PANK3
entrez
79646
canonical
uniprot
Q9H999
canonical
ensembl
ENSG00000120137
resolver
ensp
ENSP00000239231
resolver
enst
ENST00000239231
resolver
genesymbol
PANK3
resolver
hgnc
HGNC:19365
resolver
uniprot
D3DQL1
resolver
uniprot
Q53FJ9
resolver
uniprot
Q7RTX4
resolver
uniprot_entry
PANK3_HUMAN
resolver
uniprot_sec
D3DQL1
resolver
uniprot_sec
Q53FJ9
resolver
uniprot_sec
Q7RTX4
resolver
activity_regulation
ACTIVITY REGULATION: Subject to allosteric regulation, exists in two distinct conformational states, a catalytically incompetent (or open) conformation stabilized by the binding of acetyl(acyl)-CoA, and a catalytically competent (or closed) conformation stabilized by ATP-binding (PubMed:27555321). Inhibited by acetyl-CoA and its thioesters which act as allosteric inhibitors and compete with the ATP-binding site (PubMed:17631502, PubMed:20797618, PubMed:27555321, PubMed:30927326). Inhibited by sulfonylureas and thiazolidinediones (PubMed:20797618). Activated by oleoylethanolamide, palmitoyl-carnitine and oleoyl-carnitine (PubMed:20797618). {ECO:0000269|PubMed:17631502, ECO:0000269|PubMed:20797618, ECO:0000269|PubMed:27555321, ECO:0000269|PubMed:30927326}.
uniprot
proteins
amino_acid_sequence
MKIKDAKKPSFPWFGMDIGGTLVKLSYFEPIDITAEEEQEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLFGRRGNLHFIRFPTQDLPTFIQMGRDKNFSTLQTVLCATGGGAYKFEKDFRTIGNLHLHKLDELDCLVKGLLYIDSVSFNGQAECYYFANASEPERCQKMPFNLDDPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASKGDSTQADKLVRDIYGGDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNNIGSVARMCAVNEKINRVVFVGNFLRVNTLSMKLLAYALDYWSKGQLKALFLEHEGYFGAVGALLGLPNFS
uniprot
proteins
ec_number
2.7.1.33
uniprot
proteins
function
FUNCTION: Catalyzes the phosphorylation of pantothenate to generate 4'-phosphopantothenate in the first and rate-determining step of coenzyme A (CoA) synthesis. {ECO:0000269|PubMed:17631502, ECO:0000269|PubMed:20797618, ECO:0000269|PubMed:27555321, ECO:0000269|PubMed:30927326}.
uniprot
proteins
mass_dalton
41094
uniprot
proteins
mutagenesis
MUTAGEN 19; /note="G->V: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:27555321"; MUTAGEN 138; /note="E->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:27555321"; MUTAGEN 138; /note="E->V: Prevents acetyl-CoA production."; /evidence="ECO:0000269|PubMed:30927326"; MUTAGEN 195; /note="S->V: Retains 30% of wild-type activity. Refractory to inhibition by acetyl-CoA. Exhibits a 10-fold increase in the Km for pantothenate."; /evidence="ECO:0000269|PubMed:20797618"; MUTAGEN 207; /note="R->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:20797618"; MUTAGEN 207; /note="R->W: Increases affinity for ATP and decreases affinity for acetyl-CoA. Increases acetyl-CoA production."; /evidence="ECO:0000269|PubMed:30927326"; MUTAGEN 267; /note="A->F: Loss of catalytic activity but can bind ATP normally."; /evidence="ECO:0000269|PubMed:20797618"; MUTAGEN 269; /note="A->F: Loss of catalytic activity but can bind ATP normally."; /evidence="ECO:0000269|PubMed:20797618
uniprot
proteins
pathway_participation
PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. {ECO:0000269|PubMed:17631502, ECO:0000269|PubMed:20797618, ECO:0000269|PubMed:27555321, ECO:0000305|PubMed:30927326}.
uniprot
proteins
protein_family
Type II pantothenate kinase family
uniprot
proteins
pubmed
11479594
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17631502
uniprot
proteins
pubmed
20797618
uniprot
proteins
pubmed
23152917
uniprot
proteins
pubmed
27555321
uniprot
proteins
pubmed
30927326
uniprot
proteins
sequence_length
370
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23152917, ECO:0000305}.
uniprot
proteins