Q9WUA3 (K6PP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
6-phosphofructokinase type C
EC=2.7.1.11

Alternative name(s):
Phosphofructo-1-kinase isozyme C
Short name=PFK-C
Phosphofructokinase 1
Phosphohexokinase

Gene names

Name:	Pfkp
Synonyms:	Pfkc

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	784 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the third step of glycolysis, the phosphorylation of fructose-6-phosphate (F6P) by ATP to generate fructose-1,6-bisphosphate (FBP) and ADP.
Catalytic activity	ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.
Cofactor	Magnesium By similarity.
Enzyme regulation	Allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate By similarity.
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Tissue specificity	Expression is constant during tumor growth and markedly decreases when cell proliferation stops. Ref.1
Post-translational modification	GlcNAcylation decreases enzyme activity By similarity.
Sequence similarities	Belongs to the phosphofructokinase family. Two domains subfamily.

Ontologies

Keywords
Biological process	Glycolysis
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fructose 6-phosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysis Inferred from sequence or structural similarity Ref.1. Source: MGI
Cellular_component	6-phosphofructokinase complex Inferred from sequence or structural similarity Ref.1. Source: MGI
Molecular_function	6-phosphofructokinase activity Inferred from sequence or structural similarity. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9WUA3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9WUA3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     457-496: IKEIGWADVG...LEKIAEQMHS → VSLPGVLGML...LVVGLYQILI
     497-784: Missing.

