A8JQX3 · NOCT_DROME
- ProteinNocturnin
- Genecu
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids642 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Phosphatase which catalyzes the conversion of NADP+ to NAD+ and of NADPH to NADH (PubMed:31147539).
Shows a small preference for NADPH over NADP+ (PubMed:31147539).
Because of its association with the CCR4-NOT complex, has a role in mRNA deadenylation and decay (PubMed:20504953).
Required at the pupal stage for proper wing morphogenesis after eclosion (PubMed:19581445).
Shows a small preference for NADPH over NADP+ (PubMed:31147539).
Because of its association with the CCR4-NOT complex, has a role in mRNA deadenylation and decay (PubMed:20504953).
Required at the pupal stage for proper wing morphogenesis after eclosion (PubMed:19581445).
Isoform C
Doesn't have a role in light-mediated behavioral response.
Isoform D
In dorsal neurons, contributes to the light-mediated behavioral response.
Isoform E
Doesn't have a role in light-mediated behavioral response.
Catalytic activity
- H2O + NADP+ = NAD+ + phosphateThis reaction proceeds in the forward direction.
- H2O + NADPH = NADH + phosphateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 magnesium ions, but the ions are only loosely bound to the protein.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | mitochondrion | |
Molecular Function | 3'-5'-RNA exonuclease activity | |
Molecular Function | metal ion binding | |
Molecular Function | NADP phosphatase activity | |
Molecular Function | NADPH phosphatase activity | |
Biological Process | locomotor rhythm | |
Biological Process | NADP metabolic process | |
Biological Process | response to light stimulus |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNocturnin
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionA8JQX3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Viable and fertile with upward bent (curled) wings and proximally crossed posterior scutellar bristles (PubMed:19581445).
RNAi-mediated knockdown has a similar phenotype (PubMed:19581445).
RNAi-mediated knockdown in the wing, nervous system, ring gland, muscles, fat body, tracheal system, salivary gland, or gut has no impact on wing morphogenesis (PubMed:19581445).
RNAi-mediated knockdown has a similar phenotype (PubMed:19581445).
RNAi-mediated knockdown in the wing, nervous system, ring gland, muscles, fat body, tracheal system, salivary gland, or gut has no impact on wing morphogenesis (PubMed:19581445).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 363 | Disrupts catalytic activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 491 | Decreases mRNA deadelynation and decay; when associated with A-493. | ||||
Sequence: D → A | ||||||
Mutagenesis | 493 | Decreases mRNA deadelynation and decay; when associated with A-491. | ||||
Sequence: N → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000448000 | 1-642 | Nocturnin | |||
Sequence: MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQSAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAARKLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLVRMGSFNSAPKINNVDSQDDGLVLPSGLSTPALLQHVQQLRGGGIEQPSLLTRGFLKPLLADEDVADGLRCLKLNSVSRVCSAPVEGDDIRLLQWNILSQTLGQHNDGFVRCPEEALTWEHRKYLIVQEILQNQPDVICLQEVDHFKFLQTVLGSQNYAGIFFPKPDSPCLYIEQNNGPDGCAIFYKRDKLQLQGYDTRILEVWRVQSNQVAIAARLRMRSSGREFCVATTHLKARHGALLAKLRNEQGRDLIRFVKQFAGDTPLLLCGDFNAEPVEPIYATILGCDLLRLGSAYADVKLDREEILHPNADVGEFVAKSMKREPPYTTWKIREEGEECHTIDYVFYTPDRLKIKNCLDFPAGEQIGKNRTPSFQYPSDHFSLVCDFELLPPTENGKESGSGSGSDGENETEVEGSKHGSIQ |
Proteomic databases
Expression
Tissue specificity
Expressed in the head, in the dorsal neurons DN3, a subgroup of clock neurons (at protein level) (PubMed:19966839).
Ubiquitously expressed in both males and females (PubMed:19581445).
Ubiquitously expressed in both males and females (PubMed:19581445).
Induction
Nutritional conditions, such as food deprivation, and higher temperature during the larval stage increase protein expression in the adult flies (PubMed:19581445, Ref.7). Levels of expression at the pupal stage are phenocritical for the cu-dependent wing phenotype (PubMed:19581445).
In the dorsal neurons DN3, a subgroup of clock neurons, accumulates rhythmically with a peak around ZT12 (PubMed:19966839).
