Q80YV4 · PANK4_MOUSE
- Protein4'-phosphopantetheine phosphatase
- GenePank4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids820 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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. Hydrolyzing excess 4'-phosphopantetheine could constitute a directed overflow mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or other forms. Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate would forestall their conversion to inactive forms of CoA and acyl carrier protein. May play a role in the physiological regulation of CoA intracellular levels.
Catalytic activity
- (R)-4'-phosphopantetheine + H2O = (R)-pantetheine + phosphateThis reaction proceeds in the forward direction.
- (R)-4'-phosphopantetheine sulfonate + H2O = (R)-pantetheine sulfonate + phosphateThis reaction proceeds in the forward direction.
- (R)-4'-phospho-S-sulfopantetheine + H2O = (R)-S-sulfopantetheine + phosphateThis reaction proceeds in the forward direction.
Cofactor
Ni2+ (UniProtKB | Rhea| CHEBI:49786 )
Activity regulation
Activity is strongly promoted by Co2+, Ni2+, Mg2+ and Mn2+. Activity is inhibited by EDTA.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 196 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 199 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 623 | Mn2+ (UniProtKB | ChEBI); catalytic; for phosphatase activity | ||||
Sequence: D | ||||||
Binding site | 624 | Mn2+ (UniProtKB | ChEBI); catalytic; for phosphatase activity | ||||
Sequence: N | ||||||
Binding site | 659 | Mn2+ (UniProtKB | ChEBI); catalytic; for phosphatase activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular space | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | pantothenate kinase activity | |
Molecular Function | phosphatase activity | |
Biological Process | coenzyme A biosynthetic process | |
Biological Process | coenzyme A catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4'-phosphopantetheine phosphatase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ80YV4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Knockout mice have a body weight and a lifespan similar to wild-type animals. About 10% of the animals start developing cataract at 2 months. At 15 months, 50% homozygous animals are affected. Heterozygous animals develop cataract later, with 10% animals affected at 9 months and 25% at 15.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 36 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000249248 | 2-820 | 4'-phosphopantetheine phosphatase | |||
Sequence: AERGASGGGSGGDSLDKSITLPPDEIFRNLENAKRFAIDIGGSLTKLAYYSTVQHKVAKVRSFDHPGKDVEQDHEPPYEISVQEEITARLHFIKFENTYMEACLDFIRDHLVNTETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFMYQKDSDPEFRFQTNHPNIFPYLLVNIGSGVSIVKVETEDRFEWIGGSSIGGGTFWGLGALLTKTKKFDELLQLASRGRHANVDMLVQDIYGGAHQTLGLSGNLIASSFGKSATADREFSKEDMAKSLLHMISNDIGQLACLYAKLHGLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLGAIGAFLKGAEQDNPNQYSWGENYAASSGLMSTSPELCPTQRARSGTFDLLEMDRLERPLVNLPLLLDPSSYVPDTVDLTDDALARQYWLTCFEEALDGVVKRAVASQPESMDAVERAEKFRQKYWGKLQTLRHQPFAYGTLTVRSLLDTREHCLNEFNFPDPYSKVKQKENGLALKCFQSVTRSLDSLGWEERQLALVKGLLAGNVFDWGAKAVSDVLESDPQFGFEEAKRKLQERPWLVDSYTKWLQRLKGPPHKCALIFADNSGIDIILGVFPFVRELLFRGTEVILACNSGPALNDVTYSESLIVAERIAAMDPIICTALREDRLLLVQTGSSSPCLDLSLCTSRTTTCMVLPFAMWVLWTKLKSLVEKCLSPLSILLACSVLSAKSRLDKGLAVLVRERGADLVVIEGMGRAIHTNYHALLRCESLKLAVVKNAWLAERLGGQLFSVIFKYEVPTK | ||||||
Modified residue | 320 | 3'-nitrotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 393 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 404 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 406 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in liver, kidney, brain cortex and eye lens (at protein level).