Note: May be due to intron retention. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 784	784	6-phosphofructokinase type C		PRO_0000112025
Regions
	Nucleotide binding	43 – 47	5	ATP By similarity
	Nucleotide binding	201 – 205	5	ATP By similarity
	Nucleotide binding	218 – 234	17	ATP By similarity
Sites
	Active site	174	1	Proton acceptor By similarity
	Metal binding	232	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	209	1	Substrate By similarity
	Binding site	300	1	Substrate By similarity
	Binding site	306	1	Substrate By similarity
	Binding site	309	1	Substrate By similarity
Amino acid modifications
	Modified residue	394	1	N6-acetyllysine By similarity
	Modified residue	485	1	N6-acetyllysine By similarity
	Modified residue	650	1	Phosphotyrosine Ref.7
	Modified residue	687	1	N6-acetyllysine By similarity
	Glycosylation	539	1	O-linked (GlcNAc...) By similarity
Natural variations
	Alternative sequence	457 – 496	40	IKEIG…EQMHS → VSLPGVLGMLKCYCIWGGHP PLTAPTKSRFLVVGLYQILI in isoform 2.		VSP_016664
	Alternative sequence	497 – 784	288	Missing in isoform 2.		VSP_016665
	Natural variant	104	1	E → V in strain: NOD. Ref.4
	Natural variant	145	1	E → G in strain: C57BL/6J. Ref.4
	Natural variant	180	1	T → P in strain: C57BL/6. Ref.2
	Natural variant	261	1	R → Q in strain: LG/J and NOD. Ref.3 Ref.4
	Natural variant	292	1	V → M in strain: LG/J and NOD. Ref.3 Ref.4
	Natural variant	402	1	D → E in strain: C57BL/6J. Ref.4
	Natural variant	679	1	P → S in strain: C57BL/6J. Ref.4
	Natural variant	694	1	E → D in strain: LG/J and NOD. Ref.3 Ref.4
	Natural variant	696	1	I → F in strain: NOD. Ref.4
	Natural variant	777	1	S → P in strain: LG/J and NOD. Ref.3 Ref.4
	Natural variant	782	1	E → G in strain: LG/J and NOD. Ref.3 Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: E9C5AAABF26FCA65	FASTA	784	85,455
	10 20 30 40 50 60 MSDLDSSSSS AYPKYLEHLS GDGKAIGVLT SGGDAQGMNA AVRAVVRMGI YTGAKVYFIY 70 80 90 100 110 120 EGYQGLVDGG SNIVEAKWDC VSSILQVGGT IIGSARCKAF RSREGRLKAA CNLARLGITN 130 140 150 160 170 180 LCVIGGDGSL TGANLFRKEW SGLLEELARN GDIDNDTVQK YSYLNVVGMV GSIDNDFCGT 190 200 210 220 230 240 DMTIGTDSAL HRIIEVVDAI MTTAQSHQRT FVLEVMGRHC GYLALVSALT CGADWVFLPE 250 260 270 280 290 300 SPPEEDWEEN MCLKLSENRA RKKRLNIIIV SEGAIDMQNK PITSEKIKEL VVKNLGFDTR 310 320 330 340 350 360 VTILGHVQRG GTPSAFDRIL ASRMGVEAVI ALLEATPETP ACVVSLRGNQ AVRLPLMECV 370 380 390 400 410 420 QMTQDVQKAM DERRFKEAVK LRGRRFEGNL NTYKRLAIKL PDEKIVKSNC NVAVINVGAP 430 440 450 460 470 480 AAGMNAAVRS AVRVGIADGH KMFAIYDGFE GFANGQIKEI GWADVGGWTG QGGSILGTKR 490 500 510 520 530 540 TLPGKYLEKI AEQMHSHSIN ALLIIGGFEA YLGLLELAAA REKHEAFCVP MVMVPATVSN 550 560 570 580 590 600 NVPGSDFSIG ADTALNTITD TCDRIKQSAS GTKRRVFIIE TMGGYCGYLA NMGALAAGAD 610 620 630 640 650 660 AAYIFEEPFD IGDLQSNVVH LTEKMKTSIQ RGLVLRNESC SVNYTTDFIY QLYSEEGKGV 670 680 690 700 710 720 FDCRKNVLGH MQQGGAPSPF DRNFGTKISA KAMEWISAKL KGSQGTGKKF VSDDSICVLG 730 740 750 760 770 780 ICKRDLLFQP VAELKKVTDF EHRIPKEQWW LKLRPIMKIL AKYEASYDMS DSGKLESLQH HEEL
	Isoform 2 [UniParc]. Checksum: 22E3CB5080FD748C	FASTA	496	53,682
	10 20 30 40 50 60 MSDLDSSSSS AYPKYLEHLS GDGKAIGVLT SGGDAQGMNA AVRAVVRMGI YTGAKVYFIY 70 80 90 100 110 120 EGYQGLVDGG SNIVEAKWDC VSSILQVGGT IIGSARCKAF RSREGRLKAA CNLARLGITN 130 140 150 160 170 180 LCVIGGDGSL TGANLFRKEW SGLLEELARN GDIDNDTVQK YSYLNVVGMV GSIDNDFCGT 190 200 210 220 230 240 DMTIGTDSAL HRIIEVVDAI MTTAQSHQRT FVLEVMGRHC GYLALVSALT CGADWVFLPE 250 260 270 280 290 300 SPPEEDWEEN MCLKLSENRA RKKRLNIIIV SEGAIDMQNK PITSEKIKEL VVKNLGFDTR 310 320 330 340 350 360 VTILGHVQRG GTPSAFDRIL ASRMGVEAVI ALLEATPETP ACVVSLRGNQ AVRLPLMECV 370 380 390 400 410 420 QMTQDVQKAM DERRFKEAVK LRGRRFEGNL NTYKRLAIKL PDEKIVKSNC NVAVINVGAP 430 440 450 460 470 480 AAGMNAAVRS AVRVGIADGH KMFAIYDGFE GFANGQVSLP GVLGMLKCYC IWGGHPPLTA 490 PTKSRFLVVG LYQILI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phosphofructokinase C isozyme from ascites tumor cells: cloning, expression, and properties." Sanchez-Martinez C., Estevez A.M., Aragon J.J. Biochem. Biophys. Res. Commun. 271:635-640(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Ascitic tumor.