In the dorsal neurons DN3, a subgroup of clock neurons, accumulates rhythmically with a peak around ZT12 (PubMed:19966839).
Developmental stage
Expressed at every stage (PubMed:19581445).
Expressed in the embryonic salivary glands, the distal part of the proventriculus and the ring gland as well as weak expression in the midgut (PubMed:19581445).
At third instar larval stage, expressed at the proventricular and ring gland (PubMed:19581445).
No transcript detected in the larval central brain, in the imaginal disks, the salivary glands, or in the fat body (PubMed:19581445).
Expressed in the embryonic salivary glands, the distal part of the proventriculus and the ring gland as well as weak expression in the midgut (PubMed:19581445).
At third instar larval stage, expressed at the proventricular and ring gland (PubMed:19581445).
No transcript detected in the larval central brain, in the imaginal disks, the salivary glands, or in the fat body (PubMed:19581445).
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 50-87 | Disordered | ||||
Sequence: LEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLA | ||||||
Compositional bias | 68-87 | Basic and acidic residues | ||||
Sequence: SPNEEDYKPPNHHEDDGKLA | ||||||
Region | 611-642 | Disordered | ||||
Sequence: PPTENGKESGSGSGSDGENETEVEGSKHGSIQ |
Sequence similarities
Belongs to the CCR4/nocturin family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 6 isoforms produced by Alternative splicing.
A8JQX3-1
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.
- NameD
- Length642
- Mass (Da)71,880
- Last updated2007-12-04 v1
- Checksum4AF5B5856E82C41B
A8JQX3-2
- NameF
- Differences from canonical
- 1-223: MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQSAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAARKLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLVR → MKLISTVVYLLVAFYKFAKKLL
A8JQX3-3
- NameE
- Differences from canonical
- 1-222: MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQSAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAARKLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLV → MEFLMKTSRLIVTSKTFARRVAVPIP
A8JQX3-4
- NameC
- Differences from canonical
- 1-222: MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQSAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAARKLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLV → MEPAVPIKRANKAPCKNDRKAYLQKVMLT
A8JQX3-5
- NameH
- Differences from canonical
- 1-223: Missing
A8JQX3-6
- NameG
- Differences from canonical
- 1-223: MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQSAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAARKLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLVR → MEFLMKTSRLIVTSKTFARRVAVPIPSKVKMGQFYTSQRHSHSLFIFSIILRKILYRKPNAL
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_060327 | 1-222 | in isoform C | |||
Sequence: MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQSAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAARKLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLV → MEPAVPIKRANKAPCKNDRKAYLQKVMLT | ||||||
Alternative sequence | VSP_060328 | 1-222 | in isoform E | |||
Sequence: MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQSAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAARKLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLV → MEFLMKTSRLIVTSKTFARRVAVPIP | ||||||
Alternative sequence | VSP_060324 | 1-223 | in isoform F | |||
Sequence: MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQSAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAARKLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLVR → MKLISTVVYLLVAFYKFAKKLL | ||||||
Alternative sequence | VSP_060325 | 1-223 | in isoform G | |||
Sequence: MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQSAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAARKLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLVR → MEFLMKTSRLIVTSKTFARRVAVPIPSKVKMGQFYTSQRHSHSLFIFSIILRKILYRKPNAL | ||||||
Alternative sequence | VSP_060326 | 1-223 | in isoform H | |||
Sequence: Missing | ||||||
Compositional bias | 68-87 | Basic and acidic residues | ||||
Sequence: SPNEEDYKPPNHHEDDGKLA | ||||||
Sequence conflict | 579 | in Ref. 5; AAT94521 | ||||
Sequence: D → Y |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY043266 EMBL· GenBank· DDBJ | AAK85704.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014297 EMBL· GenBank· DDBJ | AAF54600.3 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAF54601.3 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | ABW08639.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | ABW08640.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | ABW08641.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AGB95853.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT023825 EMBL· GenBank· DDBJ | AAZ86746.1 EMBL· GenBank· DDBJ | mRNA | ||
BT015292 EMBL· GenBank· DDBJ | AAT94521.1 EMBL· GenBank· DDBJ | mRNA | ||
BT025859 EMBL· GenBank· DDBJ | ABF85759.1 EMBL· GenBank· DDBJ | mRNA | ||
BT070224 EMBL· GenBank· DDBJ | ACN38810.1 EMBL· GenBank· DDBJ | mRNA |