NOCT_XENLA
ID NOCT_XENLA Reviewed; 388 AA.
AC P79942;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Nocturnin {ECO:0000303|PubMed:8962150};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q9UK39};
DE AltName: Full=Carbon catabolite repression 4-like protein;
DE AltName: Full=Rhythmic message 1;
DE Short=RM1;
DE Flags: Precursor;
GN Name=noct {ECO:0000250|UniProtKB:Q9UK39}; Synonyms=ccrn4l;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retinal photoreceptor;
RX PubMed=8962150; DOI=10.1073/pnas.93.25.14884;
RA Green C.B., Besharse J.C.;
RT "Identification of a novel vertebrate circadian clock-regulated gene
RT encoding the protein nocturnin.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14884-14888(1996).
RN [2]
RP FUNCTION, AND COFACTOR.
RX PubMed=12573214; DOI=10.1016/s0960-9822(03)00014-9;
RA Baggs J.E., Green C.B.;
RT "Nocturnin, a deadenylase in Xenopus laevis retina: a mechanism for
RT posttranscriptional control of circadian-related mRNA.";
RL Curr. Biol. 13:189-198(2003).
CC -!- FUNCTION: Phosphatase which catalyzes the conversion of NADP(+) to
CC NAD(+) and of NADPH to NADH (By similarity). Shows a small preference
CC for NADPH over NADP(+) (By similarity). Component of the circadian
CC clock or downstream effector of clock function (PubMed:12573214).
CC Exhibits a high amplitude circadian rhythm with maximal levels in early
CC evening (PubMed:12573214). In constant darkness or constant light, the
CC amplitude of the rhythm decreases (PubMed:12573214).
CC {ECO:0000250|UniProtKB:Q9UK39, ECO:0000269|PubMed:12573214}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) = NAD(+) + phosphate; Xref=Rhea:RHEA:28050,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:Q9UK39};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28051;
CC Evidence={ECO:0000250|UniProtKB:Q9UK39};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADPH = NADH + phosphate; Xref=Rhea:RHEA:60664,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q9UK39};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60665;
CC Evidence={ECO:0000250|UniProtKB:Q9UK39};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12573214};
CC Note=Binds 2 magnesium ions, but the ions are only loosely bound to the
CC protein. {ECO:0000250|UniProtKB:Q9UK39};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35710}. Nucleus
CC {ECO:0000250|UniProtKB:O35710}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O35710}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9UK39}.
CC -!- TISSUE SPECIFICITY: Expressed only in the photoreceptors of the retina.
CC Expression is controlled by the retinal circadian clock.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
CC -!- CAUTION: Was initially shown to have low deadenylase activity that was
CC lost when the metal-binding Glu was mutated (PubMed:12573214). Later
CC studies showed that the purified protein lacked deadenylase activity
CC (By similarity). Was subsequently shown to act as a phosphatase (By
CC similarity). {ECO:0000250|UniProtKB:O35710,
CC ECO:0000250|UniProtKB:Q9UK39, ECO:0000269|PubMed:12573214}.
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DR EMBL; U74761; AAB39495.1; -; mRNA.
DR RefSeq; NP_001079281.1; NM_001085812.1.
DR AlphaFoldDB; P79942; -.
DR SMR; P79942; -.
DR GeneID; 378568; -.
DR KEGG; xla:378568; -.
DR CTD; 378568; -.
DR Xenbase; XB-GENE-6252647; noct.L.
DR OMA; PTGECCS; -.
DR BRENDA; 3.1.13.4; 6725.
DR BRENDA; 3.1.3.108; 6725.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 378568; Expressed in camera-type eye and 16 other tissues.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019178; F:NADP phosphatase activity; ISS:UniProtKB.
DR GO; GO:0102757; F:NADPH phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:InterPro.
DR GO; GO:0032922; P:circadian regulation of gene expression; IEA:InterPro.
DR GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB.
DR CDD; cd09096; Deadenylase_nocturnin; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR034965; Deadenylase_nocturnin.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR040109; Nocturnin.
DR PANTHER; PTHR12121:SF45; PTHR12121:SF45; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 2: Evidence at transcript level;
KW Biological rhythms; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Mitochondrion; Nucleus; Reference proteome; Repressor; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..388
FT /note="Nocturnin"
FT /id="PRO_0000218571"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 176..178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 243..246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 281..283
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
SQ SEQUENCE 388 AA; 43941 MW; 7C9F46F28D9C4E7E CRC64;
MDAQLTYTMG LLEQGYLSAR VCSMGNSTSR LYSALAKTLS SSAAVSQELL EASQHDQSEP
LDPKELLDEC QVALQDRPAR LHRDFFSLRS ESSSQQPRTF RVMQWNILAQ ALGEGKDNFI
MCPMEALKWE ERKYLILEEI LMYQPDVLCL QEVDHYFDTF QPILSRLGYQ CTFLAKPWSP
CLDVEHNNGP DGCALFFLQD RFQLVNSAKI RLSARTLKTN QVAIAETLQC CETGRQLCFA
VTHLKARTGW ERFRLAQGSD LLDNLESITQ GATVPLIICG DFNADPTEEV YKRFASSSLN
LNSAYKLLSE DGESEPPYTT WKIRTTGESC HTLDYIWYSQ HALRVNAALG LPTEEQIGPN
RLPSFNYPSD HLSLVCDFSF NEDPARLL