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MAERGASGGGSGGDSLDKSI | ||||||
Region | 2-402 | Pantothenate kinase | ||||
Sequence: AERGASGGGSGGDSLDKSITLPPDEIFRNLENAKRFAIDIGGSLTKLAYYSTVQHKVAKVRSFDHPGKDVEQDHEPPYEISVQEEITARLHFIKFENTYMEACLDFIRDHLVNTETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFMYQKDSDPEFRFQTNHPNIFPYLLVNIGSGVSIVKVETEDRFEWIGGSSIGGGTFWGLGALLTKTKKFDELLQLASRGRHANVDMLVQDIYGGAHQTLGLSGNLIASSFGKSATADREFSKEDMAKSLLHMISNDIGQLACLYAKLHGLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLGAIGAFLKGAEQDNPNQYSWGENYAASSGLMSTSPELCPTQRA | ||||||
Region | 403-820 | 4'-phosphopantetheine phosphatase | ||||
Sequence: RSGTFDLLEMDRLERPLVNLPLLLDPSSYVPDTVDLTDDALARQYWLTCFEEALDGVVKRAVASQPESMDAVERAEKFRQKYWGKLQTLRHQPFAYGTLTVRSLLDTREHCLNEFNFPDPYSKVKQKENGLALKCFQSVTRSLDSLGWEERQLALVKGLLAGNVFDWGAKAVSDVLESDPQFGFEEAKRKLQERPWLVDSYTKWLQRLKGPPHKCALIFADNSGIDIILGVFPFVRELLFRGTEVILACNSGPALNDVTYSESLIVAERIAAMDPIICTALREDRLLLVQTGSSSPCLDLSLCTSRTTTCMVLPFAMWVLWTKLKSLVEKCLSPLSILLACSVLSAKSRLDKGLAVLVRERGADLVVIEGMGRAIHTNYHALLRCESLKLAVVKNAWLAERLGGQLFSVIFKYEVPTK | ||||||
Motif | 771-775 | Subfamily II EGMGR motif | ||||
Sequence: EGMGR |
Domain
Subfamily II proteins have an EGMGR motif about 50 residues from the C-terminus (By similarity).
This motif lies near the metal-binding residues in the putative substrate-binding cleft 2 (By similarity).
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 (By similarity).
This motif lies near the metal-binding residues in the putative substrate-binding cleft 2 (By similarity).
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 (By similarity).
Sequence similarities
In the N-terminal section; belongs to the type II pantothenate kinase family.
In the C-terminal section; belongs to the damage-control phosphatase family. Phosphopantetheine phosphatase II subfamily.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q80YV4-1
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.
- Name1
- Length820
- Mass (Da)91,522
- Last updated2006-09-05 v2
- Checksum0D88CA48A8B87D3A
Q80YV4-2
- Name2
- Differences from canonical
- 703-749: Missing
Q80YV4-3
- Name3
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F7B6K4 | F7B6K4_MOUSE | Pank4 | 473 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 81 | in Ref. 3; AAH50089 | ||||
Sequence: I → T | ||||||
Sequence conflict | 146 | in Ref. 3; AAH50089 | ||||
Sequence: D → G | ||||||
Sequence conflict | 173 | in Ref. 4; DAA00010 | ||||
Sequence: S → A | ||||||
Sequence conflict | 205 | in Ref. 3; AAH50089 | ||||
Sequence: T → I | ||||||
Sequence conflict | 243 | in Ref. 3; AAH50089 | ||||
Sequence: S → F | ||||||
Sequence conflict | 351 | in Ref. 3; AAH50089 | ||||
Sequence: L → P | ||||||
Alternative sequence | VSP_020379 | 373-374 | in isoform 3 | |||
Sequence: NP → SE | ||||||
Alternative sequence | VSP_020380 | 375-820 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 479 | in Ref. 1; BAC34450 | ||||
Sequence: K → E | ||||||
Sequence conflict | 635 | in Ref. 1; BAC34450 | ||||
Sequence: P → T | ||||||
Alternative sequence | VSP_020381 | 703-749 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK050894 EMBL· GenBank· DDBJ | BAC34450.1 EMBL· GenBank· DDBJ | mRNA | ||
BX004788 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC050089 EMBL· GenBank· DDBJ | AAH50089.1 EMBL· GenBank· DDBJ | mRNA | ||
BK000016 EMBL· GenBank· DDBJ | DAA00010.1 EMBL· GenBank· DDBJ | mRNA |