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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   03-AUG-2022, entry version 157.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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 project:
RT   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; DOI=10.1016/s0021-9258(17)41869-2;
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, AND
RP   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., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC       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 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC         ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC       2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC       {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). Phosphofructokinase
CC       (PFK) enzyme functions as a tetramer composed of different combinations
CC       of 3 types of subunits, called PFKM (M), PFKL (L) and PFKP (P). The
CC       composition of the PFK tetramer differs according to the tissue type it
CC       is present in. The kinetic and regulatory properties of the tetrameric
CC       enzyme are dependent on the subunit composition, hence can vary across
CC       tissues (Probable). Interacts with ATG4B; promoting phosphorylation of
CC       ATG4B. {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 tissues.
CC   -!- PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}.
CC   -!- PTM: Phosphorylation at Ser-386 promotes interaction with ATG4B.
CC       {ECO:0000250|UniProtKB:Q01813}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E'
CC       sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17757.1; Type=Frameshift; Evidence={ECO:0000305};
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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   AlphaFoldDB; P47860; -.
DR   SMR; P47860; -.
DR   BioGRID; 248822; 4.
DR   ComplexPortal; CPX-2054; 6-phosphofructokinase, P4 homotetramer.
DR   IntAct; P47860; 4.
DR   MINT; P47860; -.
DR   STRING; 10116.ENSRNOP00000023252; -.
DR   GlyGen; P47860; 1 site.
DR   iPTMnet; P47860; -.
DR   PhosphoSitePlus; P47860; -.
DR   World-2DPAGE; 0004:P47860; -.
DR   jPOST; P47860; -.
DR   PaxDb; P47860; -.
DR   PRIDE; P47860; -.
DR   Ensembl; ENSRNOT00000023252; ENSRNOP00000023252; ENSRNOG00000017163.
DR   GeneID; 60416; -.
DR   KEGG; rno:60416; -.
DR   UCSC; RGD:61893; rat.
DR   CTD; 5214; -.
DR   RGD; 61893; Pfkp.
DR   eggNOG; KOG2440; Eukaryota.
DR   GeneTree; ENSGT00940000155002; -.
DR   InParanoid; P47860; -.
DR   OrthoDB; 172878at2759; -.
DR   PhylomeDB; P47860; -.
DR   Reactome; R-RNO-70171; Glycolysis.
DR   SABIO-RK; P47860; -.
DR   UniPathway; UPA00109; UER00182.
DR   PRO; PR:P47860; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0016020; C:membrane; 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:0042802; F:identical protein binding; IPI: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:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
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:0006096; P:glycolytic process; IDA:RGD.
DR   CDD; cd00764; Eukaryotic_PFK; 1.
DR   Gene3D; 3.40.50.460; -; 2.
DR   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR041914; PFK_vert-type.
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; Cytoplasm; Glycolysis;
KW   Glycoprotein; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..788
FT                   /note="ATP-dependent 6-phosphofructokinase, platelet type"
FT                   /id="PRO_0000112027"
FT   REGION          1..399
FT                   /note="N-terminal catalytic PFK domain 1"
FT   REGION          400..411
FT                   /note="Interdomain linker"
FT   REGION          412..788
FT                   /note="C-terminal regulatory PFK domain 2"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         97..98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         127..130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         173..175
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         210
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         217..219
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         307..310
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         481
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         538..542
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         576
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         583..585
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         639
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         665
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         671..674
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         744
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47859"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         386
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         395
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   MOD_RES         486
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   MOD_RES         651
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   MOD_RES         688
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   CARBOHYD        540
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        35..36
FT                   /note="DA -> ES (in Ref. 2; AAA17757)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="I -> M (in Ref. 2; AAA17757)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        56
FT                   /note="K -> Q (in Ref. 2; AAA17757)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="A -> T (in Ref. 2; AAA17757)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        220
FT                   /note="H -> Y (in Ref. 2; AAA17757)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        600
FT                   /note="A -> R (in Ref. 2; AAA17757)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        755
FT                   /note="R -> L (in Ref. 2; AAA17757)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        758
FT                   /note="M -> S (in Ref. 2; AAA17757)"
FT                   /evidence="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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