{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9NVE7","secondaryAccessions":["B9DI84","Q53EU3","Q5TA84","Q7RTX3","Q9H3X5"],"uniProtkbId":"PANK4_HUMAN","entryAudit":{"firstPublicDate":"2003-01-17","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2000-10-01","entryVersion":192,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"27322068"}],"value":"4'-phosphopantetheine phosphatase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322068"}],"value":"3.1.3.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"30927326"}],"value":"Inactive pantothenic acid kinase 4"},"shortNames":[{"value":"hPanK4"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:19366"}],"value":"PANK4"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322068"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27322068"}],"value":"Phosphatase which shows a preference for 4'-phosphopantetheine and its oxidatively damaged forms (sulfonate or S-sulfonate), providing strong indirect evidence that the phosphatase activity pre-empts damage in the coenzyme A (CoA) pathway (PubMed:27322068). Hydrolyzing excess 4'-phosphopantetheine could constitute a directed overflow mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or other forms (PubMed:27322068). Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate would forestall their conversion to inactive forms of CoA and acyl carrier protein (PubMed:27322068). May play a role in the physiological regulation of CoA intracellular levels (Probable)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantetheine + H2O = (R)-pantetheine + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:68328"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16753"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:61723"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322068"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:68329"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27322068"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantetheine sulfonate + H2O = (R)-pantetheine sulfonate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:68336"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:177300"},{"database":"ChEBI","id":"CHEBI:177301"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322068"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:68337"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27322068"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phospho-S-sulfopantetheine + H2O = (R)-S-sulfopantetheine + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:68340"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:177302"},{"database":"ChEBI","id":"CHEBI:177303"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322068"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:68341"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27322068"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322068"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}},{"name":"Ni(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322068"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49786"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322068"}],"value":"Phosphatase activity is strongly promoted by several divalent cation ions but it is suggested s that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatases."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322068"}],"value":"Activity is strongly promoted by Co(2+), Ni(2+), Mg(2+) and Mn(2+) (PubMed:27322068). Activity is inhibited by EDTA (PubMed:27322068)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":1920.0,"unit":"uM","substrate":"p-nitrophenylphosphate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322068"}]},{"constant":150.0,"unit":"uM","substrate":"D-pantetheine 4'-phosphate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322068"}]},{"constant":3.9,"unit":"uM","substrate":"D-pantetheine 4'-phosphate-sulfonate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322068"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322068"}],"value":"kcat is 0.17 sec(-1) with p-nitrophenylphosphate as substrate. kcat is 0.71 sec(-1) with D-pantetheine 4'-phosphate as substrate. kcat is 0.09 sec(-1) with D-pantetheine 4'-phosphate-sulfonate as substrate."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q923S8"}],"value":"Homodimer. 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Subfamily II proteins occur only in eukaryotes, in two forms: as a stand-alone unit in plants, and as a C-terminal domain of pantothenate kinases in plants, animals, and chytrid fungi (Probable)"}],"commentType":"DOMAIN"},{"commentType":"DISEASE","disease":{"diseaseId":"Cataract 49","diseaseAccession":"DI-06237","acronym":"CTRCT49","description":"A form of cataract, an opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT49 is an autosomal dominant form characterized by congenital cataract located in the posterior region of the lens. Visual impairment has onset in early childhood.","diseaseCrossReference":{"database":"MIM","id":"619593"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30585370"}]},"note":{"texts":[{"value":"The disease may be caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"In the N-terminal section; belongs to the type II pantothenate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"In the C-terminal section; belongs to the damage-control phosphatase family. Phosphopantetheine phosphatase II subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30927326"}],"value":"Despite belonging to the type II pantothenate kinase family, the pantothenate kinase domain contains a Val residue at position 147 and a Trp residue at position 211 instead of the two conserved active site residues, Glu and Arg. 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