[2]	"Genomic organization, 5'flanking region and tissue-specific expression of mouse phosphofructokinase C gene." Gunasekera D., Kemp R.G. Gene 260:103-112(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT PRO-180. Strain: C57BL/6. Tissue: Brain.
[3]	"Fine-mapping gene-by-diet interactions on chromosome 13 in a LG/J x SM/J murine model of obesity." Ehrich T.H., Hrbek T., Kenney-Hunt J.P., Pletscher L.S., Wang B., Semenkovich C.F., Cheverud J.M. Diabetes 54:1863-1872(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-261; MET-292; ASP-694; PRO-777 AND GLY-782. Strain: LG/J and SM/J.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS VAL-104; GLY-145; GLN-261; MET-292; GLU-402; SER-679; ASP-694; PHE-696; PRO-777 AND GLY-782. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Hippocampus, Kidney and Olfactory bulb.
[5]	"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)." Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: FVB/N-3. Tissue: Mammary gland.
[7]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-650, MASS SPECTROMETRY. Tissue: Mast cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y19008 mRNA. Translation: CAB64347.1. AF123533 mRNA. Translation: AAD23571.1. AF249893 , AF250369, AF250370, AF250371, AF250372, AF251021 Genomic DNA. Translation: AAF75700.1. AY779275 mRNA. Translation: AAX11357.1. AY779276 mRNA. Translation: AAX11358.1. AK049841 mRNA. Translation: BAC33949.1. AK078254 mRNA. Translation: BAC37195.1. AK152670 mRNA. Translation: BAE31405.1. AK154125 mRNA. Translation: BAE32390.1. AK165422 mRNA. Translation: BAE38177.1. AK165425 mRNA. Translation: BAE38180.1. AK170624 mRNA. Translation: BAE41918.1. AK171062 mRNA. Translation: BAE42221.1. CT010268 mRNA. Translation: CAJ18476.1. BC006926 mRNA. Translation: AAH06926.1.
IPI	IPI00124444. IPI00661241.
RefSeq	NP_062677.1. NM_019703.3.
UniGene	Mm.273874.
3D structure databases
ProteinModelPortal	Q9WUA3.
SMR	Q9WUA3. Positions 21-764.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9WUA3. 4 interactions.
STRING	10090.ENSMUSP00000117030.
PTM databases
PhosphoSite	Q9WUA3.
Proteomic databases
PaxDb	Q9WUA3.
PRIDE	Q9WUA3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000138703; ENSMUSP00000117030; ENSMUSG00000021196.
GeneID	56421.
KEGG	mmu:56421.
UCSC	uc007pjz.1. mouse. uc007pkc.1. mouse.
Organism-specific databases
CTD	5214.
MGI	MGI:1891833. Pfkp.
Phylogenomic databases
eggNOG	COG0205.
GeneTree	ENSGT00390000013209.
HOVERGEN	HBG000976.
InParanoid	Q9WUA3.
KO	K00850.
OMA	YLANMGA.
OrthoDB	EOG4NS39Z.
Enzyme and pathway databases
BRENDA	2.7.1.11. 3474.
SABIO-RK	Q9WUA3.
UniPathway	UPA00109; UER00182.
Gene expression databases
ArrayExpress	Q9WUA3.
Bgee	Q9WUA3.
CleanEx	MM_PFKP.
Genevestigator	Q9WUA3.
GermOnline	ENSMUSG00000021196. Mus musculus.
Family and domain databases
InterPro	IPR009161. 6-phosphofructokinase_euk. IPR022953. Phosphofructokinase. IPR015912. Phosphofructokinase_CS. IPR000023. Phosphofructokinase_dom. [Graphical view]
Pfam	PF00365. PFK. 2 hits. [Graphical view]
PIRSF	PIRSF000533. ATP_PFK_euk. 1 hit.
PRINTS	PR00476. PHFRCTKINASE.
SUPFAM	SSF53784. Ppfruckinase. 2 hits.
TIGRFAMs	TIGR02478. 6PF1K_euk. 1 hit.
PROSITE	PS00433. PHOSPHOFRUCTOKINASE. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	312572.
SOURCE	Search...

Entry information

Entry name

K6PP_MOUSE

Accession

Primary (citable) accession number: Q9WUA3
Secondary accession number(s): Q3TNA9 , Q3U4P1, Q3U7G4, Q4KUG1, Q543K8, Q8C5I6, Q9JI86

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	November 1, 1999
Last modified:	April 3, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program