IFNFGEQNGY KTFFVESICV DPEVVAANIV QVKLGSPDYV
     NRDSDEATED FMRRIECYEN SYESLDEDLD RDLSYIKIMD VGQSYVVNRV ADHIQSRIVY
     YLMNIHVTPR SIYLCRHGES ELNLKGRIGG DPGLSPRGRE FSKHLAQFIS DQNIKDLKVW
     TSQMKRTIQT AEALSVPYEQ WKVLNEIDAG VCEEMTYEEI QDHYPLEFAL RDQDKYRYRY
     PKGESYEDLV QRLEPVIMEL ERQENVLVIC HQAVMRCLLA YFLDKAAEEL PYLKCPLHTV
     LKLTPVAYGC KVESIFLNVA AVNTHRDRPQ NVDISRPSEE ALVTVPAHQ
//

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