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Database: UniProt/SWISS-PROT
Entry: PFKAP_RAT
LinkDB: PFKAP_RAT
Original site: PFKAP_RAT 
ID   PFKAP_RAT               Reviewed;         788 AA.
AC   P47860; Q5HZX8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   13-FEB-2019, entry version 143.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase, platelet type {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=PFK-P;
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE   AltName: Full=6-phosphofructokinase type C;
DE   AltName: Full=Phosphofructo-1-kinase isozyme C;
DE            Short=PFK-C;
DE   AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN   Name=Pfkp; Synonyms=Pfkc;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-788.
RC   TISSUE=Hypothalamus;
RX   PubMed=8106374;
RA   Gekakis N., Johnson R.C., Jerkins A., Mains R.E., Sul H.S.;
RT   "Structure, distribution, and functional expression of the
RT   phosphofructokinase C isozyme.";
RL   J. Biol. Chem. 269:3348-3355(1994).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-142 AND SER-386,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
CC       to fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose
CC         1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or
CC       fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
CC       citrate. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SUBUNIT: Homo- and heterotetramers (By similarity).
CC       Phosphofructokinase (PFK) enzyme functions as a tetramer composed
CC       of different combinations of 3 types of subunits, called PFKM (M),
CC       PFKL (L) and PFKP (P). The composition of the PFK tetramer differs
CC       according to the tissue type it is present in. The kinetic and
CC       regulatory properties of the tetrameric enzyme are dependent on
CC       the subunit composition, hence can vary across tissues (Probable).
CC       {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- TISSUE SPECIFICITY: Expressed at high level in neuroendocrine
CC       tissues.
CC   -!- PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
CC       clade "E" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17757.1; Type=Frameshift; Positions=27; Evidence={ECO:0000305};
DR   EMBL; BC088847; AAH88847.1; -; mRNA.
DR   EMBL; L25387; AAA17757.1; ALT_FRAME; mRNA.
DR   PIR; A53047; A53047.
DR   RefSeq; NP_996729.1; NM_206847.1.
DR   UniGene; Rn.2278; -.
DR   ProteinModelPortal; P47860; -.
DR   SMR; P47860; -.
DR   BioGrid; 248822; 3.
DR   ComplexPortal; CPX-2054; 6-phosphofructokinase, P4 homotetramer.
DR   IntAct; P47860; 2.
DR   STRING; 10116.ENSRNOP00000023252; -.
DR   iPTMnet; P47860; -.
DR   PhosphoSitePlus; P47860; -.
DR   World-2DPAGE; 0004:P47860; -.
DR   jPOST; P47860; -.
DR   PaxDb; P47860; -.
DR   PRIDE; P47860; -.
DR   GeneID; 60416; -.
DR   KEGG; rno:60416; -.
DR   UCSC; RGD:61893; rat.
DR   CTD; 5214; -.
DR   RGD; 61893; Pfkp.
DR   eggNOG; KOG2440; Eukaryota.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000200154; -.
DR   HOVERGEN; HBG000976; -.
DR   InParanoid; P47860; -.
DR   KO; K00850; -.
DR   OrthoDB; 172878at2759; -.
DR   PhylomeDB; P47860; -.
DR   SABIO-RK; P47860; -.
DR   UniPathway; UPA00109; UER00182.
DR   PRO; PR:P47860; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IDA:RGD.
DR   GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0070095; F:fructose-6-phosphate binding; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:RGD.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:RGD.
DR   GO; GO:0006007; P:glucose catabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IDA:RGD.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:RGD.
DR   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 2.
DR   TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; ATP-binding; Complete proteome;
KW   Cytoplasm; Glycolysis; Glycoprotein; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN         1    788       ATP-dependent 6-phosphofructokinase,
FT                                platelet type.
FT                                /FTId=PRO_0000112027.
FT   NP_BIND      97     98       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   NP_BIND     127    130       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   REGION        1    399       N-terminal catalytic PFK domain 1.
FT   REGION      173    175       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      217    219       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      307    310       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      400    411       Interdomain linker.
FT   REGION      412    788       C-terminal regulatory PFK domain 2.
FT   REGION      538    542       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      583    585       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      671    674       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   METAL       128    128       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING      34     34       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     210    210       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     273    273       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     301    301       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     481    481       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     576    576       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     639    639       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     665    665       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     744    744       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES       2      2       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES       6      6       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES      12     12       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P47859}.
FT   MOD_RES      21     21       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES     142    142       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     386    386       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     395    395       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES     486    486       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES     651    651       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES     688    688       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   CARBOHYD    540    540       O-linked (GlcNAc) serine. {ECO:0000250}.
FT   CONFLICT     35     36       DA -> ES (in Ref. 2; AAA17757).
FT                                {ECO:0000305}.
FT   CONFLICT     51     51       I -> M (in Ref. 2; AAA17757).
FT                                {ECO:0000305}.
FT   CONFLICT     56     56       K -> Q (in Ref. 2; AAA17757).
FT                                {ECO:0000305}.
FT   CONFLICT    111    111       A -> T (in Ref. 2; AAA17757).
FT                                {ECO:0000305}.
FT   CONFLICT    220    220       H -> Y (in Ref. 2; AAA17757).
FT                                {ECO:0000305}.
FT   CONFLICT    600    600       A -> R (in Ref. 2; AAA17757).
FT                                {ECO:0000305}.
FT   CONFLICT    755    755       R -> L (in Ref. 2; AAA17757).
FT                                {ECO:0000305}.
FT   CONFLICT    758    758       M -> S (in Ref. 2; AAA17757).
FT                                {ECO:0000305}.
SQ   SEQUENCE   788 AA;  85720 MW;  16FEB963C3297CA6 CRC64;
     MSDQDSSTSS TSFPKYLEHL SGDGKAIGVL TSGGDAQGMN AAVRAVVRMG IYTGAKVYFI
     YEGYQGMVDG GSNIVEAKWE CVSSILQVGG TIIGSARCQA FRSREGRLKA ACNLVRLGIT
     NLCVIGGDGS LTGANLFRKE WSGLLEELAK NGEIDSDTVK KHAYLNVVGM VGSIDNDFCG
     TDMTIGTDSA LHRIIEVVDA IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP
     ESPPEEGWEE EMCLKLSENR ARKKRLNIII VSEGAIDTQN KPITSEKIKE LVVTNLGFDT
     RVTILGHVQR GGTPSAFDRI LASRMGVEAV LALLEATPET PACVVSLRGN QAVRLPLMEC
     VQMTQDVQKA MDERRFDEAV KLRGRSFEGN LNTYKRLAIK EPDDKIPKSN CNVAIINVGA
     PAAGMNAAVR SAVRVGIAEG HKMFAIYDGF DGLANGQIKE IGWGDVGGWT GQGGSILGTK
     RTLPGKYLEK IAEQMHSKNI NALLIIGGFE AYLGLLELAA ARNKHEAFCV PMVMVPATVS
     NNVPGSDFSI GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA
     DAAYIFEEQF DIRDLQSNVM HLTEKMKTSI QRGLVLRNEN CSVNYTTDFI YQLYSEEGKG
     VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS AKAMEWISAK LKGSHGTGKK FVSDDSICVL
     GIQKRDLLFK PVAELRKATD FEHRIPKQQW WLKLRPIMKI LAKYEASYDM SDVGKLEPVH
     NHGELSAI
//
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